Product Search for novus: Novus Biologicals

NB100-1028

AIF-1/Iba1 Antibody

(21 Reviews)

(395 Publications)

0.1 mg

NB100-1028

GM1 effects on brain microglia in vivo, after peripheral administration of LPS. Immunoblot in whole brain lysates and densitometric analysis show LPS-dependent increase in AIF-1/Iba1 expression. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/34991625/) licensed under a CC-BY license.

Reactive microglia (green) in peritumoral area of IC injected human glioblastoma cells in mouse brain. NeuN (red), DAPI (blue). Antibody at 1:250. IHC image submitted by a verified customer review.

AIF-1/Iba1 in canine brain. Primary antibody used at 1 ug/mL and incubated with tissue for 30 minutes at room temperature. IHC-P image submitted by a verified customer review.

Staining in mouse brain using AIF-1/Iba1 Antibody. IHC-P image submitted by a verified customer review.

Brown arrow= AIF-1/Iba1 positive cells, Green arrow= mTOR positive cells, Black arrow= mTOR and AIF-1/Iba1 positive cells. IHC-P image submitted by a verified customer review.

Staining in rat hippocampus using AIF-1/Iba1 Antibody. IHC-Fr image submitted by a verified customer review.

Feline optic nerve microglia were immunolabeled with AIF-1/Iba1 Antibody (green), DAPI (blue). Imaging was performed using an epifluorescence microscope. IHC-Fr image submitted by a verified customer review.

Mouse dorsal root ganglia. AIF-1/Iba1 expression in reactive macrophages. Maximum intensity z-projection from 3D images. IHC image submitted by a verified customer review.

Staining in mouse brain using AIF-1/Iba1 Antibody. IHC image submitted by a verified customer review.

Analysis of LPS injected mouse brain tissue, 20 um thickness, frozen. Primary antibody dilution, 1:200. Secondary antibody CY3. Mounted with DAPI mount. Image from verified customer review.

AIF-1/Iba1 staining of AD mouse model (hippocampus). Image from verified customer review.

Negative Control showing staining of paraffin embedded Human Spleen, with no primary antibody.

(0.1ug/ml) staining of Mouse Lymph node lysate (35ug protein in RIPA buffer). Detected by chemiluminescence.

(1ug/ml) staining of Human Frontal Cortex (A) and (0.1ug/ml) Mouse (B) and Rat (C) Brain lysate (35ug protein in RIPA buffer). Detected by chemiluminescence.

(8ug/ml) staining of paraffin embedded Human Spleen. Heat induced antigen retrieval with citrate buffer Ph 6, HRP-staining.

GM1 effects on brain microglia in vivo, after peripheral administration of LPS. C) Immunoblot in whole brain lysates and densitometric analysis show LPS-dependent increase in Iba 1 expression. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/34991625), licensed under a CC-BY licence.

CXCR2+neutrophils are not required for microglial activation. a Representative images of Iba1 immunohistochemistry staining in lumbar spinal cord ventral horns of naive control, control EAE, and Cxcr2 cKO EAE mice. Quantitative analysis of Iba1+ cell (b) soma area as shown in a. A total of 2338 Iba1+ cells were included in our analyses of soma size (cont naive, 222 Iba1 cells; control EAE, 1236 Iba1+ cells; Cxcr2 cKO EAE, 880 Iba1+ cells). Control naive, n = 3; control EAE, n = 3; Cxcr2 cKO EAE, n = 3. *p 1.5, FDR-corrected p1.5, FDR-corrected p<0.05) to identify GO terms, including inflammatory response (b). The volcano plot shows significant DEGs derived from the NanoString analysis of the brains of Plcg2 inactivation (PLCG2 inact, n=3) and WT (n=3) mice (1-month male) (c). Immunostaining of microglial markers with IBA1 (green) and P2RY12 (red) and quantification of percent area in brain sections of 1-month-old male WT and PLCG2 inact demonstrate unchanged microglial morphology and area coverage (d). GO gene ontology, BP biological process, DEGs differentially expressed genes, FDR false discovery rate Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35180881), licensed under a CC-BY licence.

Deficiency of HDAC3 in microglia suppresses the cGAS-STING-mediated autoimmune response. (K) Proteins extracted from the ischemic penumbra and contralateral cortex of HDAC3 cKO and WT mice subjected to tMCAO 6 h post-reperfusion were analyzed with antibodies against cGAS, HDAC3, Iba1, and GAPDH. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32863951), licensed under a CC-BY licence.

ADT induced SPINK1 upregulation associates with NE-phenotype in mice and NEPC patients.a Box plots depicting relative expression of SPINK1, SYP, CHGA, TUBB3, and VIM transcripts (read counts) in VCaP tumors implanted orthotopically in orchiectomized mice and subjected to vehicle (n = 4) or anti-androgens [enzalutamide (n = 4) or ARN-509 (n = 4)] treatment for 4 weeks (GSE95413). b Representative images of immunohistochemical staining for the same markers shown in a using VCaP xenograft tumors as described in a. Scale bar represents 100 μm. c Box plots depicting quantification of the immunohistochemical staining in VCaP xenografts for the markers shown in b. d Representative images for immunohistochemical staining of SPINK1, SYP, CHGA, and TUBB3 in 22RV1 xenograft tumors excised from orchiectomized mice treated with enzalutamide (20 mg/kg body weight) or vehicle control (n = 5 each). Intact group represents non-castrated control mice (n = 5). Scale bar represents 50 μm. e Box plots depicting quantification of the immunohistochemical staining in 22RV1 xenografts for the markers shown in d. f Representative images showing H&E staining (×200 magnification) and immunostaining (×200 magnification) for AR, synaptophysin, and SPINK1 in tumor specimens obtained from NEPC patients’, namely WCM12, WCM155 (an organoid), and WCM677. Scale bar represents 100 µm. Data are presented as box-and-whisker plots with median, where the box extends from 25th–75th percentile, and whiskers ranges from minimum and maximum values. For panels a, c, e one-way ANOVA, Dunnett’s multiple-comparisons test was applied. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31959826), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

EBNA1 promotes the upregulation of oxidative DNA damage repair pathways in EBV converted cell lines and EBV positive BLs. a Representative western blots illustrating the expression of MTH1, OGG1, and MUTYH in pairs of EBV-negative and -positive cell lines. GAPDH was used as loading control. b Densitometry quantification of the specific bands. The intensity of the specific band in EBV positive cells relative the EBV-negative parental is shown. Mean ± SE of four independent experiments. c Representative western blots illustrating the expression of EBNA1, MTH1, OGG1, and MUTYH in the Mutu cell lines. d Densitometry quantification of expression in the EBV positive cell lines relative to the EBV-negative Mutu-30. Mean ± SE of four independent experiments Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31511648), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Rab31 expression levels in stably transfected breast cancer cells. (A) pAb RT3-IgG specifically detects rab31 in cell lysates from stably transfected MDA-MB-231 and CAMA-1 breast cancer cells in Western blot analyses. Vector control, MDA-MB-231, or CAMA-1 cells were stably transfected with the empty vector pRcRSV; batch, parental MDA-MB-231 (low endogenous rab31 expression) or CAMA-1 (no endogenous rab31 expression) cells were stably transfected with the pRcRSV-based rab31 expression vector; high, medium or low, selected cell clones of batch-transfected MDA-MB-231 or CAMA-1 cells with differing high, medium or low protein levels of rab31. (B) Rab31 antigen values (ng/mg of total protein) in rab31-transfected MDA-MB-231 and CAMA-1 cells, determined by rab31-ELISA. Mean values (± SEM) of at least three independent experiments are depicted. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/22920728), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

EGFR inhibition downregulates VEGF and HIF-1 in vitro and in vivo.SQ20B cells were seeded at 25% confluence and cultured overnight. The next morning, cells were transfected with 150 nanomoles siRNA (either EGFR SmartPool or control non-targeted) in Optimem transfection medium using Oligofectamine. After 24 hours, the transfection medium was replaced with fresh, prewarmed culture medium. 24 hours after this (48 hours after transfection), cells were exposed to either 21% or 1% oxygen. Three hours later they were harvested and Western blotting was performed. (B) SQ20B cells were treated with 10 nM cetuximab or DMSO (control) for 16 hrs, and then exposed to either 21% or 1% oxygen. Three hours later they were harvested and Western blotting was performed. (C) Nude mice were injected subcutaneously in the flank with SQ20B cells to form xenografts. When the tumors reached a size of 100–150 mm3 (approximately 7–10 days after injection), half the mice (lanes 4–6) were started on an erlotinib-containing diet (50 mg/kg/day). After 4 days of feeding, mice were sacrificed, and the tumors were removed. Half of each tumor was lysed in protein lysis buffer, and Western blotting was performed for pAkt (S473) and HIF-1 alpha . Each lane represents a tumor from a different mouse. (D) The other half of each tumor from (E) was homogenized in PBS, and then ELISA for VEGF was performed. VEGF level was normalized to tumor weights. Data shown represent mean values from 3 control mice and 3 erlotinib-treated mice. Error bars represent standard error of the mean. p value was obtained using Student's t-test. (E) H226 cells were treated with 10 µM erlotinib or DMSO (control) for 16 hrs, and then exposed to either 21% or 1% oxygen. Three hours later they were harvested and Western blotting was performed. (F) H226 cells were seeded then later that day they were treated with erlotinib (10 µM) or DMSO (control). 24 hours later, the media was changed and replaced with media containing 1% serum with or without erlotinib. Cells were exposed to 1% oxygen. 16 hours later, aliquots of supernatant were removed from dishes, and ELISA for VEGF was performed. ELISA values were normalized to the number of cells present. Data shown represent mean values. Error bars represent standard error of the mean. p value was obtained using Student's t-test. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/19657384), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Elevated levels of additional proteins and GM3 ganglioside in the MEC of MPS IIIB brain.Staining performed with antibodies to the indicated substances was observed in the MEC region of 3 month-old MPS IIIB mice (for total ubiquitin and polyubiquitin) and 6 months for all others. Staining was not seen in the MEC region of age-matched control mice (Naglu +/−) nor in the LEC region of MPS IIIB mice (the latter not shown). Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.pone.0027461), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

ERK2 utilizes kinase-docking domains to interact with ATG5–ATG12 and LC3-II.(a) Mutations in FRS on ERK2 decrease colocalization of ERK2 with ATG5–ATG12, LC3 and WIPI1. Immunofluorescence (IF) showing colocalization (depicted as white pixels by ‘colocalization finder application’) of WT-ERK2-HA, FRS ERK2 mutants (L198A-, L232A-, L198A/L232A-, Y261A-ERK2-HA) or common docking (CD) mutant (D319N-ERK2-HA) with ATG5–ATG12 (panels 1–6), LC3 (panels 7–12) or WIPI1 (panels 13–18) in EGF-treated NIH/3T3 cells. ERK2 is stained in red, and autophagy proteins are stained in green. Scale bar, 10 μm. The bars represent mean±s.e.m. **P<0.01, ****P<0.0001 compared with WT-ERK2-transfected cells; Student’s t-test, 50 cells analysed from n=2. (b) Mutations in FRS on ERK2 decrease colocalization of ERK2 with nuclear ATG5–ATG12 or LC3. IF showing colocalization (white pixels) of WT-ERK2-HA (red), FRS ERK2 mutants (L198A-, L232A-, L198A/L232A-, Y261A-ERK2-HA) or common docking (CD) mutant (D319N-ERK2-HA) with ATG5–ATG12 (panels 1–6) or LC3-II (panels 7–12) in EGF-treated NIH/3T3 cells. Scale bar, 5 μm. The bars represent mean±s.e.m. **P<0.01, ***P<0.001, ****P<0.0001 compared with WT-ERK2-transfected cells; Student’s t-test, 50 cells analysed from n=2. Arrows depict colocalization. (c) ATG5–ATG12 conjugation is required for ERK phosphorylation. Immunoblots for P-ERK, total ERK and beta -actin in NIH/3T3 cells transfected with WT ATG5 or the conjugation-defective ATG5 K130R mutant and treated with EGF (10 min). The bars represent mean±s.e.m. *P<0.05 compared with WT ATG5-transfected cells; Student’s t-test, n=3. Image collected and cropped by CiteAb from the following open publication (//www.nature.com/articles/ncomms3799), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Human tumor microarrays (TMAs).Pilocytic astrocytoma TSPO immunohistochemistry (A) and TSPO immunohistochemical scoring (C). Glioblastoma multiforme TSPO immunohistochemistry (B) and TSPO immunohistochemical scoring (D). Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.pone.0141659), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

DNMT1 reveals a SCMC-like cortical localization with aberrant localization in Nlrp2tm1a/tm1a derived oocytes.(A) Whole mount immunofluorescence co-staining with anti-DNMT1 and DAPI on the same Nlrp2M+/Z+ embryos used to stain NLRP2 reveals a SCMC-like cortical localization of DNMT1 with a diffuse nuclear stain in later stage embryos. Scale bar represented is 200 μm. (B) DNMT1 staining in paraffin embedded oocyte sections reveals a less cortical, more cytoplasmic intense stain with nucleolar focus in oocytes from Nlrp2tm1a/tm1a dams compared to oocytes from Nlrp2+/+ dams. (C) Whole mount immunofluorescence for DNMT3A in unfertilized control oocytes reveals a characteristic metaphase associated localization and no difference is noted in oocytes derived from Nlrp2tm1a/tm1adams. (D) Whole mount immunofluorescence in unfertilized oocytes reveals that as expected, DNMT3B is not yet expressed in unfertilized control oocytes and no expression is noted in oocytes derived from Nlrp2tm1a/tm1adams. Image collected and cropped by CiteAb from the following open publication (//www.nature.com/articles/srep44667), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Activation of MAPK7 in chondrocytes is essential for hypoxic adaptation and enhancement of HIF1 alpha signaling under hypoxia. a, b Immunofluorescence staining of (a) MAPK7 (b) P-MAPK7 on representative sections of distal femoral growth plates at P1. Scale bar, 200 μm. RZ, resting zone; PZ, proliferative zone; HZ, hypertrophic zone. c Western blot analysis of MAPK7 and p- MAPK7 in primary chondrocytes cultured under hypoxic conditions for 0, 1, 4, 12, or 24 h. d Immunofluorescence staining of SOX9 on representative sections of distal femoral growth plates at P1. Scale bar, 200 μm. e Western blot analysis of SOX9, COL2A1, MAPK7, HIF1 alpha , and VEGFA in CON and Mapk7 CKO chondrocytes cultured under normoxic or hypoxic conditions for 48 h. f Western blot analysis of SOX9, COL2A1, MAPK7, p-MAPK7, HIF1 alpha , and VEGFA protein levels in XMD8-92- or DMSO-treated primary chondrocytes cultured under normoxic or hypoxic conditions. Primary chondrocytes harvested from wild-type mouse knees were cultured in the presence of 5 μM XMD8-92 or an equal amount of DMSO under normoxia for 3 h, followed by normoxia or hypoxia for 48 h. XMD, XMD8-92. g, h mRNA levels of (g) Sox9 and (h) Col2a1 in CON and Mapk7 CKO chondrocytes cultured under normoxia or hypoxia were measured by real-time quantitative PCR (n = 3). *P < 0.05 (one-way ANOVA followed by Dunnett’s post hoc test). Data are presented as mean ± SD. i Immunofluorescence staining of HIF1 alpha on representative proximal tibial growth plate sections from P1 mice. Scale bar, 200 μm. j mRNA levels of Hif1a and its known target genes were measured in growth plate cartilage from P1 Mapk7 CKO mice by real-time quantitative PCR. k HIF1 alpha activity in CON and Mapk7 CKO chondrocytes cultured under normoxia or hypoxia, as evaluated by HIF1 alpha -responsive element luciferase reporter (HRE-luc) assay (n = 5). *P < 0.05 (one-way ANOVA followed by Dunnett’s post hoc test). Data are presented as mean ± SD. l mRNA level of hif1a in CON and Mapk7 CKO chondrocytes cultured under normoxia or hypoxia were measured by real-time quantitative PCR (n = 3). *P < 0.05 (one-way ANOVA followed by Dunnett’s post hoc test). Data are presented as mean ± SD. m Free ATP levels in CON and Mapk7 CKO chondrocytes cultured under normoxic or hypoxic conditions (n = 4). *P < 0.05 (one-way ANOVA followed by Dunnett’s post hoc test). Data are presented as mean ± SD. n Primary chondrocytes were transfected with WT-MAPK7 or DN-MAPK7 expression vector in the presence of CA-MEK5 expression vector. Cells were harvested 48 h after transfection and protein levels of HIF1 alpha , MAPK7 and p-MAPK7 were assayed by western blot Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/32944217), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

TRF2 transcriptionally regulates p21 expression through promoter occupancy. (A) Quantitative ChIP using TRF2 antibody gives enriched binding of TRF2 on p21 promoter in HT1080 and MDA-MB-231 cells, IgG was used as isotypic antibody control; normalized with 10% input (data represented as mean ± SEM, for three replicates). (B,C) TRF2 represses p21 promoter activity. In luciferase assay, si-RNA-mediated silencing or TRF2 over expression resulted in increased (B, *p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) or reduction (C, *p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) in p21 promoter activity in HT1080 and MDA-MB-231 cells, respectively; over expression of TRF2 devoid of DNA binding [deletion of basic (delB), myb (delM) and both basic/myb (delB-delM) domains] resulted in partial or complete rescue of p21 promoter activity in HT1080 and MDA-MB-231 cells (data represented as mean ± SEM, for three replicates) (C). (D,E) HT1080 cells over expressing TRF2 show reduced p21 protein expression, bar graph shows the densitometry analysis of three different immunoblot replicates (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates). (E) (Full images are shown in Supplementary Figure S5); TRF2 silencing results in increase in p21 protein, bar graph shows the densitometry analysis of three different immunoblots (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) (F); and mRNA expression in HT1080 cells (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates, GAPDH used as internal control for real-time PCR). Image collected and cropped by CiteAb from the following open publication (//www.nature.com/articles/s41598-017-11177-1), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunohistochemistry-Paraffin: Goat Polyclonal AIF-1/Iba1 Antibody [NB100-1028] - AIF-1/Iba1 immunoreactivity in an FFPE section of mouse spleen. NB100-1028 was diluted to 1ug per mL and was left on tissue sections for 30m at room temperature. Secondary was horse anti goat HRP polymer. Image from a verified customer review.

Reactivity:

Hu, Mu, Rt, Ca, Eq, Fe, Po

Species Glossary

Reactivity: Hu, Mu, Rt, Ca, Eq, Fe, Po

Applications:

, , , , , ,

Applications: , , , , , ,

Host:

Goat Polyclonal

Host: Goat Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

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NB100-142

Mre11 Antibody

(4 Reviews)

(234 Publications)

0.05 ml

NB100-142

<b>Genetic Strategies Validation. </b>Knockdown Validated: Mre11 Antibody [NB100-142] - Mre11 and NBS1 contribute to OriP replication and EBV episome stability. D98/HR1 cells were transfected with siRNA for Mre11 or NBS1, or Luciferase control and assayed by immunoblot (IB) with antibodies specific for Mre11 (left pane) or NBS1 (right panel), or PCNA (lower panel) as a loading control. Image collected and cropped by CiteAb from the following publication (//journals.plos.org/plosone/article?id=10.1371/journal.pone.0001257) licensed under a CC-BY license.

Immunohistochemistry: Mre11 Antibody [NB100-142] - Immunohistochemical staining of MRE11 in a human epidermis cross section.

Western Blot: Mre11 Antibody [NB100-142] - Western blot analysis of Mre11 on 50 ug of HeLa and MEF lysates, displaying bands at the molecular weight of 81 kDa.

Immunocytochemistry/Immunofluorescence: Mre11 Antibody [NB100-142] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.5% Triton X-100. The cells were incubated with anti-Mre11 [NB100-142] at a 1:500 dilution overnight at 4C and detected with an anti-rabbit DyLight 488 (Green) at a 1:500 dilution. Actin was detected with Phalloidin 568 (Red) at a 1:200 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

Chromatin Immunoprecipitation: Mre11 Antibody [NB100-142] - Aggregated END-seq signal and MRE11 ChIP-seq RPM in WT (left) and Atm -/- (right). To fairly compare ChIP-seq signal between WT and Atm -/-, MRE11 scale is proportional to spike-in normalized END-seq RPM for each genotype. Individual hotspot examples (chr12:34,592,264-34,598,265) are shown below. Note that decreased MRE11 coverage is observed within NDR of Atm -/-. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32051414/) licensed under a CC-BY license.

Knockdown Validated: Mre11 Antibody [NB100-142] - TIG-1 human primary fibroblasts, whole cell lysate (30 ug). Image from verified customer review.

ATM coordinates multiple levels of resection machinery. d Aggregated END-seq signal and MRE11 ChIP-seq RPM in WT (left) and Atm-/- (right). To fairly compare ChIP-seq signal between WT and Atm-/-, MRE11 scale is proportional to spike-in normalized END-seq RPM for each genotype. Individual hotspot examples (chr12:34,592,264-34,598,265) are shown below. Note that decreased MRE11 coverage is observed within NDR of Atm-/-. e Aggregate plot overlapping WT END-seq and Atm-/- MRE11 ChIP-seq, normalized to the same height. MRE11 shows prominent localization to the WT END-seq read-less gap. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32051414), licensed under a CC-BY licence.

Elevated levels of various proteins in MEC and in dentate gyrus of MPS IIIA brain.Staining was performed with antibodies against the proteins shown in a 7 months-old MPS IIIA mouse brain. The first 3 rows are for the MEC region and the bottom row for dentate gyrus. Age-matched C57BL6 mice, used as controls, showed no staining in the MEC region (not shown). The dentate gyrus showed AT270 inclusions in MPS IIIA (−/−) mouse brain (arrows) but not in the C57BL/6 (control) brain (bottom row). Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.pone.0027461), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$SUMO2-PCNA enriches CAF1 and FACT within the replication complex. a Western blot analysis of the indicated proteins in the CB fractions (left) and the FLAG-PCNA complexes purified from CB fractions (right) prepared from cells expressing the indicated FLAG-tagged proteins. Ub-KR indicates the FLAG-ubiquitin-PCNA (KR) fusion protein. b Western blot analysis of the indicated proteins in the CB input (left panels) used for the in vitro pull-down experiments of purified recombinant strep-tagged PCNA, SUMO2-conjugated PCNA, and GFP anchored to Strep-Tactin resins (right panels). SUMO2-modified PCNA was generated by the in vitro SUMOylation reaction using strep-PCNA and His-SUMO2 shown in Supplementary Fig. 6a, b. c Western blot analysis of the input levels of recombinant strep-PCNA and strep-SUMO2-PCNA fusion (S2-PCNA) purified from E. coli (left panel) and of strep-PCNA and strep-S2-PCNA pulled down by WT or SIM mutant FLAG-CAF1A proteins purified and anchored on FLAG M2 agarose beads from HEK293T cells expressing the corresponding constructs (right panels). d Western blot analysis of strep-S2-PCNA (upper 2 panels) and strep-PCNA (lower 2 panels) pulled down by FLAG-CAF1A purified from E. coli and anchored on FLAG M2 agarose beads. e Western blot analysis of the indicated proteins in the CB input prepared from HEK293T cells expressing FLAG-SSRP1 WT or SIM mutant (left panels) and of FLAG-SSRP1 and SPT16 pulled down from the CB fractions in vitro using purified recombinant strep-tagged PCNA, S2-PCNA, and GFP anchored to Strep-Tactin resins (right panels) Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/30006506), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Restoration of nuclear PTEN-mediated DNA damage signalling by restraining CK2 impairs tumour but not normal neural stem cell survival.(a) Immunoblot analysis displaying the impact of TBB treatment (25 μM/24 h) on CK2 beta , PTEN, p-PTEN (S380/T382/T383), p-AKT (S473) and p-PRAS40 (T246) in GXP GBM3 & 4, with beta -actin used as loading control. (b) IF of PTEN with DAPI nuclear staining in dimethylsulfoxide (DMSO)- or TBB (25 μM/24 h)-treated cells in the absence of DOX or after 5 h of exposure to DOX (0.5 μM). DOX was added 5 h before the end point of DMSO or TBB treatment. Representative images are shown. Scale bars, 20 μm. (c) Co-IF of gamma H2AX and 53BP1 foci formation with DAPI nuclear staining in DMSO- or TBB (25 μM/24 h)-treated GXP NS or GBM2 with DOX−, or 1 h or 5 h of DOX (0.5 μM) exposure followed by 5 or 24 h of recovery time. Scale bars, 10 μm. A graph quantifying the percent of gamma H2AX-positive GXP NS or GBM2 cells (y axis) with DMSO or TBB treatment at indicated time points of DOX treatment (x axis) is summarized in the graph in (d). Error bars represent mean±s.d. Representative 100 cells were randomly selected for quantification. Cells with ≥5 foci were considered as gamma H2AX positive. (e) Co-IF of FANCD2 and gamma H2AX with DAPI nuclear staining in TBB (25 μM/24 h)-treated GXP GBM2 exposed to DOX (0.5 μM) 5 h before fixation. Scale bars, 10 μm. The percent of FANCD2/ gamma H2AX-positive foci at DSB sites (y axis) in TBB− or TBB+ (x axis) in GXP GBM2 is summarized in the graph shown in (f). Error bars represent mean±s.e.m. See also Supplementary Fig. 4. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/28094268), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

GRPs enhance axonal growth in DRGs in vitro. A–C, Representative montage images are shown for control dissociated DRG culture (A), dissociated DRGs cocultured with rat GRPs (B), and dissociated DRGs cultures exposed to conditioned medium from alkaline phosphatase-expressing rat GRPs (C). beta III-tubulin (red) immunofluorescence highlights the neurons; GRPs are visualized by immunostaining for alkaline phosphatase (green). D shows quantification for the average length of the longest axon per neuron ± SEM (n ≥ 30 neurons in three separate experiments; **p ≤ 0.01 by Student’s t test). Scale bar, 250 μm. Image collected and cropped by CiteAb from the following open publication (//www.eneuro.org/lookup/doi/10.1523/ENEURO.0171-16.2017), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Ch, Ha, Bt, Bv, Ca, Pm, Eq, Fe, Pm

Species Glossary

Reactivity: Hu, Mu, Rt, Ch, Ha, Bt, Bv, Ca, Pm, Eq, Fe, Pm

Applications:

, , , , , , , , , , ,

Applications: , , , , , , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Validated by:

Validated by:

Available Formulations

Formulation	Catalog #	Availability	Price
Purified	NBP3-25349-0.025mg
Purified	NBP3-25349-0.05mg

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NB100-143

Nbs1 Antibody

(8 Reviews)

(199 Publications)

0.05 ml

NB100-143

Immunocytochemistry/Immunofluorescence: Nbs1 Antibody [NB100-143] - ICC/IF analysis of Nbs1 in HeLa cells with Nbs1 Antibody [NB100-143]. Image from verified customer review.

Immunohistochemistry-Paraffin: Nbs1 Antibody [NB100-143] - FFPE human testis using Nbs1 antibody [NB100-143] at 1:200 on a Bond Rx autostainer (Leica Biosystems). The assay involved 20 minutes of heat induced antigen retrieval (HIER) using 10 mM sodium citrate buffer (pH 6.0) and endogenous peroxidase quenching with peroxide block. The sections were incubated with primary antibody for 30 minutes and Bond Polymer Refine Detection (Leica Biosystems) with DAB was used for signal development followed by counterstaining with hematoxylin. Whole slide scanning and capturing of representative images was performed using Aperio AT2 (Leica Biosystems). Staining was performed by Histowiz.

Western Blot: Nbs1 Antibody [NB100-143] - Analysis of HeLa whole cell lysate [NB800-PC1] using rabbit polyclonal NBS1 antibody [NB100-143]. Observed Molecular Weight at ~95 kDa.

<b>Genetic Strategies Validation. </b>Western Blot: Nbs1 Antibody [NB100-143] - Detection of NBS1 in Human Bone Osteosarcoma Epithelial Cells (U2OS whole cell lysate) using Nbs1 Antibody [NB100-143] at a dilution of 1:1000. Specificity was confirmed using a siRNA anti-NBS1 (targeting sequence: GGAAGAAACGUGAACUCAA). Image provided by Sebastien Britton of the Institute of Pharmacology and Structural Biology.

Western Blot: Nbs1 Antibody [NB100-143] - Western Blot with Nbs1 Antibody [NB100-143]. TIG-1 human primary fibroblasts, whole cell lysate (30 ug). Image from verified customer review.

Immunocytochemistry/Immunofluorescence: Nbs1 Antibody [NB100-143] - Staining of HeLa cells using Nbs1 Antibody [NB100-143].

<b>Genetic Strategies Validation. </b>Knockdown Validated: Nbs1 Antibody [NB100-143] - TOPBP1 recruitment in response to rDNA breaks. TOPBP1 localization 2 h after I-Ppo1 transfection in NBS1-delta-N cells and NBS1-delta-N cells complemented with wild-type and mutant NBS1-mNG (percentage of cells with > 2 TOPBP1 caps are indicated; one of two experiments is shown). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31913317/) licensed under a CC-BY license.

HPV16 E2 partially colocalizes with the MRN complex proteins Mre11 and Nbs1. C33a cells were transfected with an HPV16 E2 expression plasmid, fixed in ice-cold methanol, and stained with an E2-specific antibody (green). DNA was stained with Hoechst 33342 (blue). (A) Endogenous Nbs1 was detected with an Nbs1-specific antibody (red/gray). (B) Endogenous Mre11 was detected with an Mre11-specific rabbit antibody (red/gray). Bar, 5 μm. Digital zoom is shown at the bottom.

TOPBP1 recruitment in response to rDNA breaks. b) TOPBP1 localization 2 h after I-Ppo1 transfection in NBS1deltaN cells and NBS1deltaN cells complemented with wild-type and mutant NBS1-mNG (percentage of cells with > 2 TOPBP1 caps are indicated; one of two experiments is shown). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31913317), licensed under a CC-BY licence.

ATM promotes cell migration and invasion independently of DNA DSB signaling in MDA-MB-231 cells.(B and C) Quantification of wound healing (B) and siRNA depletions (C) in (A). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26030852), licensed under a CC-BY licence.

KSHV LANA recruits MRN (Mre11-Rad50-NBS1) complex.(A) Co-immunoprecipitation of endogenous LANA and MRN proteins in BC3 cells. Cells were lysed using TBS-T buffer and the cell lysate was incubated with benzonase. After centrifugation, supernatant was incubated overnight with anti-LANA or IgG-control beads. The precipitated complexes were analyzed for the presence of endogenous Rad50, Mre11 and NBS1 by SDS-PAGE and immunoblotting. For the input, see Materials and methods. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.ppat.1006335), licensed under a CC-BY licence.

Replication centers of the integrated HPV recruit Mre11-Nbs1-Rad50 complex and Ku70/80 heterodimer.HeLa cells were transfected and analyzed as described previously. Co-immunostaining of HPV18 E1 (Alexa Fluor 568, second column) and the following proteins are presented: Mre11, Nbs1, Rad50, and Ku70/80 proteins (Alexa Fluor 488, first column). The localizations of the E1 and the respective DNA repair proteins are also shown in the third column as a merged image and DAPI stained nuclei are presented in the fourth column. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/19390600), licensed under a CC-BY licence.

TRIB3 suppresses the functions of the UBE3B:MYC axis to attenuate lymphomagenesis.a Occupancy heatmap of genome-wide MYC peaks in MYCWT and MYCK427R Raji cells in a window of ±10 kb surrounding the transcription start site (TSS). b Distribution of MYC tags in MYCWT and MYCK427A Raji cells. Binding is shown for a window of ±2 kb around MYC tags as reference coordinates. c GSEA shows global downregulation of MYC target genes in Ad-UBE3B versus Ad-CTRL Raji cells. d Metagene plots of global RNAPII occupancy at gene bodies in Raji cells with or without UBE3B overexpression. e Colony-forming capacity of Raji cells with or without UBE3B overexpression. The data are presented as the means ± S.E.M from three independent experiments. Statistical significance was determined by two-tailed Student’s t test. P value: 0.00047. f Relative cell viabilities of Raji cells with overexpression of the indicated genes for the indicated times. The colors represent different time points; the diameter indicates the relative cell viability. The data are presented as the means ± S.E.M from three independent experiments. g Schematic strategy for studying BCL development in MycEμ mice with the indicated infection of Ad-GFP, Ad-Ube3b, Ad-Trib3, or Ad-Ube3b plus Ad-Trib3 in vivo. h Data are the spleen weights of MycEμ mice (n = 8 per group) with overexpression of the indicated genes. Data are represented as means ± SEM. Statistical significance was determined by two-tailed Student’s t test. P values: 2.077 × 10−5, 0.0009. i Data are representative LNs in MycEμ mice overexpressing Ad-GFP, Ad-Ube3b, Ad-Trib3, or Ad-Ube3b plus Ad-Trib3. Scale bar, 0.5 cm. j Cell proliferation was determined by Ki67 staining in the spleens of the indicated mice (n = 6 per group). Data are representative images of Ki67 staining and statistical analyses of Ki67-positive cells. Data are represented as means ± SEM. Statistical significance was determined by two-tailed Student’s t test. P values: 1.352 × 10−12, 3.674 × 10−8. Scale bar, 50 μm. k Approaches to defining the self-renewal ability of mouse LCs from the indicated mice (5 months old). l Colony-forming ability of BCL cells isolated from MycEμ mice (n = 6 per group) overexpressing Ad-GFP, Ad-Ube3b, Ad-Trib3, or Ad-Ube3b plus Ad-Trib3. Data are represented as means ± SEM. Statistical significance was determined by two-tailed Student’s t test. P values: 4.318 × 10−5, 0.0001. m The tumorigenicity of BCL cells from the indicated mice was compared by limiting dilution transplantation into NSG mice; n = 8 mice per group. n Schematic strategy for studying BCL development in MycEμCD19CreTrib3F/+ mice infected with or without lentivirus Ube3bCas9. o Kaplan–Meier survival curves for MycEμCD19CreTrib3F/+ mice infected with or without lentivirus Ube3bCas9 (n = 8 per group). Statistical difference was determined by two-sided log-rank test. P value: 0.0002. p Expression of MYC in the spleens of MycEμCD19CreTrib3F/+ mice (5 months old) infected with or without lentivirus Ube3bCas9. The data are presented as presentative from three independent experiments. q Colony-forming ability of BCL cells isolated from the LNs of the indicated mice (n = 6 per group). The data are representative or the means ± SEM of three assays. Statistical significance was determined by two-tailed Student’s t test. P value: 5.417 × 10−5, 0.0042. The MycEμCreCD19Trib3F/+ mice are heterozygous for the MycEμ allele. Source data are provided as a Source Data file. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/33298911), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$The BNIP3 C-terminus can be phosphorylated.(A) Western blot detection of immunoprecipitated BNIP3 using an alpha -PKA substrate antibody specific to the phosphorylated RRXS/T sequence, located at the BNIP3 C-terminus and adjacent to the transmembrane (TM) domain. Results shown for 4 cell types: (left to right) HEK 293 cells expressing exogenous BNIP3 (dimer, 60 kD), and A549, MDA-MD-231, and AU565 cells expressing endogenous BNIP3 (monomer, 30kD). Lane 1 of each Western blot contains the whole cell lysate (WCL). (B) LC-MS/MS analysis of BNIP3 phosphorylation in HEK 293 cells with normal or elevated cAMP (8-Bromo-cAMP), showing peptide coverage (gray) and phosphorylation sites (red). The TM domain is underlined. (C) Table of BNIP3 phosphopeptides identified by LC-MS/MS, showing the percent probability, ion charge, actual and observed masses, and mass error (Da and ppm) for each peptide. Peptides shown are from analysis of BNIP3 purified from HEK 293 cells with elevated cAMP levels. (D) Schematic of the BNIP3 protein sequence, showing each C-terminal mutation representing phosphomimetic or nonphosphorylated BNIP3. (E) Expression of BNIP3 phosphomutants from stable doxycycline-inducible HEK 293 Tet On cells, treated with doxycycline (Dox) for 48 hr. (F) Subcellular localization of BNIP3 phosphomutants, showing Western blot of cytosolic and mitochondrial fractions. (G) Alkaline extraction of mitochondria-associated proteins, showing alkaline extract of the mitochondrial pellet and the alkaline-resistant mitochondrial pellet from cells expressing each BNIP3 phosphomutant. All blots are representative of at least 3 independent experiments. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/26102349), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

$TAZ induces Tfam protein expression at the translational level.a The expression of mitochondrial biogenic factors, including Tfam, Ppargc1a (Pgc1 alpha ), Nrf1, and Nrf2, was analysed using quantitative reverse transcription (qRT)-PCR in the gastrocnemius muscle of wild-type (WT) and muscle-specific TAZ knockout (mKO) mice; n = 6 for each condition (Tfam; *p = 0.0498, Nrf1; *p = 0.0467). b Protein was analysed via immunoblotting to detect TAZ and the indicated mitochondrial biogenic factors in (a). Alpha-tubulin was used as the loading control. c RNA was isolated from the control (Con) and TAZ knockdown (KD) C2C12 myotubes, and the expression of the indicated mitochondrial biogenic factors was analysed using qRT-PCR. The experiments were performed in triplicate (Tfam; *p = 0.04). d Protein from the Con and TAZ KD C2C12 myotubes was assessed via immunoblotting to detect TAZ and mitochondrial biogenic factors. Beta-actin was used as the loading control. e RNA was isolated from WT, TAZ-knockout (KO), and TAZ-rescued (T) mouse embryonic fibroblasts (MEF), and the indicated mitochondrial biogenic factors were analysed via qRT-PCR. f Protein from WT, KO, and T MEF was assessed via immunoblotting to detect TAZ and the indicated mitochondrial biogenic factors. Beta-actin was used as the loading control. g Protein was isolated from the gastrocnemius muscle of WT and mKO mice and analysed via immunoblotting to detect TAZ, YAP, and proteins involved in the translation of both phosphorylated and total forms. Alpha-tubulin was used as the loading control. h Protein obtained from the Con and TAZ KD C2C12 myotubes was assessed via immunoblotting to observe TAZ and proteins involved in translation. Beta-actin was used as the loading control. i Protein was isolated from WT, KO, and T MEF and analysed via immunoblotting to detect TAZ and proteins involved in translation. Vinculin was used as the loading control. j The polysome profile of cells described in panel i was evaluated continuously by measuring absorbance at 254 nm. The 40S, 60S, 80S, and polysome fractions are denoted by the corresponding peaks. k The distribution of Tfam, Atp5d, and Gapdh mRNA from cells described in (j) across a density gradient was analysed using reverse transcription (RT)-PCR. bp = base pairs. For a, b, g 8 to 10-week-old mice were used. Data are presented as mean ± SEM for (a), mean ± SD for (c, e). Statistical significance was analysed via two-sided t-test for (a) and one-sided t-test for (c). One-way ANOVA with Tukey’s multiple comparison test was used for (e). Representative data was shown and experiments were performed at least twice with similar results for (b, d, f–i, k). Source data are provided as a Source data file. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35115527), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

mTOR complex protein expressions and rictor phosphorylation at Ser1235.Cardiomyocytes were pretreated for 30 min with 20 nM rapamycin and then stimulated with 10 nM IGF-1 in presence or absence of 10 nM E2 for 24 h. A, shown are representative western blots for mTOR, rictor and raptor and B,C,D, quantitative analysis with mean ± SEM of fold stimulation by IGF-1 of at least 3 independently performed experiments (B,C,D). * p < 0.05, **p < 0.0095. Exposure to rapamycin lead to downregulation of mTOR and rictor, which were more pronounced under culture conditions without E2. E, Western blots for GSK3 beta -pS9, GSK3 beta , rictor pS1235 and rictor and F,G,H,I quantitative analysis of at least 3 independently performed experiments indicate that rictor phosphorylation at S1235 by GSK-3 beta which has been reported to interfere with Akt-substrate binding to mTORC2, thereby downregulating mTORC2 activity. IGF-1 induced strong phosphorylation of GSK-3 beta at Ser9 in the absence and presence of E2, however, rapamycin pretreatment only reduced this increased phosphorylation in E2 co-treated cardiomyocytes, indicating increased activity of GSK-3 beta . This higher activity was not associated with increased phosphorylation of rictor at S1235. Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.pone.0123385), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Ha, Ma, Pm

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Reactivity: Hu, Mu, Ha, Ma, Pm

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, , , , , , , , , , , ,

Applications: , , , , , , , , , , , ,

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NB110-57130

TRF-2 Antibody - BSA Free

(2 Reviews)

(136 Publications)

0.1 ml

NB110-57130

Western Blot: TRF-2 Antibody [NB110-57130] - Analysis of HeLa whole cell lysate (A), HeLa nuclear cell lysate (B), k562 cell lysate (C), HepG2 cell lysate (D), NIH/3T3 cell lysate (E), CHO cell lysate (F), PC12 cell lysate (G), and Cos7 cell lysate (H) using antibody at a concentration of 2 ug/mL.

Immunohistochemistry-Paraffin: TRF-2 Antibody [NB110-57130] - Analysis in xenografted human breast cancer tissue using DAB with hematoxylin counterstain.

Immunohistochemistry-Paraffin: TRF-2 Antibody [NB110-57130] - Analysis of FFPE human breast cancer tissue with rabbit polyclonal TRF2 antibody at a dilution of 1:200. The staining was developed with HRP-DAB detection method and the counterstaining was performed using hematoxylin. This TRF2 antibody generated an expected nuclear signal in all the cancer cells and the stromal cells. In the tested section, only a subset of myoepithelial cells showed positivity for this protein.

Immunocytochemistry/Immunofluorescence: TRF-2 Antibody [NB110-57130] - NIH3T3 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.5% Triton X-100 in PBS for 5 minutes. The cells were incubated with anti-TRF-2 Antibody NB110-57130 at 2 ug/ml overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at a 1:1000 dilution for 60 minutes. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.

Flow Cytometry: TRF-2 Antibody [NB110-57130] - An intracellular stain was performed on HeLa cells with TRF-2 Antibody NB110-57130 (blue) and a matched isotype control NBP2-24891 (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1.0 ug/mL for 30 minutes at room temperature, followed by Rabbit IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (SA5-10033, Thermo Fisher).

Chromatin Immunoprecipitation: TRF-2 Antibody [NB110-57130] - Analysis in mouse. Titrated TRF2 antibody to determine concentration required for ChIP experiment. ChIP image submitted by a verified customer review.

<b>Genetic Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: TRF-2 Antibody [NB110-57130] - RNAi-mediated depletion of human separase (ESPL1) induces TIFs. Control scrambled siRNA- (control) and ESPL1 siRNA-treated fibroblasts stained with anti-p53-binding protein 1 (53BP1; green) and anti-TRF2 (red). It is noteworthy that in ESPL1 siRNA-treated cells, 53BP1 signals frequently overlap with TRF2 signals marking the TIFs. Scale bar, 5 um. Image collected and cropped by CiteAb from the following publication (//www.nature.com/doifinder/10.1038/ncomms10405), licensed under a CC-BY license.

Flow Cytometry: TRF-2 Antibody [NB110-57130] - An intracellular stain was performed on HeLa cells with TRF-2 Antibody NB110-57130AF488 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 488.

Telomere deprotection contributes to replication stress lethality. A) Western blots of whole cell extracts from HT1080 6TG cells stably transduced with control, TRF2 shRNA (TRF sh-F) or TRF2 over expression (TRF2OE) vectors. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31530811), licensed under a CC-BY licence.

RNAi-mediated depletion of human separase (ESPL1) induces TIFs.(a) Control scrambled siRNA- (control) and ESPL1 siRNA-treated fibroblasts stained with anti-p53-binding protein 1 (53BP1; green) and anti-TRF2 (red). It is noteworthy that in ESPL1 siRNA-treated cells, 53BP1 signals frequently overlap with TRF2 signals marking the TIFs. Scale bar, 5 um. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26778495), licensed under a CC-BY licence.

$Polyphyllin I triggers PINK1/PARK2-dependent mitophagyA. MDA-MB-231 cells were treated with 8 μM PPI for different periods of time as indicated, and PARK2, P62, and ubiquitin (UB) levels in mitochondrial fractions were determined by western blot. B. Cells were cotransfected with GFP-UB and RFP-mito and treated with 8 μM PPI for 9 h, after which PARK2 (Alexa Fluor 405, pink) and P62 (Alexa Fluor 647, blue) immunostaining was detected using confocal microscopy. C. Cells cotransfected with GFP-UB and RFP-LC3 were treated with 8 μM PPI for 9 h, after which PARK2 (Alexa Fluor 405, pink) and TOMM20 (Alexa Fluor 647, blue) immunostaining was detected using confocal microscopy. Scale bars: 10 μm. D-E. MDA-MB-231 cells were treated with 8 μM PPI for different periods of time as indicated; whole-cell lysates were then separated on 8% SDS-PAGE gels and analyzed by western blot using the anti-PINK1 antibody. Relative full-length (∼63 kDa) and cleaved (∼52 kDa) PINK1 levels were quantified by densitometry and normalized to Tubulin. The results were expressed as a percentage of control, which was set at 100%. Data are presented as mean ± SD (*P< 0.01 vs. the control). F. Cells were treated with 8 μM PPI for different periods of time as indicated, and whole-cell lysates were then subjected to western blot analysis. G. Cells were treated with 8 μM PPI for 9 h, after which mitochondrial fractions were prepared and subjected to immunoprecipitation using anti-PINK1 antibody; associated PARK2 was detected using immunoblotting. H. RFP-mito-expressing MDA-MB-231 cells were treated with 8 μM PPI for 9 h, and PINK1 (Alexa Fluor 488, green) and PARK2 (Alexa Fluor 405, pink) immunostaining were evaluated using confocal microscopy. Scale bars: 10 μm. Image collected and cropped by CiteAb from the following open publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.14413), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

PHD3 depletion stabilizes hypoxic p27 expression by increasing p27 half-life. a Cell cycle arrest at G0 and subsequent release shows an increase of p27 expression in siPHD3 exposed cells. b Quantification for p27 expression under PHD3 depletion at indicated time points after cell cycle release in HeLa and 786-O cells. Asterisk indicates significant difference (p < 0,05; n = 3). c Cell cycle arrest at G0 and inhibition of protein synthesis with cycloheximide indicate increased p27 stability in PHD3 depleted HeLa cells. d Quantification of p27 expression using siPHD3 or control at indicated time points. Four independent experiments (± SEM) are shown (p < 0,05; n = 4). e Analysis of p27 stability in 786–0 cells by cycloheximide chase during reoxygenation after 24 h hypoxia demonstrates markedly increased half-life of p27 upon PHD3 depletion Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/26223520), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunohistochemical staining of HIF-1 alpha , VEGF-A and VEGF-C in normal renal tissue (A-C) and clear cell renal cell carcinoma (CCRCC) (D-F). A homogeneous cytoplasmic staining of tubular cells and weak staining in glomerules was observed with HIF-1 alpha (A), while VEGF-A and VEGF-C were positive in tubular cells, glomerular mesangium and interstitial macrophages (B and C). In CCRCC, HIF-1 alpha immmunoreactivity was nuclear and/or cytoplasmic (D), while it was perimembranous and/or diffuse cytoplasmic for VEGF-A and VEFG-C (E and F). (magnification ×200). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/19302703), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Resistance of FANCA-mutant cells with defective FANCD2 function to hydrogen peroxide (H2O2). (a) Representative images illustrating staining for subnuclear FANCD2 foci in isogenic fibroblast pairs, either deficient for FANCD2 (PD20) or FANCA (PD220) and their respective wild-type (wt) complemented counterparts. Foci were visualized three hours after treatment with H2O2 (25 μM for 2 hours). (b) Clonogenic survival of cells with or without wild-type FANCA after treatment with varying concentrations of H2O2. Datarepresent logarithmic means +/− standard error from 15-repeat experiments. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/18483568), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$gamma -Taxilin ablation causes ER stress responses and apoptosis in normoxic cells. (a) Knockdown of gamma -taxilin expression by small interfering RNA (siRNA) in HeLa S3 cells. Two different siRNA constructs are equally effective. HeLa S3 cells were treated with solvent alone (Mock), control siRNA (Co), or gamma -taxilin siRNA ( gamma -tax-1 or -2) for 96 h. (b) Induction of apoptosis by gamma -taxilin ablation in HeLa S3 cells. gamma -Taxilin ablation causes apoptosis in HeLa S3 cells, but Mock or Co treatment did not. Bar graph shows fractions of annexin-positive cells (means±S.D., n=3). *Significantly different from Mock- or Co treatment (P <0.001, Tukey–Kramer test). (c) Confocal microscopy demonstrates coincidence of gamma -taxilin depletion and apoptotic nuclei in HeLa S3 cells treated with gamma -taxilin siRNA. Scale bar, 10 μm. (d) gamma -Taxilin depletion triggers ER stress responses in HeLa S3 cells. Upper panels, taxilin and NAC proteins; middle panels, UPR proteins; and lower panel, beta -actin. (e) gamma -Taxilin ablation induces accumulation of ubiquitinated proteins in HeLa S3 cells. Cell lysates were analyzed on 7.5% SDS-PAGE, followed by immunoblotting with antibodies specific for anti-mono- and polyubiquitinated conjugates (upper panel) and beta -actin (lower panel) Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/25880086), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

$Damage response is restricted to MG. (A) RT-PCR analysis for Slc1a3, the gene encoding GLAST, at the indicated times after injury. (B) RT-PCR for MG and a photoreceptor-specific marker (Nrl) in GLAST-positive and negative fractions, after MACS in intact retinas. (C–F) qPCR quantification of Oct4, Nanog, Lin28, and Dnmt3b expression levels at the indicated time after injury in MACS GLAST-positive and negative fraction; C, intact retina as control (Student's t-test; ***p < 0.001; **p < 0.01; *p < 0.05). Image collected and cropped by CiteAb from the following open publication (//journal.frontiersin.org/article/10.3389/fnins.2016.00523/full), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Effect of ET-1 and Cx43 on HIF-1 alpha expression and glucose uptake when c-Src is inhibited.Astrocytes were preincubated with 100 ng/µL PP2 (c-Src inhibitor) or 100 ng/µL PP3 (inactive analogue) for 1 h. Then, cells were incubated in the absence (control) or presence of 0.1 µM ET-1 for 24 h. A) HIF-1 alpha Western blot and quantification. The results are expressed as percentages of the level found in the controls treated with PP3 and they show that the inhibitor of c-Src PP2 prevented the up-regulation of HIF-1 alpha promoted by ET-1. ***p<0.001 versus the absence of ET-1. B) Glucose uptake expressed as pmol of 2-deoxyglucose taken up per hour and per milligram of protein. The results show that the inhibitor of c-Src PP2 prevented the increase in the rate of glucose uptake promoted by ET-1. ***p<0.001 versus the absence of ET-1. C) Astrocytes were preincubated with 100 ng/µL PP2 or 100 ng/µL PP3 for 1 h. Then, cells were transfected with NT-siRNA or with Cx43-siRNA and after 48 h HIF-1 alpha was analysed by Western blot. The results are expressed as percentages of the level found in the PP3 NT-siRNA and they show that the inhibitor of c-Src PP2 prevented the up-regulation of HIF-1 alpha promoted by silencing Cx43. ***p<0.001 versus the corresponding NT-siRNA. Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.pone.0032448), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Genotyping of transgenes.PCR genotyping was performed for all four transgenes as described in materials and methods. Sizes of the amplified products obtained are: 240 bp for Hif-1 alpha (wild type); 274 bp for Hif-1 alpha flox/flox; 410 bp for Hif-2 alpha (wild type); 444bp for Hif-2 alpha flox/flox; 370 bpfor Cre transgene; 350 bpfor rtTA transgene. One representative sample was genotyped for the four transgenes from each of three generated mouse strains: SPC-rtTA-/tg/(tetO)7-Cre-/tg/Hif-1 alpha fl/fl (Lane 1), SPC-rtTA-/tg/(tetO)7-Cre-/tg/Hif-2 alpha fl/fl mouse (Lane 2), and SPC-rtTA-/tg/(tetO)7-Cre-/tg/Hif-1 alpha /2 alpha fl/fl (Lane 3)). Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.pone.0139270), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

The expression patterns of Yap and GFAP-Cre recombinase in postnatal mouse eyes. (A) Schematic of a transverse section of mouse eye. (B-C) Immunostaining with anti-Yap antibody (green) on frozen eye sections at different ages. Nuclei were counterstained with DAPI (blue). Yap staining was detected in scattered cells within the INL (arrowheads) and GCL of the retina and the lens epithelium (arrows). (D) Cre recombinase (red) was expressed in the lens epithelium and INL, GCL of retina in frozen eye sections of Tomatof/+; GFAP-Cre mice at P14. Nuclei were counterstained with DAPI (blue). LE, lens epithelium; TZ, transitional zone; RPE, retinal pigment epithelium; OS, outer segment; IS, inner segment; ONL, outer nuclear layer; OPL, outer plexiform layer; INL, inner nuclear layer; IPL, inner plexiform layer; GCL, ganglion cell layer. Scale bars: 25 μm (B-C), 100 μm (D). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31011480), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Representative picture of western blot in histopathologically unchanged tissue (N) and primary cancerous tissue (C) from patients with CRC. Immunodetection of bands was performed with Rp anti- PHD1, - PHD2, - PHD3 and - FIH Ab, followed by incubation with goat anti-rabbit HRP-conjugated Ab. The membrane was stripped and incubated with Rp anti-GAPDH Ab, followed by incubation with goat anti-rabbit HRP-conjugated Ab. Bands were revealed using SuperSignal West Femto Chemiluminescent Substrate, Thermo Fisher Scientific (Rockford, IL) and Biospectrum® Imaging System 500, UVP Ltd. (Upland, CA). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/24195777), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, ChHa, Pm

Species Glossary

Reactivity: Hu, Mu, Rt, ChHa, Pm

Applications:

, , , , , , , , ,

Applications: , , , , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

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Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

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Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB110-57130AF350
Alexa Fluor 405	NB110-57130AF405
Alexa Fluor 488	NB110-57130AF488
Alexa Fluor 532	NB110-57130AF532
Alexa Fluor 594	NB110-57130AF594
Alexa Fluor 647	NB110-57130AF647
Alexa Fluor 700	NB110-57130AF700
Alexa Fluor 750	NB110-57130AF750
Allophycocyanin	NB110-57130APC
Biotin	NB110-57130B
DyLight 350	NB110-57130UV
DyLight 405	NB110-57130V
DyLight 488	NB110-57130G
DyLight 550	NB110-57130R
DyLight 594	NB110-57130DL594
DyLight 650	NB110-57130C
DyLight 680	NB110-57130FR
DyLight 755	NB110-57130IR
FITC	NB110-57130F
HRP	NB110-57130H
Janelia Fluor 549	NB110-57130JF549
Janelia Fluor 646	NB110-57130JF646
PE	NB110-57130PE
PerCP	NB110-57130PCP
mFluor Violet 450 SE	NB110-57130MFV450
mFluor Violet 500 SE	NB110-57130MFV500
mFluor Violet 610 SE	NB110-57130MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB110-57130SS

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NB100-56506

TRF-2 Antibody (4A794.15) - BSA Free

(1 Review)

(114 Publications)

0.1 mg

NB100-56506

Immunohistochemistry-Paraffin: TRF-2 Antibody (4A794.15) [NB100-56506] - Transitional cell carcinoma, urinary bladder, stained with TRF2 antibody (4 ug/mL), peroxidase-conjugate and DAB chromogen. Note specific nuclear staining. Tumor/normal adjacent tissue array slide was used for this test. Staining of formalin-fixed tissues is enhanced by boiling tissue sections in 10 mM sodium citrate buffer, pH 6.0 for 10-20 min followed by cooling at RT for 20 min.

Immunocytochemistry/Immunofluorescence: TRF-2 Antibody (4A794.15) [NB100-56506] - Localization of candidate RNAs at telomeres. Localization of SNORD17 at telomeres in human U-2 OS cells. Cells were fixed and sequentially incubated with Abs against TRF-2 and AlexaFluor 488-conjugated anti-mouse IgG. Subsequently, the cells were hybridized with the RNA probes and subjected to fluorescence microscopy. Three different cells are shown. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0123387), licensed under a CC-BY license.

Flow Cytometry: TRF-2 Antibody (4A794.15) [NB100-56506] - Intracellular flow cytometric analysis of TRF2 in 10^6 human Jurkat cells using 0.1 ug of NB100-56506. The shaded histogram represents cells alone, blue represents isotype control and red represents NB100-56506, anti-TRF2.

Western Blot: TRF-2 Antibody (4A794.15) [NB100-56506] - Total protein from mouse 3T3 cells was separated on a 12% gel by SDS-PAGE, transferred to PVDF membrane and blocked in 5% non-fat milk in TBST. The membrane was probed with 2.0 ug/mL anti-TRF2 in 1% non-fat milk in TBST and detected with an anti-mouse HRP secondary antibody using chemiluminescence.

Immunocytochemistry/Immunofluorescence: TRF-2 Antibody (4A794.15) [NB100-56506] - Localization of candidate RNAs at telomeres. Localization of NEAT1 at telomeres in human U-2 OS cells. Cells were fixed and sequentially incubated with Abs against TRF-2 and AlexaFluor 488-conjugated anti-mouse IgG. Subsequently, the cells were hybridized with the RNA probes and subjected to fluorescence microscopy. Three different cells are shown. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0123387), licensed under a CC-BY license.

Flow Cytometry: TRF-2 Antibody (4A794.15) [NB100-56506] - An intracellular stain was performed on A431 cells with TRF2 Antibody [4A794.15] NB100-56506 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1.0 ug/mL for 30 minutes at room temperature, followed by Mouse IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (35503, Thermo Fisher).

Immunocytochemistry/Immunofluorescence: TRF-2 Antibody (4A794.15) [NB100-56506] - Staining of TRF2-bound telomeres in human HeLa cells (Courtesy of Fotiadou, et al, 2004).

Immunocytochemistry/Immunofluorescence: TRF-2 Antibody (4A794.15) [NB100-56506] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X PBS + 0.5% Triton-X100. The cells were incubated with anti-TRF-2 (4A794.15) conjugated to FITC [NB100-56506F] at 5 ug/mL for 1 hour at room temperature. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

TRF2deltaBdeltaM expression induces chromosome end-to-end fusions in all inducible cell lines. (A) Immunoblots of MCF-10A, TO, SH-TO and SV-TO cell lines with and without DOX and HEK 293T. After 96 h of DOX treatment, the inducible cell lines expressed the truncated TRF2deltaBdeltaM protein (50 kDa); in contrast, uninduced cell lines, MCF-10A parental cell line and HEK 293T cells displayed only the endogen TRF2 protein (66 kDa). Lamin B1 was used as loading control. Image collected and cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.25502), licensed under a CC-BY licence.

HIF protein stabilization and HIF-1 alpha transcriptional activityRepresentative western blot showing protein levels of HIF-1 alpha and HIF-2 alpha (n = 3) in (A) cardiomyocytes derived from R1 and R1HIF-1 alpha −/− mESC exposed to 1% O2 and (B) cardiomyocytes derived from HG8 mESC exposed to 1% O2 and DMOG. Cropped representative western blots are shown from total of n = 3. mRNA levels of (C) Glut1 and (D) VEGF in cardiomyocytes derived from HG8 mESC exposed to 1% O2 or DMOG determined by qRT-PCR (n = 3). Data are presented as 2− delta Cq ± SEM (groups were compared using one-way ANOVA with the Tukey (HSD) post hoc test *p < 0.05). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/29137374), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Acetaldehyde toxicity to human FANCD2‐deleted human cells and FANCD2 ubiquitylation in BRCA2‐deleted cellsA, BHuman DLD1 cells in which FANCD2 was deleted with CRISPR/Cas9 and control cells were incubated with the indicated concentrations of cisplatin (A) or acetaldehyde (B) for 6 days before processing for dose‐dependent viability assays. Graphs are representative of two independent experiments, each performed in triplicate. Error bars represent SD of triplicate values obtained from a single experiment. Inset, Western blot detection of FANCD2 expression. SMC1 was used as a loading control.CBRCA2‐proficient (+BRCA2) or BRCA2‐deficient (−BRCA2) DLD1 cells were incubated with 4 mM acetaldehyde for 48 h before being processed for immunoblotting as indicated.DH1299 cells expressing a DOX‐inducible BRCA2 shRNA were grown in the presence or absence of DOX and transfected with control or FANCD2 siRNA before being processed for immunoblotting as indicated. DOX, doxycycline. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/28729482), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

KDM4A interacts with the mTORC1/2 complex.(a) Relative mRNA levels of negative and positive regulators of the PTEN/AKT/mTOR pathway following KDM4A depletion. Quantifications of mRNAs by RT–qPCR were normalized against beta -actin (ActB) mRNA. Asterisks denote a statistical difference between siKDM4A-treated cells and siGFP control cells, two-sided t-test P<0.05 (graph represents two independent experiences). Error bars represent standard deviation. (b) Co-immunoprecipitation of endogenous mTORC1/2 complex members with Flag-KDM4A in 293T transfected cells. (c) Comparison of mTORC1/2-associated proteins with Flag-tagged mTOR or KDM4A. The 293T cells were transfected with either Flag-eYFP, Flag-KDM4A or Flag-mTOR, and protein lysates were subjected to anti-Flag immunoprecipitation. (d) Co-immunoprecipitation of Flag-KDM4A and HA-DEPTOR in 293T cells. (e) Endogenous KDM4A co-immunoprecipitates with Flag-DEPTOR. (f) DEPTOR PDZ domain associates with endogenous KDM4A. Flag immunoprecipitation of flag-tagged full length or fragments of DEPTOR. The samples were not sonicated in this experiment to confirm that the interaction is independent of nucleus disruption. (g) Endogenous KDM4A and DEPTOR associate in 293E cells. (h) Endogenous KDM4A and DEPTOR co-immunoprecipitate in NHA-hTERT cells. Image collected and cropped by CiteAb from the following open publication (//www.nature.com/articles/ncomms12700), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Ma, Mar

Species Glossary

Reactivity: Hu, Mu, Rt, Ma, Mar

Applications:

, , , , , , , , , ,

Applications: , , , , , , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Alt Catalog#

IMG-124A

Alt Catalog# IMG-124A

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB100-56506AF350
Alexa Fluor 405	NB100-56506AF405
Alexa Fluor 488	NB100-56506AF488
Alexa Fluor 532	NB100-56506AF532
Alexa Fluor 594	NB100-56506AF594
Alexa Fluor 647	NB100-56506AF647
Alexa Fluor 700	NB100-56506AF700
Alexa Fluor 750	NB100-56506AF750
Allophycocyanin	NB100-56506APC
Biotin	NB100-56506B
DyLight 350	NB100-56506UV
DyLight 405	NB100-56506V
DyLight 488	NB100-56506G
DyLight 550	NB100-56506R
DyLight 594	NB100-56506DL594
DyLight 650	NB100-56506C
DyLight 680	NB100-56506FR
DyLight 755	NB100-56506IR
FITC	NB100-56506F
HRP	NB100-56506H
Janelia Fluor 549	NB100-56506JF549
Janelia Fluor 646	NB100-56506JF646
PE	NB100-56506PE
PerCP	NB100-56506PCP
mFluor Violet 450 SE	NB100-56506MFV450
mFluor Violet 500 SE	NB100-56506MFV500
mFluor Violet 610 SE	NB100-56506MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-56506SS
Azide Free	NBP2-33212

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NB300-232

SCP3/SYCP3 Antibody - BSA Free

(2 Reviews)

(78 Publications)

0.1 ml

NB300-232

Immunocytochemistry/Immunofluorescence: SCP3/SYCP3 Antibody [NB300-232] - Exposure to DEHP impairs meiotic progression of oocytes from pachytene to diplotene. Immunolabeling of the oocyte chromosomes with anti-SYCP3 antibody (red) and Hoechst 33342 (blue). All experiments were repeated at least three times independently. (* P<0.05; ** P<0.01) Image collected and cropped by CiteAb from the following publication (//www.nature.com/doifinder/10.1038/cddis.2017.350), licensed under a CC-BY license.

Immunocytochemistry/Immunofluorescence: SCP3/SYCP3 Antibody [NB300-232] - Loss of lamin C2 has no effect on meiotic telomere attachment. Chromosome spread preparations of pachytene-like lamin C2-/- spermatocytes showing that all telomeres are associated with SUN1. Anti-SUN1 staining in co-localisation with SYCP3. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pgen.1003261), licensed under a CC-BY license.

Western Blot: SCP3/SYCP3 Antibody [NB300-232] - SCP3 Antibody [NB300-232] - Analysis of SCP3 in mouse testis protein.

Immunohistochemistry-Paraffin: SCP3/SYCP3 Antibody [NB300-232] - Analysis of SCP3 in human testis using DAB with hematoxylin counterstain.

Immunocytochemistry/Immunofluorescence: SCP3/SYCP3 Antibody [NB300-232] - SCP3 Antibody [NB300-232] - SCP3 labeled in mouse pachytene preparation (red), using NB300-232 SCP3 antibody. CDK2 staining, near teleomeres, is also present (green).

Immunohistochemistry-Paraffin: SCP3/SYCP3 Antibody [NB300-232] - IHC-P analysis of formalin fixed paraffin embedded tissue section of mouse testes using SCP3 antibody at 1:200 dilution. Specific staining may be seen in the spermatogonial cells and the primary spermatocytes.

CYP51 regulates the expression of the meiosis-specific cohesin subunits REC8 and STAG3. (A,B) RS21745 treatment decreased REC8 and STAG3 expression. Ovaries at 14.5 dpc were cultured with 10 uM RS21745 for 3 days in vitro. (A) Expression of the cohesin subunits following RS21745 treatment by qRT-PCR. All qRT-PCR values were normalized to beta-actin and were expressed as a relative ratio to the control; the means+/-s.e.m. of 3 values are shown. (B) Expression of REC8 and STAG3 following RS21745 treatment by western blotting GAPDH was used as internal reference. (C-F) Inhibition of CYP51 disturbed the distribution of both REC8 and STAG3 on the chromosomes. (C,E) In the control groups, REC8 and STAG3 expression was observed at high levels in zygotene oocytes. In the CYP51 inhibition groups, the cohesin signals were absent in zygotene cells. (D,F) The percentage of REC8-positive or STAG3-positive oocytes at the zygotene stage was recorded. Unidentified germ cells were not included in the analyses. Scale bars: 10 um. The data are presented as the means+/-s.e.m. of 3-9 ovaries per group. Asterisk (*) denotes a statistically significant difference between the control and the treatment groups. ***P<0.001 (t-test). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30420384), licensed under a CC-BY licence.

Exposure to DEHP impairs meiotic progression of oocytes from pachytene to diplotene. (a) Immunolabeling of the oocyte chromosomes with anti-SYCP3 antibody (red) and Hoechst 33342 (blue). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28771232), licensed under a CC-BY licence.

Dose-dependent decrease or increase of the number of meiotic germ cells (SCP3, MLH1) and of gammaH2AX positive cell, respectively, in nicotine treated fetal ovaries cultured for 4 days. (A) Representative IF images of ovarian tissue sections for SCP3. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30001218), licensed under a CC-BY licence.

Induction of meiosis is compromised in the cortical germ cells of D17 embryos subject to oestrogen level alterations. (B) Sections from the D17 (HH43) left gonad shown in A immunostained for gammaH2AX (green) and SYCP3 (red). ZW-WT, ZW wild type; ZW-Fa, ZW treated with fadrozole from D7-7.5 (HH31); ZW-E2, ZW treated with beta-oestradiol at D7-7.5; ZZ-E2, ZZ treated with beta-oestradiol at D7-7.5; ZW-Fa(sr), ZW, partially sex-reversed gonad, treated with fadrozole at D4; ZZ-E2(sr), ZZ, partially sex-reversed gonad, treated with beta-oestradiol at D4. All gonadal models have a cortical domain containing germ cells. In ZW-Fa ovary and ZW-E2 ovary, most cortical germ cells express SYCP3 like the ZW-WT control. In ZW-Fa(sr) ovotestis, very few germ cells express gammaH2AX and SYCP3 (orange dotted circled areas). In ZZ-E2(sr) ovotestis and ZZ-E2 testis overlain by a cortex, some cortical germ cells express gammaH2AX but none expresses SYCP3. White dotted line highlights the cortical domain borders. See Fig. S4 for the medullary structure of the ZZ-E2, ZW-Fa(sr) and ZZ-E2(sr) models. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32001442), licensed under a CC-BY licence.

NSCs Reduce Succinate Levels and Reprogram the Metabolism of Type 1 Pro-inflammatory Mφ toward Oxidative Phosphorylation In Vitro(A) Experimental setup for in vitro MφLPS co-cultures with iNSCs/NSCs.(B and C) Gene expression microarrays of MφLPS-iNSCs/NSCs. (B) Venn diagram of differentially expressed genes (adjusted p value < 0.1). (C) Heatmap of genes differentially expressed (adjusted p value < 0.1) in MφLPS-iNSCs or MφLPS-NSCs.(D and E) qRT-PCR independent validation of differentially expressed inflammatory genes as in (C). (D) Expression of genes related to type 1 inflammatory (E) and anti-inflammatory Mφ phenotypes relative to Actb. Data are mean fold change (±SEM) versus MφLPS from n ≥ 3 independent replicates per condition.(F) qRT-PCR of BV2LPS-iNSCs/NSCs (±SEM) from n ≥ 3 independent experiments per condition. BV2 and BV2LPS are shown as controls.(G and H) Extracellular flux (XF) assay of the oxygen consumption rate (OCR) (G) and extracellular acidification rate (ECAR) (H) in MφLPS-iNSCs/NSCs. Data were normalized on total protein content and are expressed as mean values (±SEM) from n ≥ 3 independent experiments per condition.(I and J) Levels of significantly changed extracellular (EXTRA_Metab, I) and intracellular (INTRA_Metab, J) metabolites in MφLPS versus Mφ at 25 hr. Data are mean a.u. (±SEM) from n ≥ 2 independent experiments per condition.(K and L) Hif-1 alpha (K), PKM2 (K), and IL-1 beta (L) expression levels relative to beta -actin. Data are mean fold change versus MφLPS (±SEM) from n ≥ 3 independent experiments per condition.∗p ≤ 0.05 and ∗∗p ≤ 0.01 versus MφLPS. See also Tables S2 and S3. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/29478844), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Lp(a) upregulates GPx1 and Prdx6 expression in human HepG2 cells. HepG2 cells were treated with 5 μg/mL of Lp(a) or LDL for 6 hours at 37°C. Western blots of cell lysates were performed with an anti-Gpx1 antibody (a), an anti-Prdx6 antibody (b), an anti-Sod1 antibody (c), and an anti-Park7 antibody (d) using an anti-actin antibody as a loading control. Representative blots are shown. Protein levels were normalized against actin and expressed relative to that of untreated cells. Results are expressed as mean ± SEM for pooled triplicate incubations run in quadruplicate. ∗P<0.05, relative to untreated HepG2 cells. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/30596094), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Metformin-mediated AMPK activation is involved in suppression of TGF-beta -induced NOX4 expression in LF. a WB using anti-NOX4, and anti-beta -actin of cell lysates from control (lane 1, 2) and metformin (lane 3, 4) treated LF. Metformin treatment was started 1 h before TGF-beta (2 ng/ml) stimulation and protein samples were collected after 24 h treatment with TGF-beta . Lower panel is the average (±SEM) taken from three independent experiments shown as relative expression. Open bar is control and filled bar is metformin treated. *p < 0.05. b Left panel: LF were treated with TGF-beta and mRNA samples were collected at indicated time points (n = 9). *p < 0.05. Right panel: LF were treated with TGF-beta in the presence or absence of metformin (10 mM) and mRNA samples were collected after 12 h treatment with TGF-beta (n = 6). Open bar is control and filled bar is metformin treated. Real time-PCR was performed using primers to NOX4 or beta -actin, as a control. NOX4 expression was normalized to beta -actin. Shown is the fold increase (±SEM) relative to control treated cells. *p < 0.05. c WB using anti-NOX4, anti-type I collagen, anti-alpha -smooth muscle actin (SMA) and anti-beta -actin of cell lysates from control siRNA (lane 1, 2) and NOX4 siRNA (lane 3, 4) transfected LF. TGF-beta (2 ng/ml) treatment was started 48 h post transfection. Protein samples were collected after 24 h treatment with TGF-beta . In the right panels are the average (±SEM) taken from four independent experiments shown as relative expression. Open bar is control and filled bar is TGF-beta treated. *p < 0.05. d WB using anti-phospho-AMPK, anti-NOX4, anti-type I collagen, anti-alpha SMA, and anti-beta -actin of cell lysates from control siRNA (lane 1, 2, 3, 4) and AMPK siRNA (lane 5, 6) transfected LF. Metformin treatment was started 48 h post transfection and 1 h before TGF-beta (2 ng/ml) stimulation, and protein samples were collected after 24 h treatment with TGF-beta . In the right panels are the average (±SEM) taken from five independent experiments shown as relative expression. Open bar is control and filled bar is TGF-beta treated. *p < 0.05 Image collected and cropped by CiteAb from the following open publication (//respiratory-research.biomedcentral.com/articles/10.1186/s12931-016-0420-x), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Bv, Ch, Fe, Pa

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Bv, Ch, Fe, Pa

Applications:

, , , ,

Applications: , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB300-232AF350
Alexa Fluor 405	NB300-232AF405
Alexa Fluor 488	NB300-232AF488
Alexa Fluor 532	NB300-232AF532
Alexa Fluor 594	NB300-232AF594
Alexa Fluor 647	NB300-232AF647
Alexa Fluor 700	NB300-232AF700
Alexa Fluor 750	NB300-232AF750
Allophycocyanin	NB300-232APC
Biotin	NB300-232B
DyLight 350	NB300-232UV
DyLight 405	NB300-232V
DyLight 488	NB300-232G
DyLight 550	NB300-232R
DyLight 594	NB300-232DL594
DyLight 650	NB300-232C
DyLight 680	NB300-232FR
DyLight 755	NB300-232IR
FITC	NB300-232F
HRP	NB300-232H
Janelia Fluor 549	NB300-232JF549
Janelia Fluor 646	NB300-232JF646
PE	NB300-232PE
PerCP	NB300-232PCP
mFluor Violet 450 SE	NB300-232MFV450
mFluor Violet 500 SE	NB300-232MFV500
mFluor Violet 610 SE	NB300-232MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB300-232SS

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NB300-229

SCP1 Antibody - BSA Free

(3 Reviews)

(54 Publications)

0.1 ml

NB300-229

Immunocytochemistry/Immunofluorescence: SCP1 Antibody - BSA Free [NB300-229] - Double immunofluorescence of testicular spread preparations of the adult mice, SYCP3 (green) and SCP1 (red). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32081844/) licensed under a CC-BY license.

Immunohistochemistry-Paraffin: SCP1 Antibody [NB300-229] - Punctate staining of murine SCP1 in mouse ovary using NB300-229.

Immunocytochemistry/Immunofluorescence: SCP1 Antibody [NB300-229] - SCP1 labeled in mouse pachytene preparation (red), using NB300-229. CDK2 staining, near teleomeres, is also present (green).

Immunocytochemistry/Immunofluorescence: SCP1 Antibody [NB300-229] - Spermatocytes cells fixed in PFA. Detected with anti-mouse 594. ICC/IF image submitted by a verified customer review.

Immunocytochemistry/Immunofluorescence: SCP1 Antibody [NB300-229] - Mouse spermatozoa. Green: SCP1 staining. ICC/IF image submitted by a verified customer review.

Immunocytochemistry/Immunofluorescence: SCP1 Antibody [NB300-229] - Mouse spermatocyte. Red: scp1 colocalized with scp3 (green). ICC/IF image submitted by a verified customer review.

Immunocytochemistry/Immunofluorescence: SCP1 Antibody - BSA Free [NB300-229] - Immunostaining of SCP3/SYCP3 (NB300-231) and SCP1 on adult Cxxc1 het and CKO chromosome spreads. Green, SCP3/SYCP3; orange, SCP1. Scale bar, 10 um. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30365547/) licensed under a CC-BY license.

Meiotic progression and chromosome paring in XX, XO and XY oocytes. (B) Pairing of homologous chromosomes in XX, XO and XY oocytes. Images show the immunofluorescence analysis of SYCP3 (white) and SYCP1 (red), and FISH analysis of the X chromosome (green) and Y chromosome (purple). The dashed squares in the merged images are shown at high magnification (right). The numbers of samples showing the phenotype are shown with the total number tested (left). Arrowheads indicate asynapsed bivalents at the end of the chromosomes. Scale bars, 10 um. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32214314), licensed under a CC-BY licence.

Meiotic spreads.Meiotic chromosome spreads from wild type and Fance mutant (MT) primary spermatocytes isolated from the testes at 20 dpp. Each chromatin spread was staged by analyzing SYCP3 (red) and SYCP1 (green), which are axial element and central region components of the synaptonemal complex respectively. Most of the Fance mutant spermatocytes displayed normal synapsis (middle panels); however a sub-set displayed synapsis abnormalities including an association between non-homologous chromosome ends (arrow head) and abnormal SYCP3 structures (arrows). Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0159800), licensed under a CC-BY licence.

$hIAPP upregulates the HIF1 alpha /PFKFB3 stress pathway. a Summary of the differentially expressed genes of interest after microarray analysis25 performed on RNA isolated from wild type (WT) and hIAPP overexpressing (HIP) rat islets (4.5 months) presented as a fold change over WT. Asterisk represents genes that were differentially expressed in one experiment. b LDHA and MCT1 mRNA levels in HIP versus WT as measured by qRT-PCR. c Lactate production rate (fold change) measured in isolated islets from HIP relative to WT. d Representative Western blot of PFKFB3 and HIF1 alpha protein levels in whole cell extracts and nuclear-enriched fractions of islets from 6 months old WT (3) and HIP (3) rats. GAPDH and PARP were used as loading controls for whole cell extract (WCE) and nuclear extracts, respectively. e Quantification of HIF1 alpha (upper panel) and PFKFB3 (lower panel) in cytoplasmic and nuclear fractions. Data are presented as mean ± SEM, n = 3 independent experiments for (b) and (d), and n = 4 independent experiments for (c). Statistical significance was analyzed by Student t-test (*p < 0.05, **p < 0.01) Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31213603), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

PRDX proteins bind to HIF-1 alpha and HIF-2 alpha A. HeLa cells were transfected with an expression vector encoding V5-epitope-tagged PRDX2 (PRDX2-V5) and exposed to 1% O2 for 24 h. Whole cell lysate (WCL) was subject to immunoprecipitation (IP) using anti-HIF-1 alpha antibody or control IgG, followed by immunoblot assays with antibody against V5 epitope or HIF-1 alpha . B. HeLa cells were transfected with PRDX2-V5 vector and exposed to 1% O2 for 24 h. The WCL was subject to IP using anti-V5 antibody or control IgG, followed by immunoblot assays with antibody against V5 or HIF-1 alpha . Light IgG: immunoglobulin light chain from the secondary antibody. C. HeLa cells were transfected with vector encoding a V5-tagged PRDX family member and exposed to 1% O2 for 24 h. WCL was subject to IP using anti-HIF-1 alpha antibody, followed by immunoblot assays with antibody against V5 or HIF-1 alpha . D. HeLa cells were transfected with empty vector (EV) or vector encoding a V5-tagged PRDX family member and exposed to 1% O2 for 24 h. WCL was subject to IP using anti-HIF-2 alpha antibody, followed by immunoblot assays with antibody against V5 or HIF-2 alpha . Image collected and cropped by CiteAb from the following open publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.7142), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

MRE11 associates with the DS region of OriP.A) DNA affinity purification assays were performed with Raji nuclear extracts and DNA templates derived from DS wt, DS nm-, or delta DS. Input and template bound proteins were analyzed by Western blot with antibodies to TRF2, MRE11, EBNA1, PCNA, and PARP1, as indicated. B) Schematic of template DNA used for DNA affinity purification in A, and their respective protein binding sites. C) ChIP assays to monitor EBNA1, TRF2, and MRE11 binding at OriP wt or OriP nm- in transfected 293 cells. Immunoprecipitated DNA was quantified by real time PCR relative to total input DNA recovered for each transfected cell. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/18040525), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Mu, Rt, Ch, Ma, Pa, Pm, Hu(-)

Species Glossary

Reactivity: Mu, Rt, Ch, Ma, Pa, Pm, Hu(-)

Applications:

, , , , , ,

Applications: , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB300-229AF350
Alexa Fluor 405	NB300-229AF405
Alexa Fluor 488	NB300-229AF488
Alexa Fluor 532	NB300-229AF532
Alexa Fluor 594	NB300-229AF594
Alexa Fluor 647	NB300-229AF647
Alexa Fluor 700	NB300-229AF700
Alexa Fluor 750	NB300-229AF750
Allophycocyanin	NB300-229APC
Biotin	NB300-229B
DyLight 350	NB300-229UV
DyLight 405	NB300-229V
DyLight 488	NB300-229G
DyLight 550	NB300-229R
DyLight 594	NB300-229DL594
DyLight 650	NB300-229C
DyLight 680	NB300-229FR
DyLight 755	NB300-229IR
FITC	NB300-229F
HRP	NB300-229H
Janelia Fluor 549	NB300-229JF549
Janelia Fluor 646	NB300-229JF646
PE	NB300-229PE
PerCP	NB300-229PCP
mFluor Violet 450 SE	NB300-229MFV450
mFluor Violet 500 SE	NB300-229MFV500
mFluor Violet 610 SE	NB300-229MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB300-229SS

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NB600-506

alpha Tubulin Antibody (YL1/2) - BSA Free

(4 Reviews)

(53 Publications)

0.1 ml

NB600-506

Immunocytochemistry/Immunofluorescence: alpha Tubulin Antibody (YL1/2) [NB600-506] - NIH3T3 cells were fixed and permeabilized for 10 minutes with -20C MeOH. The cells were incubated with alpha Tubulin Antibody [YL1/2] (NB600-506) at 1ug/ml overnight at 4C and detected with an anti-rat DyLight 488 (Green) at a 1:1000 dilution for 60 minutes. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.

Immunocytochemistry/Immunofluorescence: alpha Tubulin Antibody (YL1/2) [NB600-506] - Rat FR cells were fixed and permeabilized for 10 minutes with -20C MeOH. The cells were incubated with alpha Tubulin Antibody [YL1/2] (NB600-506) at 1ug/ml overnight at 4C and detected with an anti-rat DyLight 488 (Green) at a 1:1000 dilution for 60 minutes. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.

Western Blot: alpha Tubulin Antibody (YL1/2) [NB600-506] - Total protein from human HeLa, mouse 3T3, rat PC12 and African green monkey Cos7 cell lines was separated on a 12% gel by SDS-PAGE, transferred to PVDF membrane and blocked in 5% non-fat milk in TBST. The membrane was probed with a 1:6000 dilution of anti-Tubulin (YL 1/2) in 1% non-fat milk in TBST and detected with an anti-rat HRP secondary antibody using chemiluminescence. Alpha tubulin molecular weight: 50 kDa.

Immunohistochemistry-Paraffin: alpha Tubulin Antibody (YL1/2) [NB600-506] - Tubulin antibody was tested in human breast cancer xenograft using DAB with hematoxylin counterstain.

Flow Cytometry: alpha Tubulin Antibody (YL1/2) [NB600-506] - An intracellular stain was performed on PC12 cells with Tubulin [YL1/2] Antibody NB600-506AF488 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 488.

Western Blot: alpha Tubulin Antibody (YL1/2) [NB600-506] - Tissue levels of VEGF and PCNA.VEGF levels were estimated by western blot. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0112995), licensed under a CC-BY license.

Western Blot: alpha Tubulin Antibody (YL1/2) [NB600-506] - Western blot analysis of alpha Tubulin (molecular weight: 50 kDa) expression in 1) HeLa, 2) NTERA-2, 3) A431, 4) HepG2, 5) MCF7, 6) NIH-3T3, 7) PC-12 and 8) Cos 7 whole cell lysates using NB600-506.

Western Blot: alpha Tubulin Antibody (YL1/2) [NB600-506] - Western Blot analysis of whole cell lysates of HeLa, NIH-3T3 and PC-12 cell lines using Tubulin antibody (clone YL1/2). Alpha tubulin molecular weight: 50 kDa.

Immunocytochemistry/Immunofluorescence: alpha Tubulin Antibody (YL1/2) [NB600-506] - Tubulin YL1/2 antibody was tested in HeLa cells with Dylight 550 (red). Nuclei were counterstained with DAPI (blue).

Immunocytochemistry/Immunofluorescence: alpha Tubulin Antibody (YL1/2) [NB600-506] - B-Tubulin staining (488) and Pericentrin (594) in Mitotic Cell. Image from verified customer review.

Immunocytochemistry/Immunofluorescence: alpha Tubulin Antibody (YL1/2) [NB600-506] - IF Confocal analysis of NIH/3T3 cells using Tubulin antibody (NB600-506, 1:5). An Alexa Fluor 488-conjugated Goat to rat IgG was used as secondary antibody (green). Actin filaments were labeled with Alexa Fluor 568 phalloidin (red). DAPI was used to stain the cell nuclei (blue).

Immunocytochemistry/Immunofluorescence: alpha Tubulin Antibody (YL1/2) [NB600-506] - HeLa cells were fixed and permeabilized for 10 minutes using -20C MeOH. The cells were incubated with anti-Tubulin (YL1/2) at a 1:200 dilution overnight at 4C and detected with an anti-rat Dylight 488 (Green) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

Flow Cytometry: alpha Tubulin Antibody (YL1/2) [NB600-506] - Analysis of Alexa Fluor (R) 647 conjugate of NB600-506. An intracellular stain was performed on HeLa cells with Tubulin antibody (YL1/2) NB600-506AF647 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 647.

Flow Cytometry: alpha Tubulin Antibody (YL1/2) [NB600-506] - An intracellular stain was performed on NIH3T3 cells with Tubulin [YL1/2] Antibody NB600-506AF488 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 488.

Induction of HIF-1 alpha in mouse and human brain tissue samples from pneumococcal meningitis. a Immunohistochemistry of brain tissue 36 h post-S. pneumoniae infection in intracerebrally infected mouse model shows positive HIF-1 alpha in several inflammatory and neural cells. b Zoomed area from a in the cortex region of the infected mouse brain shows significant nuclear HIF-1 alpha (black arrows) indicating its activation along with positive staining in the granulocytic infiltrate. c Non-infected hemisphere of the same mouse at 36 h post infection shows no specific staining for HIF-1 alpha signal. d Positive staining in the cortex region (black arrows) was also observed at 24 h post-intracerebral infection, which was also observed at e 48 h post-infection in the intracisternally infected mice. f Control mice that were intracerebrally injected with 0.9% NaCl did not show any positive staining in the same region. g Brain sections from human pneumococcal meningitis patients double stained for HIF-1 alpha (brown) and GFAP (red) show nuclear staining for HIF-1 alpha (black arrows) in lymphocytes of the inflammatory infiltrate (g, left) and in the edematous brain tissue comprising GFAP positive reactive astrocytes (g, right), where macrophages showed cytoplasmic staining (black circles). h Neurons labeled with MAP2 (red) were also co-stained with HIF-1 alpha (brown) in the cortex but mostly the pyknotic ones and not the vital neurons (black circles). i Positive HIF-1 alpha staining could also be observed in vessel associated cells in the cortex region. j Activated HIF-1 alpha indicated by nuclear staining (red) could be observed in brains ECs from pneumococcal meningitis patients by immunofluorescence staining using CD31 as an endothelial marker. Scale bar b–f is 20 µm, g–i is 25 µm, j left most image 20 µm and the zoomed images 10 µm. Mouse brain stainings are representative of three mice each at 24, 36, 48 h post-infection and two control mice at 48 h post- vehicle injection. Human pneumococcal meningitis stainings are representative of 4 cases outlined in Table 1 Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/32529267), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Cell cycle block under PHD3 depletion is accompanied by p27 induction. a PHD3 depletion induces a cell cycle block in G0/G1. HeLa and renal cell adenocarcinoma cells (786-O) were transfected with control (siScr) or PHD3 targeted (siPHD3) siRNA followed by synchronization at G0 and 24-h hypoxic exposure. Cell cycle progression was monitored by FACS analysis 8 h after cell cycle release. The combined means of three independent experiments are presented (±SEM) shown in the tables below. b PHD3 depletion induces p27 expression in HeLa cells and in 786-O cells under hypoxia (1 % O2) and normoxia (21 % O2) by siPHD3 and independent adenoviral shRNA against PHD3. p21 or p16 expression is not elevated by PHD3 knockdown. c Depletion of either PHD1 or PHD2 by siRNA does not increase p27 expression in 786-O cells Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/26223520), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Requirement of Sec16A and p115 for optimal type I IFN innate immune response in cells exposed to cytosolic DNA and RNA sensor ligands.(A–D) HeLa cells were transfected with nonsilencing (Ns) RNA duplexes or two different sets of siRNA duplexes that specifically target p115 or Sec16A as indicated. 72 h post-transfection, cells were left untreated (Ctl) or stimulated with poly I:C (2.5 µg/ml), poly dA:dT (1 µg/ml) or SeV (200 HAU/ml) for 6 h to 8 h. RNA was extracted and analyzed by RT-qPCR using primers for ifn beta , ifit1, oas1. Data are means +/− S.D. (n = 3). * Significantly below the induction response; * P<0.05, ** P<0.01, *** P<0.001. (B and D) Cellular extracts were also prepared and subjected to immunoblot analysis using indicated antibodies. One of three independent experiments with similar results is shown. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/22792062), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Av, Ce, Dr, In, Ma, Pm, Pm, Ye

Species Glossary

Reactivity: Hu, Mu, Rt, Av, Ce, Dr, In, Ma, Pm, Pm, Ye

Applications:

, , , , , ,

Applications: , , , , , ,

Host:

Rat Monoclonal

Host: Rat Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB600-506AF350
Alexa Fluor 405	NB600-506AF405
Alexa Fluor 488	NB600-506AF488
Alexa Fluor 532	NB600-506AF532
Alexa Fluor 594	NB600-506AF594
Alexa Fluor 647	NB600-506AF647
Alexa Fluor 700	NB600-506AF700
Alexa Fluor 750	NB600-506AF750
Allophycocyanin	NB600-506APC
Biotin	NB600-506B
DyLight 350	NB600-506UV
DyLight 405	NB600-506V
DyLight 488	NB600-506G
DyLight 550	NB600-506R
DyLight 594	NB600-506DL594
DyLight 650	NB600-506C
DyLight 680	NB600-506FR
DyLight 755	NB600-506IR
FITC	NB600-506F
HRP	NB600-506H
Janelia Fluor 549	NB600-506JF549
Janelia Fluor 646	NB600-506JF646
PE	NB600-506PE
mFluor Violet 450 SE	NB600-506MFV450
mFluor Violet 500 SE	NB600-506MFV500
mFluor Violet 610 SE	NB600-506MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB600-506SS
Azide and BSA Free	NBP2-80571

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NB200-103

p53 Antibody (PAb 240) - BSA Free

(3 Reviews)

(39 Publications)

0.1 ml

NB200-103

Flow Cytometry: p53 Antibody (PAb 240) [NB200-103] - An intracellular stain was performed on HeLa cells with p53 Antibody [PAb 240] NB200-103 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1.0 ug/mL for 30 minutes at room temperature, followed by Mouse IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (35503, Thermo Fisher).

Immunocytochemistry/Immunofluorescence: p53 Antibody (PAb 240) [NB200-103] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.5% Triton X-100. The cells were incubated with anti-p53 (PAb 240) [NB200-103] at a 1:200 dilution overnight at 4C and detected with an anti-mouse DyLight 488 (Green) at a 1:500 dilution. Actin was detected with Phalloidin 568 (Red) at a 1:200 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

Immunocytochemistry/Immunofluorescence: p53 Antibody (PAb 240) [NB200-103] - HeLa cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.5% Triton X-100 in PBS for 5 minutes. The cells were incubated with anti-p53 Antibody (PAb 240) NB200-103 at 2 ug/ml overnight at 4C and detected with an anti-mouse Dylight 488 (Green) at a 1:1000 dilution for 60 minutes. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.

Immunocytochemistry/Immunofluorescence: p53 Antibody (PAb 240) [NB200-103] - Neuro2a cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.5% Triton X-100 in PBS for 5 minutes. The cells were incubated with anti-p53 Antibody (PAb 240) NB200-103 at 2 ug/ml overnight at 4C and detected with an anti-mouse Dylight 488 (Green) at a 1:1000 dilution for 60 minutes. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.

Flow (Intracellular): p53 Antibody (PAb 240) [NB200-103] - An intracellular stain was performed on HeLa cells with p53 (PAb240) NB200-103 (blue) and a matched isotype control NBP2-27287 (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature, followed by APC-conjugated anti-mouse IgG secondary antibody F0101B.

Flow Cytometry: p53 Antibody (PAb 240) [NB200-103] - An intracellular stain was performed on HeLa cells with p53 (PAb240) NB200-103AF647 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 647.

Flow Cytometry: p53 Antibody (PAb 240) [NB200-103] - An intracellular stain was performed on A549 cells with p53 (PAb240) NB200-103AF488 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 10 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 488.

Flow Cytometry: p53 Antibody (PAb 240) [NB200-103] - An intracellular stain was performed on MCF7 cells with p53 [PAb 240] Antibody NB200-103AF647 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 647.

Flow Cytometry: p53 Antibody (PAb 240) [NB200-103] - An intracellular stain was performed on Neuro2a cells with p53 Antibody [PAb 240] NB200-103 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1.0 ug/mL for 30 minutes at room temperature, followed by Mouse IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (35503, Thermo Fisher).

Reactivity:

Hu, Mu, Rt, Ye, Xp(-)

Species Glossary

Reactivity: Hu, Mu, Rt, Ye, Xp(-)

Applications:

, , , , , ,

Applications: , , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB200-103AF350
Alexa Fluor 405	NB200-103AF405
Alexa Fluor 488	NB200-103AF488
Alexa Fluor 532	NB200-103AF532
Alexa Fluor 594	NB200-103AF594
Alexa Fluor 647	NB200-103AF647
Alexa Fluor 700	NB200-103AF700
Alexa Fluor 750	NB200-103AF750
Allophycocyanin	NB200-103APC
Biotin	NB200-103B
DyLight 350	NB200-103UV
DyLight 405	NB200-103V
DyLight 488	NB200-103G
DyLight 550	NB200-103R
DyLight 594	NB200-103DL594
DyLight 650	NB200-103C
DyLight 680	NB200-103FR
DyLight 755	NB200-103IR
FITC	NB200-103F
HRP	NB200-103H
Janelia Fluor 549	NB200-103JF549
Janelia Fluor 646	NB200-103JF646
PE	NB200-103PE
PerCP	NB200-103PCP
mFluor Violet 450 SE	NB200-103MFV450
mFluor Violet 500 SE	NB200-103MFV500
mFluor Violet 610 SE	NB200-103MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB200-103SS
Azide and BSA Free	NBP2-80898

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NB100-1612

beta-III Tubulin Antibody

(2 Reviews)

(39 Publications)

0.25 ml

NB100-1612

beta-III Tubulin Western Blot using homogenates of adult mouse brain (1:3000).

Reactivity:

Hu, Mu, Rt

Species Glossary

Reactivity: Hu, Mu, Rt

Applications:

, , , , ,

Applications: , , , , ,

Host:

Chicken Polyclonal

Host: Chicken Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

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NB100-154

Rad50 Antibody

(2 Reviews)

(34 Publications)

0.1 ml

NB100-154

Western Blot: Rad50 Antibody [NB100-154] - WB detection of RAD50 protein in 30ug whole cell lysate of 293T cells using Rad50 antibody at 1:2000 dilution (Submitted via Verified Customer Review).

Western Blot: Rad50 Antibody [NB100-154] - Detection of Rad50 in HeLa nuclear extracts.

Reactivity:

Hu, Mu, Ha

Species Glossary

Reactivity: Hu, Mu, Ha

Applications:

, , , ,

Applications: , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

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NB100-1639

alpha Tubulin Antibody (YOL1/34) - BSA Free

(1 Review)

(25 Publications)

0.25 mg

NB100-1639

Flow (Intracellular): alpha Tubulin Antibody (YOL1/34) [NB100-1639] - An intracellular stain was performed on HeLa cells with Tubulin [YOL1/34] Antibody NB100-1639 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1.0 ug/mL for 30 minutes at room temperature, followed by Rat IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 488.

Flow Cytometry: alpha Tubulin Antibody (YOL1/34) [NB100-1639] - An intracellular stain was performed on HeLa cells with alpha Tubulin Antibody [YOL1/34] NB100-1639AF647 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 647. Image using the Alexa Fluor 647 format of this antibody.

Immunocytochemistry/Immunofluorescence: alpha Tubulin Antibody (YOL1/34) [NB100-1639] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X PBS + 0.05% Triton-X100. The cells were incubated with anti-Tubulin Antibody [YOL1/34] at 5 ug/ml overnight at 4C and detected with an anti-rat Dylight 488 (Green) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

Immunocytochemistry/Immunofluorescence: alpha Tubulin Antibody (YOL1/34) - BSA Free [NB100-1639] - alpha Tubulin Antibody (YOL1/34) [NB100-1639] - NIH3T3 cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X PBS + 0.05% Triton-X100. The cells were incubated with anti-Tubulin Antibody [YOL1/34] at 5 ug/ml overnight at 4C and detected with an anti-rat Dylight 488 (Green) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

Immunocytochemistry/Immunofluorescence: alpha Tubulin Antibody (YOL1/34) [NB100-1639] - PC12 cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X PBS + 0.05% Triton-X100. The cells were incubated with anti-Tubulin Antibody [YOL1/34] at 5 ug/ml overnight at 4C and detected with an anti-rat Dylight 488 (Green) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

Immunocytochemistry/Immunofluorescence: alpha Tubulin Antibody (YOL1/34) [NB100-1639] - Mutants unable to ubiquitinate histone H2B-K123 display growth and Cdc14 release defects when combined with MEN mutants. Representative images from Cdc14 release assay. Cells are assayed for spindle morphology and Cdc14 release phenotype by indirect immunofluorescence with anti-tubulin or anti-HA, which recognizes the HA-tagged version of Cdc14 in all strains. Cells are visualized by nuclear staining with DAPI and by differential interference contrast (DIC) optics for comparison. No release refers to dense nucleolar staining of Cdc14-HA, full release refers to cells with uniform Cdc14-HA localization throughout the nucleus, while partial release refers to cells with both nuclear and residual nucleolar staining. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pgen.1000588), licensed under a CC-BY license.

Mutants unable to ubiquitinate histone H2B-K123 display growth and Cdc14 release defects when combined with MEN mutants. (B) Representative images from Cdc14 release assay. Cells are assayed for spindle morphology and Cdc14 release phenotype by indirect immunofluorescence with anti-tubulin or anti-HA, which recognizes the HA-tagged version of Cdc14 in all strains. Cells are visualized by nuclear staining with 4',6-diamidino-2-phenylindole (DAPI) and by differential interference contrast (DIC) optics for comparison. No release refers to dense nucleolar staining of Cdc14-HA, full release refers to cells with uniform Cdc14-HA localization throughout the nucleus, while partial release refers to cells with both nuclear and residual nucleolar staining. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pgen.1000588), licensed under a CC-BY licence.

Reactivity:

Hu, Mu, Rt, Dr, Fu, Ye

Species Glossary

Reactivity: Hu, Mu, Rt, Dr, Fu, Ye

Applications:

, , , , ,

Applications: , , , , ,

Host:

Rat Monoclonal

Host: Rat Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 405	NB100-1639AF405
Alexa Fluor 488	NB100-1639AF488
Alexa Fluor 647	NB100-1639AF647
Alexa Fluor 700	NB100-1639AF700
Biotin	NB100-1639B-0.25ml
DyLight 350	NB100-1639UV
DyLight 405	NB100-1639V
DyLight 488	NB100-1639G
DyLight 550	NB100-1639R-0.25ml
DyLight 650	NB100-1639C-0.25ml
DyLight 680	NB100-1639FR
DyLight 755	NB100-1639IR
FITC	NB100-1639F-0.25ml
HRP	NB100-1639H-0.25ml

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-1639SS
Azide and BSA Free	NBP2-80569

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At	=	A. thaliana	SyHa	=	Golden Syrian Hamster
All	=	All Species	Ha	=	Hamster
An	=	Animal	Hu	=	Human
ArHa	=	Armenian Hamster	I	=	Insect
Av	=	Avian	Ll	=	Llama
Bb	=	Baboon	Ma	=	Mammal
Ba	=	Bacteria	Mk	=	Monkey
Bv	=	Bovine	Mu	=	Mouse
Ca	=	Canine	Multi	=	Multi-species
Ce	=	C. Elegans	NA	=	Non-species specific
Ch	=	Chicken	Or	=	Orangutan
ChHa	=	Chinese Hamster	Pl	=	Plant
Cm	=	Cynomolgus Monkey	Pm	=	Primate
Do	=	Donkey	Po	=	Porcine
Dr	=	Drosophilia	Rb	=	Rabbit
Ec	=	E. Coli	Rt	=	Rat
Eq	=	Equine	RM	=	Rhesus Macaque
Fe	=	Feline	Sh	=	Sheep
Ft	=	Ferret	Vb	=	Vertebrate
Fi	=	Fish	Vi	=	Virus
Fu	=	Fungi	Xp	=	Xenopus
Ge	=	Gerbil	Ye	=	Yeast
GP	=	Guinea Pig	Ze	=	Zebrafish
Gt	=	Goat

Category

Protein/Target

Applications

Reactivity

Citation

Antibody Validation

Reviews

Host

Available Conjugates

Format

Marker

Modification

Clonality

Clone

Gene Symbol

Images Type

Isotype

Preservative

Research Areas

Has Sample Size

Promotional Item

Species Glossary

AIF-1/Iba1 Antibody

Mre11 Antibody

Nbs1 Antibody

TRF-2 Antibody - BSA Free

TRF-2 Antibody (4A794.15) - BSA Free

SCP3/SYCP3 Antibody - BSA Free

SCP1 Antibody - BSA Free

alpha Tubulin Antibody (YL1/2) - BSA Free

p53 Antibody (PAb 240) - BSA Free

beta-III Tubulin Antibody

Rad50 Antibody

alpha Tubulin Antibody (YOL1/34) - BSA Free