| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP2-24875SS | |||
| Azide Free | NBP2-33263 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP1-77299SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP1-77533SS | |||
| Azide Free | NBP2-33252 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP2-24588SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP1-77077SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-56527SS | |||
| Azide and BSA Free | NBP2-80616 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Azide and BSA Free | NBP2-27335 | |||
| BSA Free | NB100-56599SS | |||
| Azide and BSA Free | NBP2-27335SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Azide Free | NBP2-27405 | |||
| BSA Free | NBP2-27404SS | |||
![Flow Cytometry: TLR3 Antibody (40C1285.6) [NBP2-24875] - Expression of TLR3 protein on epithelial cells. HNEC (A), Detroit-562 (B) and FaDu (C) were stained intracellularly with FITC-Abs against TLR3 (open histograms) or appropriate isotype control (shaded histograms) and analyzed by flow cytometry. Representative pictures from one out of three independent experiments are shown. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0098239), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TLR3-Antibody-40C1285-6-Flow-Cytometry-NBP2-24875-img0014.jpg "Flow Cytometry: TLR3 Antibody (40C1285.6) [NBP2-24875] - Expression of TLR3 protein on epithelial cells. HNEC (A), Detroit-562 (B) and FaDu (C) were stained intracellularly with FITC-Abs against TLR3 (open histograms) or appropriate isotype control (shaded histograms) and analyzed by flow cytometry. Representative pictures from one out of three independent experiments are shown. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0098239), licensed under a CC-BY license.")
![Western Blot: TLR3 Antibody (40C1285.6) [NBP2-24875] - All the cell lines displayed a strong expression of TLR3 protein. Cell lysates were electrophoresed and blotted to PVDF membrane, which was probed with TLR3-specific antibody. To confirm the immunoreactivity of the antibody, different positive controls were included. Beta-actin was served as loading control and was used to normalize expression levels between cells. Data are representative for analysis of >=2 independent experiments. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0060671) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TLR3-Antibody-40C1285-6-Western-Blot-NBP2-24875-img0015.jpg)
![Immunohistochemistry-Paraffin: TLR3 Antibody (40C1285.6) [NBP2-24875] - Mouse colon using TLR3 antibody (clone 40C1285.6) at 1:500 dilution with HRP-DAB detection and hematoxylin counterstaining. Intense signal was found in subset of cells at the bases of the crypts.](http://images.novusbio.com/fullsize/TLR3-Antibody-40C1285-6-Immunohistochemistry-Paraffin-NBP2-24875-img0006.jpg)
![Flow Cytometry: TLR3 Antibody (40C1285.6) [NBP2-24875] - Expression of TLR3 in Fravel, L363, OPM1, RPMI8226, XG1, and NCI-H929 as determined by flow cytometry. HCMLs were stained using an intracellular staining protocol with TLR3 antibodies followed by relevant secondary fluorescent-conjugated antibodies. Filled histograms (purple) represent the isotype controls and the open histograms (red) indicate TLR3. Data are representative for analysis of >=2 independent experiments. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0060671) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TLR3-Antibody-40C1285-6-Flow-Cytometry-NBP2-24875-img0016.jpg)
![Western Blot: TLR3 Antibody (40C1285.6) [NBP2-24875] - Analysis of TLR3 in lysates from A) human intestine and F) ovary using TLR3 antibody at 3 ug/ml. Goat anti-mouse HRP conjugate was used as secondary.](http://images.novusbio.com/fullsize/TLR3-Antibody-40C1285-6-Western-Blot-NBP2-24875-img0018.jpg)
![Western Blot: TLR3 Antibody (40C1285.6) [NBP2-24875] - HEK293T cells were transfected with TLR3, TLR3-9-3 and TLR3-3-9. Western blot was performed using anti-TLR3 or anti-HA antibodies. Anti-Beta-actin antibodies were used as a loading control. The representative data from three experiments are shown. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0092391) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TLR3-Antibody-40C1285-6-Western-Blot-NBP2-24875-img0017.jpg)
![Immunohistochemistry-Paraffin: TLR3 Antibody (40C1285.6) [NBP2-24875] - Tissue section of mouse intestine using TLR3 antibody (clone 40C1285.6) at 1:500 dilution with HRP-DAB detection and hematoxylin counterstaining. The representative image shows a punctate staining of the ER and endosomes in a subset of cells in Peyer's patches (organized lymphoid nodules) in the tested section.](http://images.novusbio.com/fullsize/TLR3-Antibody-40C1285-6-Immunohistochemistry-Paraffin-NBP2-24875-img0007.jpg)
![Immunohistochemistry-Paraffin: TLR3 Antibody (40C1285.6) [NBP2-24875] - Analysis of TLR3 in (A) human gut lumen (longitudinal section, transverse region) using this antibody at 10 ug/ml (Data courtesy Dr. Elizabeth Furrie, University of Dundee) and mouse spleen tissue using isotype control (B) and this antibody (C) at 5 mg/ml.](http://images.novusbio.com/fullsize/TLR3-Antibody-40C1285-6-Immunohistochemistry-Paraffin-NBP2-24875-img0002.jpg)
![Immunohistochemistry: TLR3 Antibody (40C1285.6) - BSA Free [NBP2-24875] - The nasal epithelium expresses TLR3, TLR7, TLR9, RIG-I & MDA-5.Sections of nasal biopsies were incubated with antibodies against TLR3 (A), TLR7 (B), TLR9 (C), RIG-I (D), & MDA-5 (E) & visualized by 3, 3′-diaminobenzidine (brown). In control slides (F), N-series universal negative control reagent was used. All sections were accompanied with a square magnification. All slides were counterstained with haematoxylin (blue). The figure shows one representative biopsy out of four (3 male, 1 female). The arrows indicate positive stained cells. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24886842), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp2-24875_mouse-monoclonal-tlr3-antibody-40c1285-6-310202415384128.jpg)
![Immunohistochemistry: TLR3 Antibody (40C1285.6) - BSA Free [NBP2-24875] - TLRs are expressed & functional in chondrocytes.A RT-PCR for TLR3 & 9 expression in primary human & murine chondrocytes. GAPDH served as loading control. B Confocal microscopy of labelled CpG (green) & poly(I:C) (red) uptake by either primary human chondrocytes (scale bar 20 µm) or murine hip caps (scale bar 50 µm (centre) 20 µm (right)). DAPI (blue) was used as counterstaining for nuclei. C IFN alpha ELISA of murine chondrocytes stimulated with ODN (one-way ANOVA:F (2, 9) = 2.21, p = 0.16, N = 4). D IFN alpha ELISA of primary human chondrocytes stimulated with ODN & poly(I:C) (one-way ANOVA:F (3, 11) = 0.75, p = 0.55, N = 4). E IFN beta ELISA of murine chondrocytes stimulated with poly(I:C) or ODN (one-way ANOVA: F (2, 15) = 59.61, p < 0.0001, N = 6). F IFN beta ELISA of primary human chondrocytes stimulated with poly(I:C) or ODN (one-way ANOVA:F (2, 6) = 95.43, p = <0.0001, N = 3). G Staurosporine was used to induce cell death. The release of RNA from human primary chondrocytes after treatment was measured in the culture supernatant using the RiboGreen assay (RM ANOVA: F (4, 12) = 101.2, p < 0.0001, N = 4). Dunnett’s post-hoc test revealed an increase for 200, 500, & 1000 ng/ml staurosporine treatment compared to the untreated control. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35277480), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp2-24875_mouse-monoclonal-tlr3-antibody-40c1285-6-31020241611475.jpg)
![Western Blot: TLR3 Antibody (40C1285.6) - BSA Free [NBP2-24875] - TLR mRNA & protein expression in airlifted immortal human corneal (HCET) & conjunctival epithelial cells (IOBA-NHC). (a) Averaged fold increase of TLR mRNA in IOBA-NHC cells. The increase was statistically significant for each TLR. (b) Averaged fold increase of TLR mRNA in HCET cells. The increase was statistically significant for each TLR. Cells were airlifted for 10 days. TLR mRNA level was determined by qPCR & compared to submerged cells. The experiment was repeated 3 times. Y error bars represent the standard deviation of the averaged results. (c) Micrographs of a representative western blot showing TLR protein expression in IOBA-NHC cells. Lane 1: submerged-cultured; lane 2: 3 days after airlifting culture; lane 3: 7 days after airlifting culture; lane 4: 10 days after airlifting culture. Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) protein was probed as loading control. (d) Averaged TLR protein increase in IOBA-NHC cells 10 days after airlifting culture compared to submerged-cultured cells. X-ray films from 2 independent western blot experiments were scanned in a densitometer, & the results were averaged. The increase was statistically significant for each TLR protein tested. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24976686), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp2-24875_mouse-monoclonal-tlr3-antibody-40c1285-6-310202416113516.jpg)
![Western Blot: RIPK3/RIP3 Antibody [NBP1-77299] - Analysis of RIP3 in HeLa cell lysate with RIPK3/RIP3 antibody [NBP1-77299] at (A) 1 and (B) 2 ug/mL. Observed molecular weight ~60 kDa. Theoretical molecular weight 53 kDa.](http://images.novusbio.com/fullsize/RIPK3-RIP3-Antibody-Western-Blot-NBP1-77299-img0014.jpg "Western Blot: RIPK3/RIP3 Antibody [NBP1-77299] - Analysis of RIP3 in HeLa cell lysate with RIPK3/RIP3 antibody [NBP1-77299] at (A) 1 and (B) 2 ug/mL. Observed molecular weight ~60 kDa. Theoretical molecular weight 53 kDa.")
![Western Blot: RIPK3/RIP3 Antibody [NBP1-77299] - Mouse Cell lines. 15 ug of lysates per lane. Antibodies: [NBP1-77299], (0.5 ug/mL), 1h incubation at RT in 5% NFDM/TBST. Secondary: Goat anti-rabbit IgG HRP conjugate at 1:10000 dilution. Observed molecular weight ~50 kDa. Theoretical molecular weight 53 kDa.](http://images.novusbio.com/fullsize/RIPK3-RIP3-Antibody-Western-Blot-NBP1-77299-img0022.jpg)
![Western Blot: RIPK3/RIP3 Antibody [NBP1-77299] - Analysis using RIPK3/RIP3 antibody [NBP1-77299]. L929 cell line (mouse). 20 ug whole cell lysate. Primary antibody: 1:2000. Secondary antibody: 1:20000. Western blot image submitted by a verified customer review. Observed molecular weight ~57 kDa. Theoretical molecular weight 53 kDa.](http://images.novusbio.com/fullsize/RIPK3-RIP3-Antibody-Western-Blot-NBP1-77299-img0024.jpg)
![Western Blot: RIPK3/RIP3 Antibody [NBP1-77299] - C2C12 Cells. 15 ug of lysates per lane. Antibodies: RIPK3/RIP3 antibody [NBP1-77299], 1h incubation at RT in 5% NFDM/TBST. Secondary: Goat anti-rabbit IgG HRP conjugate at 1:10000 dilution. Lane 1: NBP1-77299, 0.1 ug/mL in the presence of peptide blocking. Lane 2: NBP1-77299, 0.1 ug/mL Lane 3: NBP1-77299, 0.2 ug/mL Lane 4: NBP1-77299, 0.5 ug/mL. Observed molecular weight ~55 kDa. Theoretical molecular weight 53 kDa.](http://images.novusbio.com/fullsize/RIPK3-RIP3-Antibody-Western-Blot-NBP1-77299-img0021.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: RIPK3/RIP3 Antibody [NBP1-77299] - Bone-marrow-derived macrophages exhibit significant reduction in RIPK3/RIP3 levels in RIPK3/RIP3deltaGlobal, RIPK3/RIP3deltaMphi-Cre and RIPK3/RIP3deltaEC-Cre mice. Protein lysates were immunoblotted to identify CD11b, RIPK3/RIP3 and beta-actin (loading control). Image collected and cropped by CiteAb from the following publication (www.dmm.biologists.org/lookup/doi/10.1242/dmm.041962) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/RIPK3-RIP3-Antibody-Knockout-Validated-NBP1-77299-img0025.jpg)
![<b>Genetic Strategies Validation. </b>Knockdown Validated: RIPK3/RIP3 Antibody [NBP1-77299] - RIPK3/RIP3-deficiency impacts MCP-1 and IL-1beta expression in BMDMs and MCP-1 and E-Selectin/CD62E expression in cultured endothelial cells. Protein lysates were immunoblotted for RIPK3/RIP3 and the loading control, GAPDH (n=4 independent experiments). Image collected and cropped by CiteAb from the following publication (www.dmm.biologists.org/content/13/1/dmm041962) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/RIPK3-RIP3-Antibody-Knockdown-Validated-NBP1-77299-img0026.jpg)
![Western Blot: RIPK3/RIP3 Antibody - BSA Free [NBP1-77299] - Bone-marrow-derived macrophages exhibit significant reduction in RIPK3 levels in Ripk3 delta Global, Ripk3 delta MΦ-Cre & Ripk3 delta EC-Cre mice. (A,B) BMDMs were isolated, differentiated on chamber slides for 7 days, immunostained for macrophage markers CD68 (red; A) & CD11b (pink; B), & co-stained for nuclei (Hoechst; blue). All cells from seven separate BMDM isolations were positive for these markers (n=7). (C) A phagocytosis assay was performed on BMDMs with fluorescent polystyrene beads. Phagocytic cells display TRITC+/Hoechst+ signal, & 85% of cells from two separate BMDM isolations were double positive (n=2). (D-F) Protein or RNA was collected from control, Ripk3 delta Global, Ripk3 delta MΦ-Cre & Ripk3 delta EC-Cre BMDMs. RNA was converted to cDNA & analyzed by qPCR for Ripk3 levels (D). Protein lysates were immunoblotted to identify CD11b, RIPK3 & beta -actin (loading control) (E) & quantified (F). (G) RNA from control & Ripk3 delta Global BMDMs was converted to cDNA & analyzed by qPCR for Ripk3-Exon 10 levels. For panels D,F,G, each dot represents a BMDM isolation from an individual animal. Statistics for panels D & F were calculated using one-way ANOVA with Dunnett's multiple comparisons test. Overall ANOVA P-values (prior to the post hoc tests) are 0.0002 (D) & <0.0001 (F). Statistics for panel G were calculated using an unpaired t-test with Welch's correction. *P<0.05, **P<0.01, ***P<0.001, ****P<0.0001. Data are mean±s.d. Scale bars: 25 µm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31953345), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-77299_rabbit-polyclonal-ripk3-rip3-antibody-310202416171485.jpg)
![Western Blot: RIPK3/RIP3 Antibody - BSA Free [NBP1-77299] - p-MLKL levels are nearly undetectable in advanced plaques. (A-C) After 3 months on a Western diet, protein was collected from control (n=7), Ripk3 delta MΦ-Cre (n=5), Ripk3 delta EC-Cre (n=3) & Ripk3 delta SMC-Cre (n=3) aortas. Protein lysates were immunoblotted to identify p-MLKL (Abcam; #ab196436), MLKL & beta -actin (loading control) (A) & quantified (B,C). A faint positive p-MLKL signal can be seen in the representative blot in the control arch region; however, we could only detect p-MLKL in two out of the 18 aortas analyzed (B). Note that the same transfer membrane used for detecting CD11b (in Fig. 4S) was reprobed for p-MLKL & MLKL in A; the beta -actin control blots are therefore the same in both figures. (D,E) Protein lysates were immunoblotted to identify RIPK3 & GAPDH (loading control) (D) & quantified (E). For panels B,C,E, each dot represents an individual animal. Statistics were calculated using two-way ANOVA. Overall ANOVA P-values are 0.76 (B), 0.07 (C) & 0.46 (E). Data are mean±s.d. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31953345), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-77299_rabbit-polyclonal-ripk3-rip3-antibody-31020241616072.jpg)
![Immunocytochemistry/ Immunofluorescence: RIPK3/RIP3 Antibody - BSA Free [NBP1-77299] - Validation of RIPK3/RIP3 in Rat Kidney Tissue. Immunofluorescent analysis of 4% paraformaldehyde-fixed Rat Kidney tissue labeling RIPK3/RIP3 with at 20 ug/mL, followed by goat anti-rabbit IgG secondary antibody at 1/500 dilution (red).](http://images.novusbio.com/fullsize/nbp1-77299_rabbit-polyclonal-ripk3-rip3-antibody-2711202419562182.jpg)
![Immunohistochemistry: RIPK3/RIP3 Antibody - BSA Free [NBP1-77299] - Validation of RIPK3/RIP3 in Mouse Kidney Tissue. Immunohistochemical analysis of paraffin-embedded mouse kidney tissue using anti-RIPK3/RIP3 antibody at 2.5 ug/ml. Tissue was fixed with formaldehyde and blocked with 10% serum for 1 h at RT; antigen retrieval was by heat mediation with a citrate buffer (pH6). Samples were incubated with primary antibody overnight at 4C. A goat anti-rabbit IgG H&L (HRP) at 1/250 was used as secondary. Counter stained with Hematoxylin.](http://images.novusbio.com/fullsize/nbp1-77299_rabbit-polyclonal-ripk3-rip3-antibody-2711202419333448.gif)
![Immunohistochemistry: RIPK3/RIP3 Antibody - BSA Free [NBP1-77299] - Validation of RIPK3/RIP3 in Rat Kidney Tissue.Immunohistochemical analysis of paraffin-embedded rat kidney tissue using anti-RIPK3/RIP3 antibody at 5 ug/ml. Tissue was fixed with formaldehyde and blocked with 10% serum for 1 h at RT; antigen retrieval was by heat mediation with a citrate buffer (pH6). Samples were incubated with primary antibody overnight at 4C. A goat anti-rabbit IgG H&L (HRP) at 1/250 was used as secondary. Counter stained with Hematoxylin.](http://images.novusbio.com/fullsize/nbp1-77299_rabbit-polyclonal-ripk3-rip3-antibody-271120242074698.jpg)
![Western Blot: RIPK3/RIP3 Antibody - BSA Free [NBP1-77299] - Validation in Human Cell Lines. Loading: 15 ug of lysates per lane.Antibodies: RIPK3/RIP3 , (0.5 ug/mL), 1h incubation at RT in 5% NFDM/TBST.Secondary: Goat anti-rabbit IgG HRP conjugate at 1:10000 dilution.](http://images.novusbio.com/fullsize/nbp1-77299_rabbit-polyclonal-ripk3-rip3-antibody-2711202420243399.gif)
![Western Blot: A20/TNFAIP3 Antibody (59A426) [NBP1-77533] - Human Jurkat lysate probed with A20 antibody at 4 ug/ml.](http://images.novusbio.com/fullsize/A20-TNFAIP3-Antibody-59A426-Western-Blot-NBP1-77533-img0005.jpg "Western Blot: A20/TNFAIP3 Antibody (59A426) [NBP1-77533] - Human Jurkat lysate probed with A20 antibody at 4 ug/ml.")
![Flow Cytometry: A20/TNFAIP3 Antibody (59A426) [NBP1-77533] - An intracellular stain was performed on SK-MEL-28 cells with A20/TNFAIP3 (59A426) antibody NBP1-77533AF647 (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.](http://images.novusbio.com/fullsize/A20-TNFAIP3-Antibody-59A426-Flow-Cytometry-NBP1-77533-img0013.jpg)
![Simple Western: A20/TNFAIP3 Antibody (59A426) [NBP1-77533] - Lane view shows a specific band for A20/TNFAIP3 in 0.05 mg/ml of Jurkat lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/A20-TNFAIP3-Antibody-59A426-Simple-Western-NBP1-77533-img0008.jpg)
![Immunohistochemistry-Paraffin: A20/TNFAIP3 Antibody (59A426) [NBP1-77533] - Human placenta probed with A20 antibody at 5 ug/ml, cytoplasmic staining of decidual cells is observed. Human tissue TMA 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.](http://images.novusbio.com/fullsize/A20-TNFAIP3-Antibody-59A426-Immunohistochemistry-Paraffin-NBP1-77533-img0010.jpg)
![Immunocytochemistry/Immunofluorescence: A20/TNFAIP3 Antibody (59A426) [NBP1-77533] - HepG2 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-A20/TNFAIP3 (59A426) at 10 ug/ml 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](http://images.novusbio.com/fullsize/A20-TNFAIP3-Antibody-59A426-Immunocytochemistry-Immunofluorescence-NBP1-77533-img0016.jpg)
![Immunocytochemistry/Immunofluorescence: A20/TNFAIP3 Antibody (59A426) [NBP1-77533] - Caco-2 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.05% Triton X-100 in PBS for 5 minutes. The cells were incubated with anti-A20/TNFAIP3 Antibody [59A426] NBP1-77533 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.](http://images.novusbio.com/fullsize/A20-TNFAIP3-Antibody-59A426-Immunocytochemistry-Immunofluorescence-NBP1-77533-img0018.jpg)
![Flow Cytometry: A20/TNFAIP3 Antibody (59A426) [NBP1-77533] - An intracellular stain was performed on RH-30 cells with A20/TNFAIP3 Antibody (59A426) NBP1-77533PE (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 Phycoerythrin.](http://images.novusbio.com/fullsize/A20-TNFAIP3-Antibody-59A426-Flow-Cytometry-NBP1-77533-img0017.jpg)
![Immunohistochemistry-Paraffin: RIPK3/RIP3 Antibody [NBP2-24588] - Analysis of RIP3 using polyclonal RIPK3/RIP3 Antibody [NBP2-24588]. Human pancreas probed with RIPK3/RIP3 antibody at 10 ug/ml.](http://images.novusbio.com/fullsize/RIPK3-RIP3-Antibody-Immunohistochemistry-Paraffin-NBP2-24588-img0004.jpg "Immunohistochemistry-Paraffin: RIPK3/RIP3 Antibody [NBP2-24588] - Analysis of RIP3 using polyclonal RIPK3/RIP3 Antibody [NBP2-24588]. Human pancreas probed with RIPK3/RIP3 antibody at 10 ug/ml.")
![<b>Biological Strategies Validation. </b>Western Blot: RIPK3/RIP3 Antibody [NBP2-24588] - Representative western blot analysis of RIP1, RIPK3/RIP3, and beta-actin in WI-38 NCs and IR-SCs 24 h after incubation with Veh or 10 uM PL. A cell lysate of etoposide-treated Jurkat cells was used as a positive control. Image collected and cropped by CiteAb from the following publication (//www.aging-us.com/article/101100/text) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/RIPK3-RIP3-Antibody-Western-Blot-NBP2-24588-img0006.jpg)
![Immunocytochemistry/Immunofluorescence: RIPK3/RIP3 Antibody [NBP2-24588] - 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 RIPK3/RIP3 Antibody [NBP2-24588] at a 1:200 dilution overnight at 4C and detected with DyLight 488 (Green) at a 1:500 dilution. Alpha tubulin was used at a 1:1000 dilution as a co-stain and detected with DyLight 550 (Red) at a 1:500 dilution. Nuclei were detected with DAPI (Blue) at 2.0ug/ml in 1X PBS. Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/RIPK3-RIP3-Antibody-Immunocytochemistry-Immunofluorescence-NBP2-24588-img0003.jpg)
![Western Blot: RIPK3/RIP3 Antibody [NBP2-24588] - Analysis of RIP3 using polyclonal RIPK3/RIP3 antibody [NBP2-24588]. Human tissue blot probed with 5 ug/ml of RIP3 antibody: 1) brain, 2) heart, 3) small intestine, 4) kidney, 5) liver, 6) lung, 7) skeletal muscle, 8) stomach, 9) spleen, 10) ovary, 11) testis, 12) placenta probed at 5 ug/ml, 13) Ramos cell lysate probed at 7 ug/ml. Theoretical molecular weight 56.7 kDa.](http://images.novusbio.com/fullsize/RIPK3-RIP3-Antibody-Western-Blot-NBP2-24588-img0005.jpg)
![Western Blot: RIPK3/RIP3 Antibody - BSA Free [NBP2-24588] - HOIP limits the activity of TRAIL‐induced apoptosis‐ & necroptosis‐mediating signalling complexesControl & HOIP KO HeLa cells were treated with FLAG‐lz‐TRAIL (500 ng/ml) for the indicated times. The TRAIL complex I was immunoprecipitated via anti‐FLAG beads. Complex II was isolated by immunoprecipitating caspase‐8 from complex I‐depleted lysates. Western blot was performed using the indicated antibodies. * indicates unspecific bands.WT & HOIP‐deficient TNF KO MEFs, pre‐treated for 1 h with zVAD, were stimulated with iz‐TRAIL (1 μg/ml) for the indicated times. FADD‐containing complexes were immunoprecipitated & analysed by Western blot.Data information: See also Fig EV2. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28258062), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp2-24588_rabbit-polyclonal-ripk3-rip3-antibody-31020241534394.jpg)
![Western Blot: RIPK3/RIP3 Antibody - BSA Free [NBP2-24588] - The catalytic activity of HOIP contributes to preventing TRAIL‐induced apoptosis but is dispensable for preventing necroptosisLysates from control or HOIP KO K562 cells reconstituted w/ empty vector, HOIP WT or HOIP C885S analysed by WB.HOIP KO K562 cells reconstituted w/ empty vector, HOIP WT or HOIP C885S, pre‐treated w/ zVAD and/or Nec‐1s for 1 h as indicated, treated w/ iz‐TRAIL (1 μg/ml) for 24 h. Percentage of cell death determined by flow cytometry after PI labelling (n = 5; mean ± SEM). *P < 0.05, **P < 0.01; statistics performed using ANOVA.Control & HOIP KO K562 cells reconstituted w/ empty vector, HOIP WT or HOIP C885S treated w/ iz‐TRAIL (100 ng/ml) for the indicated times. Lysates analysed w/ the indicated antibodies.Lysates from TNF KO HOIP KO MEFs reconstituted w/ empty vector, HOIP WT or HOIP C885S analysed by WB.TNF KO HOIP KO MEFs reconstituted w/ empty vector, HOIP WT or HOIP C885S, pre‐treated w/ zVAD & Nec‐1s for 1 h as indicated, treated w/ iz‐TRAIL (1 μg/ml) for 24 h. Percentage of cell death determined by flow cytometry after PI labelling (n = 4; mean ± SEM). *P < 0.05, ***P < 0.001; statistics performed using ANOVA.TNF KO HOIP KO MEFs reconstituted w/ empty vector, pre‐treated w/ zVAD and/or the RIPK3 inhibitor GSK'872 for 1 h as indicated, treated w/ iz‐TRAIL (1 μg/ml) for 24 h. Percentage of cell death determined by flow cytometry after PI labelling (n = 3; mean ± SEM). *P < 0.05; statistics performed using t‐test.TNF KO HOIP KO MEFs reconstituted w/ empty vector, HOIP WT or HOIP C885S, pre‐treated w/ zVAD for 1 h, treated w/ iz‐TRAIL (1 μg/ml) for the indicated times. FADD‐containing complexes immunoprecipitated & analysed by WB. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28258062), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp2-24588_rabbit-polyclonal-ripk3-rip3-antibody-310202416114733.jpg)
![Western Blot: TLR3 Antibody [NB100-56571] - Myocardial infarction (MI) increased TLR3 expression and its physical association with Trif in mouse myocardium. Heart samples were taken from infarct area at 4 weeks after MI. (A) and (B) show mRNA and protein levels of TLR3 in sham and MI hearts. n = 4 mice/group. Data are means +/- S.D. AP < 0.01 versus sham. Image collected and cropped by CiteAb from the following publication (//doi.wiley.com/10.1111/jcmm.13328) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TLR3-Antibody-Western-Blot-NB100-56571-img0009.jpg "<b>Biological Strategies Validation and Orthogonal Strategies Validation.</b>Western Blot: TLR3 Antibody [NB100-56571] - Myocardial infarction (MI) increased TLR3 expression and its physical association with Trif in mouse myocardium. Heart samples were taken from infarct area at 4 weeks after MI. (A) and (B) show mRNA and protein levels of TLR3 in sham and MI hearts. n = 4 mice/group. Data are means +/- S.D. AP < 0.01 versus sham. Image collected and cropped by CiteAb from the following publication (//doi.wiley.com/10.1111/jcmm.13328) licensed under a CC-BY license.")
![<b>Biological Strategies Validation and Orthogonal Strategies Validation.</b>Immunohistochemistry-Frozen: TLR3 Antibody [NB100-56571] - Frozen mouse eye tissue sections stained with TLR3, a retinal pigment epithelium (RPE) marker and DAPI. Top panel: TLR3 (red) colocalized with the RPE (green) marker. Bottom panel: Tissue stained with isotype control (no TLR3 Ab), RPE and DAPI. Data courtesy of Kleinman et al.](http://images.novusbio.com/fullsize/TLR3-Antibody-Immunohistochemistry-Frozen-NB100-56571-img0002.jpg)
![Flow Cytometry: TLR3 Antibody [NB100-56571] - Analysis using the FITC conjugate of NB100-56571. Staining of TLR3 in Balb/c mouse splenocytes using this antibody at 1 ug/10^6 cells. Green represents rabbit IgG isotype control this antibody; red represents anti-TLR3 antibody.](http://images.novusbio.com/fullsize/TLR3-Antibody-Flow-Cytometry-NB100-56571-img0008.jpg)
![Western Blot: TLR3 Antibody [NB100-56571] - Analysis of TLR3 in mouse spleen tissue lysate using NB100-56571 at 2 ug/ml.](http://images.novusbio.com/fullsize/TLR3-Antibody-Western-Blot-NB100-56571-img0005.jpg)
![Immunohistochemistry: TLR3 Antibody [NB100-56571] - Pig lung poisoned through aspiration with gastric juice and organophosphate (dimethoate EC40) after 48 hours of IC ventilation. Image from verified customer review.](http://images.novusbio.com/fullsize/TLR3-Antibody-Immunohistochemistry-NB100-56571-img0006.jpg)
![Flow Cytometry: TLR3 Antibody [NB100-56571] - Intracellular flow analysis of TLR3 in Balb/c mouse splenocytes and mouse RAW cells using TLR3 antibody (red) and isotype control antibody (green) at 1 ug/10^6 cells.](http://images.novusbio.com/fullsize/TLR3-Antibody-Flow-Cytometry-NB100-56571-img0001.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: TLR3 Antibody [NB100-56571] - siRNA was transfected at 50 nM for 48 hrs, and poly(I:C) was added at 100 ug/ml for 4 hrs before cell harvest. Negative control (NC) siRNA served as control. RNAiMAX transfection reagent was used in all the siRNA experiments. Panel shows the knockdown effects of siRNAs. Image collected and cropped by CiteAb from the following publication (//doi.wiley.com/10.1111/jcmm.13328) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TLR3-Antibody-Knockdown-Validated-NB100-56571-img0010.jpg)
![Western Blot: TLR3 Antibody [NB100-56571] - Myocardial infarction (MI) increased TLR3 expression & its physical association with Trif in mouse myocardium. Heart samples were taken from infarct area at 4 weeks after MI. (A) & (B) show mRNA & protein levels of TLR3 in sham & MI hearts. n = 4 mice/group. Data are means ± S.D. AP < 0.01 versus sham. (C) Representative immunohistochemistry images of heart sections stained for TLR3 (brown colour). An isotype IgG control was performed to verify the specificity of TLR3 reactivity. (D) Lysates of heart tissue were immunoprecipitated with anti‐TLR3 antibodies (IP: TLR3), followed by SDS–PAGE & immunoblotting (IB) with indicated antibodies. IP with isotype IgG (IP: IgG) was performed as a control to exclude the non‐specific binding of antibodies to cellular proteins. Green arrows indicate non‐specific bands. The association between TLR3 & Trif, but not MyD88, was detectable in sham myocardium & was increased in infarct myocardium. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28945004), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56571_rabbit-polyclonal-tlr3-antibody-310202415523938.jpg)
![Western Blot: TLR3 Antibody [NB100-56571] - Myocardial infarction (MI) increased TLR3 expression & its physical association with Trif in mouse myocardium. Heart samples were taken from infarct area at 4 weeks after MI. (A) & (B) show mRNA & protein levels of TLR3 in sham & MI hearts. n = 4 mice/group. Data are means ± S.D. AP < 0.01 versus sham. (C) Representative immunohistochemistry images of heart sections stained for TLR3 (brown colour). An isotype IgG control was performed to verify the specificity of TLR3 reactivity. (D) Lysates of heart tissue were immunoprecipitated with anti‐TLR3 antibodies (IP: TLR3), followed by SDS–PAGE & immunoblotting (IB) with indicated antibodies. IP with isotype IgG (IP: IgG) was performed as a control to exclude the non‐specific binding of antibodies to cellular proteins. Green arrows indicate non‐specific bands. The association between TLR3 & Trif, but not MyD88, was detectable in sham myocardium & was increased in infarct myocardium. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28945004), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56571_rabbit-polyclonal-tlr3-antibody-3102024165731.jpg)
![Immunohistochemistry: TLR3 Antibody [NB100-56571] - Myocardial infarction (MI) increased TLR3 expression & its physical association with Trif in mouse myocardium. Heart samples were taken from infarct area at 4 weeks after MI. (A) & (B) show mRNA & protein levels of TLR3 in sham & MI hearts. n = 4 mice/group. Data are means ± S.D. AP < 0.01 versus sham. (C) Representative immunohistochemistry images of heart sections stained for TLR3 (brown colour). An isotype IgG control was performed to verify the specificity of TLR3 reactivity. (D) Lysates of heart tissue were immunoprecipitated with anti‐TLR3 antibodies (IP: TLR3), followed by SDS–PAGE & immunoblotting (IB) with indicated antibodies. IP with isotype IgG (IP: IgG) was performed as a control to exclude the non‐specific binding of antibodies to cellular proteins. Green arrows indicate non‐specific bands. The association between TLR3 & Trif, but not MyD88, was detectable in sham myocardium & was increased in infarct myocardium. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28945004), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56571_rabbit-polyclonal-tlr3-antibody-310202415535158.jpg)
![Western Blot: TLR3 Antibody [NB100-56571] - TLR3‐knockout (TLR3‐KO) attenuated cardiac autophagy induced by MI. The infarct & remote tissues were separately sampled from the left ventricle after 4 weeks of MI. Accordingly, anterior & posterior tissues of the left ventricle were sampled from sham hearts as controls. (A) Representative Western blot images & quantitative analyses of autophagy markers. n = 4–8/group. Quantitative data are fold changes of WT‐sham. aP < 0.05, AP < 0.01 versus respective WT‐sham; bP < 0.05, BP < 0.01 versus respective WT‐MI. (B) Representative electron microphotographs of ultrathin sections of resin‐embedded heart biopsies. Arrows indicate autophagic vacuoles. (C) Lysates of infarct tissue were immunoprecipitated (IP), followed by SDS–PAGE & immunoblotting (IB) with indicated antibodies. IP with isotype IgG served as a control. Green arrows indicate non‐specific bands. Representative images were taken from four independent experiments. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28945004), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56571_rabbit-polyclonal-tlr3-antibody-310202415525214.jpg)
![Western Blot: TLR3 Antibody [NB100-56571] - A TLR3 agonist polyinosinic‐polycytidylic acid (poly(I:C)) induced autophagy in cultured cardiomyocytes through a TRIF‐dependent pathway. (A) Poly(I:C) increased autophagy markers in cultured H9c2 rat ventricular cells. (B) Poly(I:C) stimulated autophagosome formation but did not affect autophagic flux. Primary cultured neonatal rat ventricular myocytes (NRVMs) were transfected with a tandem mRFP‐GFP‐LC3 adenovirus for 24 hrs, followed by treatment with poly(I:C) (100 μg/ml, 4 hrs). Autophagosomes & autolysosomes were, respectively, visualized as yellow‐ & red‐only punctas under a confocal microscope. (C) An autophagic flux inhibitor chloroquine (CQ) induced accumulations of LC3‐II & p62/SQSTM1 proteins in H9c2 myocytes receiving poly(I:C) (100 μg/ml, 4 hrs). CQ was applied at 10 μM, immediately prior to poly(I:C). (D) Effects of indicated siRNA on poly(I:C)‐induced changes in autophagy markers in NRVMs. All the siRNAs were transfected at 50 nM for 48 hrs, & poly(I:C) was added at 100 μg/ml for 4 hrs before cell harvest. Negative control (NC) siRNA served as control. RNAiMAX transfection reagent was used in all the siRNA experiments. The upper panel shows the knockdown effects of siRNAs, & the lower panel shows representative Western blot images (presented from four independent experiments) & densitometry quantitative data (normalized into ‘fold of vehicle group’). All quantitative data are expressed as means ± S.D. aP < 0.05, AP < 0.01 versus vehicle; bP < 0.05, BP < 0.01 versus poly(I:C). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28945004), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56571_rabbit-polyclonal-tlr3-antibody-3102024168394.jpg)
![Immunohistochemistry: RIPK1/RIP1 Antibody - BSA Free [NBP1-77077] - Immunohistochemistry of RIPK1/RIP1 in mouse kidney tissue with RIPK1/RIP1 antibody at 2.5 ug/mL.](http://images.novusbio.com/fullsize/nbp1-77077_rabbit-polyclonal-ripk1-rip1-antibody-271120242045651.jpg "Immunohistochemistry: RIPK1/RIP1 Antibody - BSA Free [NBP1-77077] - Immunohistochemistry of RIPK1/RIP1 in mouse kidney tissue with RIPK1/RIP1 antibody at 2.5 ug/mL.")
![Immunohistochemistry: RIPK1/RIP1 Antibody - BSA Free [NBP1-77077] - Immunohistochemistry of RIPK1/RIP1 in mouse kidney tissue with RIPK1/RIP1 antibody at 2.5 ug/ml.](http://images.novusbio.com/fullsize/nbp1-77077_rabbit-polyclonal-ripk1-rip1-antibody-2711202420272453.gif)
![<b>Biological Strategies Validation. </b>Western Blot: RIPK1/RIP1 Antibody [NBP1-77077] - At 6 h after CCI, RIP1 protein levels in the cortex detected by western blotting were decreased in Nec-1 and melatonin pretreatment groups, but there was no change in the Z-VAD pretreatment group. Values are represented as means +/- SEM (n = 3). B-actin was used as a control in western blot assays. All data were analyzed by one way ANOVA plus Tukey's test. *P < 0.05 and **P < 0.01 vs. CCI group. Image collected and cropped by CiteAb from the following publication (//www.frontiersin.org/article/10.3389/fnmol.2019.00222/full) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/RIPK1-RIP1-Antibody-Western-Blot-NBP1-77077-img0005.jpg)
![Immunohistochemistry: RIPK1/RIP1 Antibody [NBP1-77077] - Traumatic brain injury (TBI) tissues show increased necroptosis compared with normal brain tissues (NBTs). The expression of RIP1 was tested in NBT and TBI tissues from Jiangsu Province Hospital by immunohistochemistry. Image collected and cropped by CiteAb from the following publication (//www.frontiersin.org/article/10.3389/fnmol.2019.00222/full) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/RIPK1-RIP1-Antibody-Immunohistochemistry-NBP1-77077-img0007.jpg)
![Western Blot: RIPK1/RIP1 Antibody [NBP1-77077] - Rat kidney tissue lysate with RIPK1 antibody at 1 ug/mL.](http://images.novusbio.com/fullsize/RIPK1-RIP1-Antibody-Western-Blot-NBP1-77077-img0001.jpg)
![Western Blot: RIPK1/RIP1 Antibody - BSA Free [NBP1-77077] - Traumatic brain injury (TBI) tissues show increased necroptosis compared with normal brain tissues (NBTs). (A) The protein expressions of receptor-interacting protein 1 (RIP1), RIP3 & mixed lineage kinase domain-like protein (MLKL) were analyzed in human NBT (n = 4) & TBI tissues (n = 9) via western blotting. beta -actin was used as a control. (B–D) Protein expression of RIP1, RIP3 & MLKL was analyzed by statistical. (E) The expressions of RIP1, RIP3 & MLKL were tested in NBT & TBI tissues from Jiangsu Province Hospital by immunohistochemistry. (F) Electron microscopy was used to examine human normal brain & TBI tissues. Intact cell membrane (violet arrow) is labeled in NBT. Complete & continuous nuclear membrane (black arrow), swollen mitochondria (green arrow) & vacuoles (red arrow) are labeled in TBI tissues. All data were analyzed by one way analysis of variance (ANOVA) plus Tukey’s test. **P < 0.01 vs. NBT group. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31607859), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-77077_rabbit-polyclonal-ripk1-rip1-antibody-310202416171410.jpg)
![Immunohistochemistry: RIPK1/RIP1 Antibody - BSA Free [NBP1-77077] - Effect of Nec-1, Z-VAD & melatonin on necroptosis. (A) At 6 h after CCI, RIP1, RIP3 & MLKL protein levels in the cortex detected by western blotting were decreased in Nec-1 & melatonin pretreatment groups, but there was no change in the Z-VAD pretreatment group. (B–D) Protein expression of RIP1, RIP3 & MLKL was analyzed by statistical. (E) Immunohistochemistry assays examined the effect of Nec-1, Z-VAD & melatonin on cortex RIP1, RIP3 & MLKL, respectively. (F) At 6 h after CCI, RIP1, RIP3 & MLKL protein levels in the hippocampus CA1 detected by western blotting were decreased in the Nec-1 & melatonin pretreatment groups, but not the Z-VAD pretreatment group. (G–I) Protein expression of RIP1, RIP3 & MLKL was analyzed by statistical. (J) Immunohistochemistry assays examined the effect of Nec-1, Z-VAD & melatonin on RIP1, RIP3 & MLKL in hippocampus CA1, respectively. (K) TdT-mediated dUTP Nick-End Labeling (TUNEL; green) & cleaved caspase-3 (red) dual immunofluorescent labeling was used & were analyzed by statistical (L,M) in the five groups. Values are represented as means ± SEM (n = 3). beta -actin was used as a control in western blot assays. All data were analyzed by one way ANOVA plus Tukey’s test. *P < 0.05 & **P < 0.01 vs. CCI group. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31607859), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-77077_rabbit-polyclonal-ripk1-rip1-antibody-31020241616014.jpg)
![Western Blot: RIPK1/RIP1 Antibody - BSA Free [NBP1-77077] - Tissues were obtained to perform western blot assays. (A) Location of collected tissues was labeled. Collected cortical tissues & hippocampus CA1 were marked by white & yellow frame, respectively. RIP1, RIP3 & MLKL in the (B) cortex & (C) hippocampus CA1 were examined via western blot from 0 h to 48 h after controlled cortical impact (CCI). Protein expression of RIP1, RIP3 & MLKL in the (D–F) cortex & (G–I) hippocampus CA1 from 0 h to 48 h after CCI was analyzed by statistical. Values are represented as means ± SEM (n = 3–4). (J) Cleaved caspase-3 was detected in cortex & hippocampus CA1 via western blotting from 0 h to 48 h after CCI. (K,L) Protein expression of cleaved caspase-3 in the cortex & hippocampus CA1 from 0 h to 48 h after CCI was measured. Values are represented as means ± SEM (n = 4–5). (M) Cleaved caspase-8 was detected in cortex & hippocampus CA1 via western blotting from 0 h to 48 h after CCI. (N,O) Protein expression of cleaved caspase-8 in the cortex & hippocampus CA1 from 0 h to 48 h after CCI was analyzed. Values are represented as means ± SEM (n = 4–5). beta -actin was used as a control in western blot assays. All data were analyzed by one way ANOVA plus Tukey’s test. *P < 0.05 & **P < 0.01 vs. sham group. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31607859), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-77077_rabbit-polyclonal-ripk1-rip1-antibody-31020241618915.jpg)
![Immunohistochemistry: RIPK1/RIP1 Antibody - BSA Free [NBP1-77077] - Traumatic brain injury (TBI) tissues show increased necroptosis compared with normal brain tissues (NBTs). (A) The protein expressions of receptor-interacting protein 1 (RIP1), RIP3 & mixed lineage kinase domain-like protein (MLKL) were analyzed in human NBT (n = 4) & TBI tissues (n = 9) via western blotting. beta -actin was used as a control. (B–D) Protein expression of RIP1, RIP3 & MLKL was analyzed by statistical. (E) The expressions of RIP1, RIP3 & MLKL were tested in NBT & TBI tissues from Jiangsu Province Hospital by immunohistochemistry. (F) Electron microscopy was used to examine human normal brain & TBI tissues. Intact cell membrane (violet arrow) is labeled in NBT. Complete & continuous nuclear membrane (black arrow), swollen mitochondria (green arrow) & vacuoles (red arrow) are labeled in TBI tissues. All data were analyzed by one way analysis of variance (ANOVA) plus Tukey’s test. **P < 0.01 vs. NBT group. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31607859), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-77077_rabbit-polyclonal-ripk1-rip1-antibody-310202416175211.jpg)
![Western Blot: RIPK1/RIP1 Antibody - BSA Free [NBP1-77077] - Effect of Nec-1, Z-VAD & melatonin on necroptosis. (A) At 6 h after CCI, RIP1, RIP3 & MLKL protein levels in the cortex detected by western blotting were decreased in Nec-1 & melatonin pretreatment groups, but there was no change in the Z-VAD pretreatment group. (B–D) Protein expression of RIP1, RIP3 & MLKL was analyzed by statistical. (E) Immunohistochemistry assays examined the effect of Nec-1, Z-VAD & melatonin on cortex RIP1, RIP3 & MLKL, respectively. (F) At 6 h after CCI, RIP1, RIP3 & MLKL protein levels in the hippocampus CA1 detected by western blotting were decreased in the Nec-1 & melatonin pretreatment groups, but not the Z-VAD pretreatment group. (G–I) Protein expression of RIP1, RIP3 & MLKL was analyzed by statistical. (J) Immunohistochemistry assays examined the effect of Nec-1, Z-VAD & melatonin on RIP1, RIP3 & MLKL in hippocampus CA1, respectively. (K) TdT-mediated dUTP Nick-End Labeling (TUNEL; green) & cleaved caspase-3 (red) dual immunofluorescent labeling was used & were analyzed by statistical (L,M) in the five groups. Values are represented as means ± SEM (n = 3). beta -actin was used as a control in western blot assays. All data were analyzed by one way ANOVA plus Tukey’s test. *P < 0.05 & **P < 0.01 vs. CCI group. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31607859), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-77077_rabbit-polyclonal-ripk1-rip1-antibody-310202416163731.jpg)
![Western Blot: RIPK1/RIP1 Antibody - BSA Free [NBP1-77077] - Tissues were obtained to perform western blot assays. (A) Location of collected tissues was labeled. Collected cortical tissues & hippocampus CA1 were marked by white & yellow frame, respectively. RIP1, RIP3 & MLKL in the (B) cortex & (C) hippocampus CA1 were examined via western blot from 0 h to 48 h after controlled cortical impact (CCI). Protein expression of RIP1, RIP3 & MLKL in the (D–F) cortex & (G–I) hippocampus CA1 from 0 h to 48 h after CCI was analyzed by statistical. Values are represented as means ± SEM (n = 3–4). (J) Cleaved caspase-3 was detected in cortex & hippocampus CA1 via western blotting from 0 h to 48 h after CCI. (K,L) Protein expression of cleaved caspase-3 in the cortex & hippocampus CA1 from 0 h to 48 h after CCI was measured. Values are represented as means ± SEM (n = 4–5). (M) Cleaved caspase-8 was detected in cortex & hippocampus CA1 via western blotting from 0 h to 48 h after CCI. (N,O) Protein expression of cleaved caspase-8 in the cortex & hippocampus CA1 from 0 h to 48 h after CCI was analyzed. Values are represented as means ± SEM (n = 4–5). beta -actin was used as a control in western blot assays. All data were analyzed by one way ANOVA plus Tukey’s test. *P < 0.05 & **P < 0.01 vs. sham group. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31607859), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-77077_rabbit-polyclonal-ripk1-rip1-antibody-310202416163751.jpg)
![Immunohistochemistry: RIPK1/RIP1 Antibody - BSA Free [NBP1-77077] - Effect of Nec-1, Z-VAD & melatonin on necroptosis. (A) At 6 h after CCI, RIP1, RIP3 & MLKL protein levels in the cortex detected by western blotting were decreased in Nec-1 & melatonin pretreatment groups, but there was no change in the Z-VAD pretreatment group. (B–D) Protein expression of RIP1, RIP3 & MLKL was analyzed by statistical. (E) Immunohistochemistry assays examined the effect of Nec-1, Z-VAD & melatonin on cortex RIP1, RIP3 & MLKL, respectively. (F) At 6 h after CCI, RIP1, RIP3 & MLKL protein levels in the hippocampus CA1 detected by western blotting were decreased in the Nec-1 & melatonin pretreatment groups, but not the Z-VAD pretreatment group. (G–I) Protein expression of RIP1, RIP3 & MLKL was analyzed by statistical. (J) Immunohistochemistry assays examined the effect of Nec-1, Z-VAD & melatonin on RIP1, RIP3 & MLKL in hippocampus CA1, respectively. (K) TdT-mediated dUTP Nick-End Labeling (TUNEL; green) & cleaved caspase-3 (red) dual immunofluorescent labeling was used & were analyzed by statistical (L,M) in the five groups. Values are represented as means ± SEM (n = 3). beta -actin was used as a control in western blot assays. All data were analyzed by one way ANOVA plus Tukey’s test. *P < 0.05 & **P < 0.01 vs. CCI group. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31607859), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-77077_rabbit-polyclonal-ripk1-rip1-antibody-310202416163761.jpg)
![Immunocytochemistry/ Immunofluorescence: RIPK1/RIP1 Antibody - BSA Free [NBP1-77077] - Immunofluorescence of RIPK1/RIP1 in Mouse Kidney cells with RIPK1/RIP1 antibody at 20 ug/mL.](http://images.novusbio.com/fullsize/nbp1-77077_rabbit-polyclonal-ripk1-rip1-antibody-2711202419172268.jpg)
![Western Blot: Caspase-8 Antibody (90A992) [NB100-56527] - Western blot analysis of Caspase-8 in Jurkat cells using Caspase-8 antibody at 1 ug/ml. Cells were treated with 2 uM staurosporine for different time periods. Caspase-8 activation is detected in western blots by the presence of Caspase-8 cleavage fragments. The antibody detected both pro (full length) and active (cleaved) Caspase-8, depending on the treatment time points. A basal level of endogenously cleaved Caspase-8 can be see in untreated Jurkat cells. Goat anti-mouse lg HRP secondary antibody and PicoTect ECL substrate solution were used for this test.](http://images.novusbio.com/fullsize/Caspase-8-Antibody-90A992-Western-Blot-NB100-56527-img0018.jpg "<b>Biological Strategies Validation. </b>Western Blot: Caspase-8 Antibody (90A992) [NB100-56527] - Western blot analysis of Caspase-8 in Jurkat cells using Caspase-8 antibody at 1 ug/ml. Cells were treated with 2 uM staurosporine for different time periods. Caspase-8 activation is detected in western blots by the presence of Caspase-8 cleavage fragments. The antibody detected both pro (full length) and active (cleaved) Caspase-8, depending on the treatment time points. A basal level of endogenously cleaved Caspase-8 can be see in untreated Jurkat cells. Goat anti-mouse lg HRP secondary antibody and PicoTect ECL substrate solution were used for this test.")
![<b>Biological Strategies Validation. </b>Western Blot: Caspase-8 Antibody (90A992) [NB100-56527] - Caspase-8 expression in 786-O and A-498 cellsClose](http://images.novusbio.com/fullsize/Caspase-8-Antibody-90A992-Western-Blot-NB100-56527-img0022.jpg)
![Immunohistochemistry-Paraffin: Caspase-8 Antibody (90A992) [NB100-56527] - Formalin-fixed, paraffin-embedded human spleen (top) and breast (bottom) stained with Caspase-8 antibody at 4 ug/ml. Localization can be cytoplasmic and nuclear. Cancer/normal adjacent tissue array 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.](http://images.novusbio.com/fullsize/Caspase-8-Antibody-90A992-Immunohistochemistry-Paraffin-NB100-56527-img0014.jpg)
![Flow Cytometry: Caspase-8 Antibody (90A992) [NB100-56527] - Flow cytometric analysis of Caspase-8 in HeLa cells using 0.1 ug of Caspase-8 antibody. Shaded histogram represents cells without antibody; green represents isotype control; red represents Caspase-8 antibody. Goat anti-mouse IgG-FITC secondary antibody was used for this test. IC-Flow (Intracellular Staining Flow Cytometry Kit) was used to fix and prepare the cells for staining.](http://images.novusbio.com/fullsize/Caspase-8-Antibody-90A992-Flow-Cytometry-NB100-56527-img0008.jpg)
![Western Blot: Caspase-8 Antibody (90A992) [NB100-56527] - Analysis using the Biotin conjugate of NB100-56527. Detection of human Caspase-8 using Jurkat lysates with NB100-55786 at 2 ug/ml (lane 1) and 0.5 ug/ml (lane 2) dilution. NB100-55786 only detects 55 kDa Caspase-8 in Jurkat cells.](http://images.novusbio.com/fullsize/Caspase-8-Antibody-90A992-Western-Blot-NB100-56527-img0021.jpg)
![Simple Western: Caspase-8 Antibody (90A992) [NB100-56527] - Simple Western lane view shows a specific band for Caspase 8 in 0.5 mg/ml of Hek293 lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/Caspase-8-Antibody-90A992-Simple-Western-NB100-56527-img0019.jpg)
![Western Blot: Caspase-8 Antibody - (Pro and Active) [NBP1-05123] - The level of proteins playing essential roles in programmed cell death (Bax, BcL-2, Cyt c, and caspases 3, 8, and 9) and inflammation (TNF-a) in the heart of hypertensive rats (A) SHR and (B) DOCA-salt, and rats after administration of URB597. The expression of examined protein is shown in comparison to the control. Image collected and cropped by Citeab from the following publication (The Effect of Long-Term Administration of Fatty Acid Amide Hydrolase Inhibitor URB597 on Oxidative Metabolism in the Heart of Rats with Primary and Secondary Hypertension. Molecules (2018) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Caspase-8-Antibody-Pro-and-Active-Western-Blot-NBP1-05123-img0006.jpg "<b>Biological Strategies Validation. </b>Western Blot: Caspase-8 Antibody - (Pro and Active) [NBP1-05123] - The level of proteins playing essential roles in programmed cell death (Bax, BcL-2, Cyt c, and caspases 3, 8, and 9) and inflammation (TNF-a) in the heart of hypertensive rats (A) SHR and (B) DOCA-salt, and rats after administration of URB597. The expression of examined protein is shown in comparison to the control. Image collected and cropped by Citeab from the following publication (The Effect of Long-Term Administration of Fatty Acid Amide Hydrolase Inhibitor URB597 on Oxidative Metabolism in the Heart of Rats with Primary and Secondary Hypertension. Molecules (2018) licensed under a CC-BY license.")
![<b>Biological Strategies Validation. </b>Immunohistochemistry-Paraffin: Caspase-8 Antibody - (Pro and Active) [NBP1-05123] - Formalin-fixed, paraffin-embedded sections from a brain tumor tissue array stained for Caspase-8 expression using NBP1-05123 at 1:2000. A. Anaplastic glioma cores from two different patients, positive (left) and negative (right) staining for caspase-8. B. Higher magnification from the caspase-8 positive (A, left) core.](http://images.novusbio.com/fullsize/Caspase-8-Antibody-Pro-and-Active-Immunohistochemistry-Paraffin-NBP1-05123-img0002.jpg)
![Western Blot: Caspase-8 Antibody - (Pro and Active) [NBP1-05123] - AML12 whole cell lysate. Good specific band is observed. Primary antibody at 1: 2000, secondary antibody at 1: 20000. Skimmed milk as blocking buffer. Western blot image submitted by a verified customer review.](http://images.novusbio.com/fullsize/Caspase-8-Antibody-Pro-and-Active-Western-Blot-NBP1-05123-img0003.jpg)
![Western Blot: Caspase-8 Antibody - (Pro and Active) [NBP1-05123] - The level of proteins playing essential roles in programmed cell death (Bax, BcL-2, Cyt c, & caspases 3, 8, & 9) & inflammation (TNF-alpha ) in the heart of hypertensive rats (A) SHR & (B) DOCA-salt, & rats after administration of URB597. The expression of examined protein is shown in comparison to the control. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30223427), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-05123_rabbit-polyclonal-caspase-8-antibody-pro-and-active-31020241534352.jpg)
![Western Blot: Caspase-8 Antibody - (Pro and Active) [NBP1-05123] - The level of proteins playing essential roles in programmed cell death (Bax, BcL-2, Cyt c, & caspases 3, 8, & 9) & inflammation (TNF-alpha ) in the heart of hypertensive rats (A) SHR & (B) DOCA-salt, & rats after administration of URB597. The expression of examined protein is shown in comparison to the control. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30223427), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-05123_rabbit-polyclonal-caspase-8-antibody-pro-and-active-310202415394532.jpg)
![Western Blot: Caspase-8 Antibody - (Pro and Active) [NBP1-05123] - The level of proteins playing essential roles in programmed cell death (Bax, BcL-2, Cyt c, & caspases 3, 8, & 9) & inflammation (TNF-alpha ) in the heart of hypertensive rats (A) SHR & (B) DOCA-salt, & rats after administration of URB597. The expression of examined protein is shown in comparison to the control. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30223427), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-05123_rabbit-polyclonal-caspase-8-antibody-pro-and-active-31020241535665.jpg)
![Western Blot: TLR3 [p Tyr759] Antibody [NBP2-24904] - Image from verified customer review.](http://images.novusbio.com/fullsize/TLR3-[p-Tyr759]-Antibody-Western-Blot-NBP2-24904-img0003.jpg "Western Blot: TLR3 [p Tyr759] Antibody [NBP2-24904] - Image from verified customer review.")
![Immunocytochemistry/Immunofluorescence: TLR3 [p Tyr759] Antibody [NBP2-24904] - Analysis of IgG, AID and TLR3 (A) and a hyper-IgM (HIGM) syndrome patient (B and C). A and B: Paraformaldehyde-fixed, frozen tonsillar mucosa tissue sections. C. Paraformaldehyde-fixed, mucosal B cells from the colon lamina propria of the HIGM patient. Arrowheads indicate cells co-expressing phospho TLR3, AID, and IgG. Data courtesy of W. Xu. et. al., and the Journal of Immunology](http://images.novusbio.com/fullsize/TLR3-[p-Tyr759]-Antibody-Immunocytochemistry-Immunofluorescence-NBP2-24904-img0002.jpg)
![Western Blot: PARP Antibody (194C1439) - Cleaved [NB100-56599] - Analysis of cleaved PARP in staurosporine-treated Jurkat cells at various time points, antibody at 2 ug/mL. The band corresponding to cleaved PARP is only seen in the treated samples. Anti-mouse Ig HRP conjugate was used in this test.](http://images.novusbio.com/fullsize/PARP-Antibody-194C1439-Cleaved-Western-Blot-NB100-56599-img0004.jpg "<b>Biological Strategies Validation. </b>Western Blot: PARP Antibody (194C1439) - Cleaved [NB100-56599] - Analysis of cleaved PARP in staurosporine-treated Jurkat cells at various time points, antibody at 2 ug/mL. The band corresponding to cleaved PARP is only seen in the treated samples. Anti-mouse Ig HRP conjugate was used in this test.")
![<b>Biological Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: PARP Antibody (194C1439) - Cleaved [NB100-56599] - A431 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-PARP Antibody (194C1439) at 5 ug/ml overnight at 4C and detected with an anti-mouse Dylight 488 (Green) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/PARP-Antibody-194C1439-Cleaved-Immunocytochemistry-Immunofluorescence-NB100-56599-img0005.jpg)
![Western Blot: PARP Antibody (194C1439) - Cleaved [NB100-56599] - Analysis using 293T lysates expressing PARP. Image from verified customer review.](http://images.novusbio.com/fullsize/PARP-Antibody-194C1439-Cleaved-Western-Blot-NB100-56599-img0003.jpg)
![Western Blot: TLR3 Antibody (27N3D4) [NBP2-27404] - Analysis of TLR3 using TLR3 monoclonal antibody. Human intestine (A), human spleen (B), and mouse RAW lysate (C) probed with TLR3 antibody at 2 ug/ml. I goat anti-rat Ig HRP secondary antibody and PicoTect ECL substrate solution were used for this test.](http://images.novusbio.com/fullsize/TLR3-Antibody-27N3D4-Western-Blot-NBP2-27404-img0001.jpg "Western Blot: TLR3 Antibody (27N3D4) [NBP2-27404] - Analysis of TLR3 using TLR3 monoclonal antibody. Human intestine (A), human spleen (B), and mouse RAW lysate (C) probed with TLR3 antibody at 2 ug/ml. I goat anti-rat Ig HRP secondary antibody and PicoTect ECL substrate solution were used for this test.")
![Flow Cytometry: TLR3 Antibody (27N3D4) [NBP2-27404] - Analysis of TLR3 using TLR3 monoclonal antibody. Mouse splenocytes were probed with TLR3 antibody (red) and isotype control antibody (green) at 1 ug/10^6 cells.](http://images.novusbio.com/fullsize/TLR3-Antibody-27N3D4-Flow-Cytometry-NBP2-27404-img0009.jpg)
![Flow Cytometry: TLR3 Antibody (27N3D4) [NBP2-27404] - Analysis using Azide Free version of NBP2-27404. TLR3 using TLR3 monoclonal antibody. Mouse RAW cells and splenocytes were probed with TLR3 antibody (red) and isotype control antibody (green) at 1 ug/10^6 cells.](http://images.novusbio.com/fullsize/TLR3-Antibody-27N3D4-Flow-Cytometry-NBP2-27404-img0006.jpg)
![Flow Cytometry: TLR3 Antibody (27N3D4) [NBP2-27404] - Analysis using Azide Free version of NBP2-27404. TLR3 using TLR3 monoclonal antibody. Mouse RAW cells were probed with TLR3 antibody (red) and isotype control antibody (green) at 0.1 ug/10^6 cells.](http://images.novusbio.com/fullsize/TLR3-Antibody-27N3D4-Flow-Cytometry-NBP2-27404-img0007.jpg)
![Flow Cytometry: TLR3 Antibody (27N3D4) [NBP2-27404] - Analysis of TLR3 using TLR3 monoclonal antibody. Mouse RAW cells were probed with TLR3 antibody (red) and isotype control antibody (green) at 1 ug/10^6 cells.](http://images.novusbio.com/fullsize/TLR3-Antibody-27N3D4-Flow-Cytometry-NBP2-27404-img0008.jpg)
![Flow Cytometry: TLR3 Antibody (27N3D4) - BSA Free [NBP2-27404] - An intracellular stain was performed on THP-1 cells with TLR3 Antibody [27N3D4] NBP2-27405AF700 (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 700.](http://images.novusbio.com/fullsize/nbp2-27404_rat-monoclonal-tlr3-antibody-27n3d4-177202495942.jpg)
![Flow Cytometry: TLR3 Antibody (27N3D4) - BSA Free [NBP2-27404] - An intracellular stain was performed on Raw264.7 cells with TLR3 [27N3D4] Antibody NBP2-27405AF700 (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 700.](http://images.novusbio.com/fullsize/nbp2-27404_rat-monoclonal-tlr3-antibody-27n3d4-17720241044614.jpg)
![Immunohistochemical analysis of paraffin-embedded mouse spleen tissue using MLKL [p Ser345] Antibody (JM92-37). The section was pre-treated using heat mediated antigen retrieval with Tris-EDTA buffer (pH 9.0) for 20 minutes.The tissues were blocked in 5% BSA for 30 minutes at room temperature, washed with ddH2O and PBS, and then probed with the primary antibody for 30 minutes at room temperature. The detection was performed using an HRP conjugated compact polymer system. DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX.](http://images.novusbio.com/fullsize/MLKL-p-Ser345-Antibody-JM92-37-Immunohistochemistry-Paraffin-NBP2-66953-img0004.jpg "Immunohistochemical analysis of paraffin-embedded mouse spleen tissue using MLKL [p Ser345] Antibody (JM92-37). The section was pre-treated using heat mediated antigen retrieval with Tris-EDTA buffer (pH 9.0) for 20 minutes.The tissues were blocked in 5% BSA for 30 minutes at room temperature, washed with ddH2O and PBS, and then probed with the primary antibody for 30 minutes at room temperature. The detection was performed using an HRP conjugated compact polymer system. DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX.")
![Immunohistochemical analysis of paraffin-embedded mouse colon tissue using MLKL [p Ser345] Antibody (JM92-37). The section was pre-treated using heat mediated antigen retrieval with Tris-EDTA buffer (pH 9.0) for 20 minutes. The tissues were blocked in 5% BSA for 30 minutes at room temperature, washed with ddH2O and PBS, and then probed with the primary antibody (1/50) for 30 minutes at room temperature. The detection was performed using an HRP conjugated compact polymer system. DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX.](http://images.novusbio.com/fullsize/MLKL-p-Ser345-Antibody-JM92-37-Immunohistochemistry-Paraffin-NBP2-66953-img0001.jpg)
![Immunohistochemical analysis of paraffin-embedded mouse liver tissue using MLKL [p Ser345] Antibody (JM92-37). The section was pre-treated using heat mediated antigen retrieval with Tris-EDTA buffer (pH 9.0) for 20 minutes. The tissues were blocked in 5% BSA for 30 minutes at room temperature, washed with ddH2O and PBS, and then probed with the primary antibody (1/50) for 30 minutes at room temperature. The detection was performed using an HRP conjugated compact polymer system. DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX.](http://images.novusbio.com/fullsize/MLKL-p-Ser345-Antibody-JM92-37-Immunohistochemistry-Paraffin-NBP2-66953-img0002.jpg)
![Immunohistochemical analysis of paraffin-embedded mouse lung tissue using MLKL [p Ser345] Antibody (JM92-37). The section was pre-treated using heat mediated antigen retrieval with Tris-EDTA buffer (pH 9.0) for 20 minutes. The tissues were blocked in 5% BSA for 30 minutes at room temperature, washed with ddH2O and PBS, and then probed with the primary antibody (1/50) for 30 minutes at room temperature. The detection was performed using an HRP conjugated compact polymer system. DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX.](http://images.novusbio.com/fullsize/MLKL-p-Ser345-Antibody-JM92-37-Immunohistochemistry-Paraffin-NBP2-66953-img0003.jpg)
![Western blot analysis of MLKL [p Ser345] on different lysates with MLKL [p Ser345] Antibody (JM92-37) at 1/1,000 dilution and competitor's antibody at 1/1,000 dilution.Lane 1: L-929 cell lysateLane 2: L929 treated with 20μM Z-VAD for 3.5 hours, then added 100nM SM-164 and 20ng/ml TNF-alpha for 3 hours cell lysateLysates/proteins at 20 µg/Lane.Predicted band size: 54 kDaObserved band size: 54 kDaExposure time: 1 minute 10 seconds;4-20% SDS-PAGE gel.Proteins were transferred to a PVDF membrane and blocked with 5% NFDM/TBST for 1 hour at room temperature. The primary antibody at 1/1,000 dilution and competitor's antibody at 1/1,000 dilution were used in 5% NFDM/TBST at 4℃ overnight. Goat Anti-Rabbit IgG - HRP Secondary Antibody at 1/50,000 dilution was used for 1 hour at room temperature.](http://images.novusbio.com/fullsize/nbp2-66953_rabbit-monoclonal-mlkl-p-ser345-antibody-jm92-37-western-blot-2412024103144..jpg)
![IHC-Frozen:MLKL [p Ser345] Antibody (JM92-37)-Analysis of frozen mouse spleen tissue with Rabbit anti-Phospho-MLKL (S345) antibody at 1/100 dilution.The section was pre-treated using heat mediated antigen retrieval with sodium citrate buffer (pH 6.0) for about 2 minutes in microwave oven. The tissues were blocked in 10% negative goat serum for 1 hour at room temperature, washed with PBS, and then probed with the primary antibody (green) at 1/100 dilution overnight at 4 ℃, washed with PBS. Goat Anti-Rabbit IgG H&L (iFluor™ 488) was used as the secondary antibody at 1/1,000 dilution. Nuclei were counterstained with DAPI (blue).](http://images.novusbio.com/fullsize/nbp2-66953_rabbit-monoclonal-mlkl-p-ser345-antibody-jm92-37-immunocytochemistry-immunofluorescence-3072024102815..jpg)