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Recombinant Human VEGF 165 Protein

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Recombinant Human VEGF165(Catalog # 293-VE) stimulates proliferation in HUVEC human umbilical vein endothelial cells. The ED50 is 1-6 ng/mL.
As an alternative, please consider our next generation Recombinant Human VEGF 165 (Catalog # BT-VEGF). It has equivalent bioactivity to Recombinant Human VEGF 165 (Catalog # 293-VE). It combines R&D Systems quality with ...read more
1 μg/lane of Recombinant Human VEGF165was resolved by SDS-PAGE with silver staining, under reducing (R) and non-reducing (NR) conditions, showing major bands at 20-22 kDa and 39-42 kDa, respectively. Multiple bands in ...read more

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Reactivity HuSpecies Glossary
Applications Bioactivity

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Recombinant Human VEGF 165 Protein Summary

Details of Functionality
Measured in a cell proliferation assay using HUVEC human umbilical vein endothelial cells. Conn, G. et al. (1990) Proc. Natl. Acad. Sci. USA 87:1323. The ED50 for this effect is 1-6 ng/mL.
Source
Spodoptera frugiperda, Sf 21 (baculovirus)-derived human VEGF protein
Ala27-Arg191
Accession #
N-terminal Sequence
Ala27
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
VEGFA
Purity
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
19.2 kDa (monomer).
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
20-22 kDa, under reducing conditions.
39-42 kDa, under non-reducing conditions.
Publications
Read Publications using
293-VE in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA with BSA as a carrier protein.
Purity
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. Alternatively, reconstitute at 100‑500 μg/mL in sterile 4 mM HCl containing 0.1% human or bovine serum albumin.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human VEGF 165 Protein

  • MVCD1
  • VAS
  • vascular endothelial growth factor A
  • Vascular permeability factor
  • Vasculotropin
  • VEGF
  • VEGFA
  • VEGF-A
  • VEGFMGC70609
  • VPF
  • VPFvascular endothelial growth factor

Background

Vascular endothelial growth factor (VEGF or VEGF-A), also known as vascular permeability factor (VPF), is a potent mediator of both angiogenesis and vasculogenesis in the fetus and adult (1-3). It is a member of the PDGF family that is characterized by the presence of eight conserved cysteine residues and a cystine knot structure (4). Humans express alternately spliced isoforms of 121, 145, 165, 183, 189, and 206 amino acids (aa) in length (4). VEGF165 appears to be the most abundant and potent isoform, followed by VEGF121 and VEGF189 (3, 4). Isoforms other than VEGF121 contain basic heparin-binding regions and are not freely diffusible (4). Human VEGF165 shares 88% aa sequence identity with corresponding regions of mouse and rat, 96% with porcine, 95% with canine, and 93% with feline, equine and bovine VEGF, respectively. VEGF binds the type I transmembrane receptor tyrosine kinases VEGF R1 (also called Flt-1) and VEGF R2 (Flk-1/KDR) on endothelial cells (4). Although VEGF affinity is highest for binding to VEGF R1, VEGF R2 appears to be the primary mediator of VEGF angiogenic activity (3, 4). VEGF165 binds the semaphorin receptor, Neuropilin-1 and promotes complex formation with VEGF R2 (5). VEGF is required during embryogenesis to regulate the proliferation, migration, and survival of endothelial cells (3, 4). In adults, VEGF functions mainly in wound healing and the female reproductive cycle (3). Pathologically, it is involved in tumor angiogenesis and vascular leakage (6, 7). Circulating VEGF levels correlate with disease activity in autoimmune diseases such as rheumatoid arthritis, multiple sclerosis and systemic lupus erythematosus (8). VEGF is induced by hypoxia and cytokines such as IL-1, IL-6, IL-8, oncostatin M and TNF-alpha (3, 4, 9).

Due to its role in angiogenesis of blood vessels, tumor and stroma cells use VEGF to stimulate formation of blood vessels and the proliferation and survival of endothelial cells. Specific immunotherapies targeting the VEGF signaling pathway include the recombinant antibody against VEGF (Bevacizumab), antibodies targeting the main VEGF receptor (VEGFR2), and small molecule inhibitors against VEGF receptor tyrosine kinases (10). Immune checkpoint inhibitors are an important tool in cancer therapies as tumor cells can hijack immune checkpoint signals to evade detection by immune cells. In addition to stimulating the formation of tumor blood vessels, VEGF has immunosuppressive effects by acting on dendritic cells to block their antigen-presenting and T cell stimulatory functions. Targeting VEGF in combination with other immune checkpoint ligands or receptors may prove more effective in immunotherapy approaches to certain cancer types (11). Because of its role in the formation of blood vessels, VEGF is also an important factor in skeletal development where blood supply and vascularization are crucial. This has made VEGF an important molecule in regenerative studies for bone repair as sustained release of VEGF has been shown to improve the efficiency of bone regeneration (12).

In differentiation protocols for stems cells, VEGF is a commonly added growth factor for the transformation of induced pluripotent stem cells into hematopoietic progenitor cells used to make Natural Killer cells (13, 14). VEGF has also been used to transform intermediate mesoderm into kidney glomerular podocytes or stem cell-derived liver spheres (15, 16). VEGF may also be used in assistance of stem cell transplantations by supporting angiogenesis at sites of stem cell transplants or as a honing tool for adipose-derived mesenchymal stem cells or bone marrow stem cells to migrate to (17, 18).
  1. Leung, D.W. et al. (1989) Science 246:1306.
  2. Keck, P.J. et al. (1989) Science 246:1309.
  3. Byrne, A.M. et al. (2005) J. Cell. Mol. Med. 9:777.
  4. Robinson, C.J. and S.E. Stringer (2001) J. Cell. Sci. 114:853.
  5. Pan, Q. et al. (2007) J. Biol. Chem. 282:24049.
  6. Weis, S.M. and D.A. Cheresh (2005) Nature 437:497.
  7. Thurston, G. (2002) J. Anat. 200:575.
  8. Carvalho, J.F. et al. (2007) J. Clin. Immunol. 27:246.
  9. Angelo, L.S. and R. Kurzrock (2007) Clin. Cancer Res. 13:2825.
  10. Apte, R.S. et al. (2019) Cell 176(6):1248.
  11. Sangro, B. et al. (2021) Nature 18:525-543.
  12. Hu, K. & Olsen, B.R. (2016) Bone 91:30-38.
  13. Zhou, Y. et al. (2022) Cancers 14:2266.
  14. Li, Y. et al. (2018) Cell Stem Cell 23(2):181-192.
  15. Musah, S. et al. (2018) Nat. Protoc. 13(7):1662-1685.
  16. Meseguer-Ripolles, J. et al. (2021) STAR Protoc. 2(2):100502.
  17. Hutchings, G. et al. (2020) Int. J. Mol. Sci. 21(11):3790.
  18. Zhang, W. et al. (2014) Euro Cell and Mater. 27:1-12.

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Publications for VEGF (293-VE)(449)

We have publications tested in 20 confirmed species: Human, Mouse, Rat, Avian - Quail, Bovine, Canine, Chicken, N/A, Porcine, Primate - Callitrix jacchus (Common Marmoset), Primate - Chlorocebus sabaeus (Green Monkey), Primate - Macaca fascicularis (Crab-eating Monkey or Cynomolgus Macaque), Primate - Macaca mulatta (Rhesus Macaque), Rabbit, Rats, Sheep, Transgenic Mouse, Transgenic Rabbit, Xenopus, Zebrafish.

We have publications tested in 21 applications: Binding Analysis, Binding Assay, Bioassay, Cell Culture, Differentiation, ELISA, ELISA (Capture), ELISA (Standard), ELISA Capture, ELISA Development, Immunoassay Development, Immunoassay Standard, In Vivo, In vivo assay, Mass Spectrometry, Organ Culture, Quantum Dot, Stimulation, Surface Plasmon Resonance, Surface Plasmon Resonance (SPR, Western Blot.


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Binding Analysis
(1)
Binding Assay
(3)
Bioassay
(363)
Cell Culture
(18)
Differentiation
(2)
ELISA
(1)
ELISA (Capture)
(3)
ELISA (Standard)
(6)
ELISA Capture
(4)
ELISA Development
(1)
Immunoassay Development
(1)
Immunoassay Standard
(1)
In Vivo
(45)
In vivo assay
(1)
Mass Spectrometry
(1)
Organ Culture
(1)
Quantum Dot
(1)
Stimulation
(1)
Surface Plasmon Resonance
(3)
Surface Plasmon Resonance (SPR
(1)
Western Blot
(6)
All Applications
Filter By Species
Human
(345)
Mouse
(59)
Rat
(11)
Avian - Quail
(1)
Bovine
(11)
Canine
(2)
Chicken
(5)
N/A
(3)
Porcine
(5)
Primate - Callitrix jacchus (Common Marmoset)
(1)
Primate - Chlorocebus sabaeus (Green Monkey)
(1)
Primate - Macaca fascicularis (Crab-eating Monkey or Cynomolgus Macaque)
(1)
Primate - Macaca mulatta (Rhesus Macaque)
(1)
Rabbit
(4)
Rats
(1)
Sheep
(1)
Transgenic Mouse
(1)
Transgenic Rabbit
(1)
Xenopus
(1)
Zebrafish
(1)
All Species
Showing Publications 1 - 10 of 449. Show All 449 Publications.
Publications using 293-VE Applications Species
Keller, S;Kunz, U;Schmid, U;Beusmans, J;Büchert, M;He, M;Jayadeva, G;Le Tourneau, C;Luedtke, D;Niessen, HG;Oum'hamed, Z;Pleiner, S;Wang, X;Graeser, R; Comprehensive biomarker and modeling approach to support dose finding for BI 836880, a VEGF/Ang-2 inhibitor Journal of translational medicine 2024-10-14 [PMID: 39402675] (Mass Spectrometry, N/A) Mass Spectrometry N/A
Lee, H;Xie, T;Kang, B;Yu, X;Schaffter, SW;Schulman, R; Plug-and-play protein biosensors using aptamer-regulated in vitro transcription Nature communications 2024-09-12 [PMID: 39266511] (Bioassay, Human) Bioassay Human
Lekkala, VKR;Shrestha, S;Al Qaryoute, A;Dhinoja, S;Acharya, P;Raheem, A;Jagadeeswaran, P;Lee, MY; Enhanced Maturity and Functionality of Vascularized Human Liver Organoids through 3D Bioprinting and Pillar Plate Culture bioRxiv : the preprint server for biology 2024-08-22 [PMID: 39229042] (Bioassay, Human) Bioassay Human
Xu, W;Wang, Z;Liu, T;Ma, X;Jiao, M;Zhao, W;Yu, L;Hua, Y;Cai, Z;Li, J;Zhang, T; Eurycomanone inhibits osteosarcoma growth and metastasis by suppressing GRP78 expression Journal of ethnopharmacology 2024-08-18 [PMID: 39163893] (Bioassay, Human) Bioassay Human
Kent, GM;Atkins, MH;Lung, B;Nikitina, A;Fernandes, IM;Kwan, JJ;Andrews, TS;MacParland, SA;Keller, GM;Gage, BK; Human liver sinusoidal endothelial cells support the development of functional human pluripotent stem cell-derived Kupffer cells Cell reports 2024-08-14 [PMID: 39146183] (Bioassay, Human) Bioassay Human
Bisson, JA;Gordillo, M;Kumar, R;de Silva, N;Yang, E;Banks, KM;Shi, ZD;Lee, K;Yang, D;Chung, WK;Huangfu, D;Evans, T; GATA6 regulates WNT and BMP programs to pattern precardiac mesoderm during the earliest stages of human cardiogenesis bioRxiv : the preprint server for biology 2024-07-11 [PMID: 39026742] (Bioassay, Human) Bioassay Human
Moon, SY;Kim, HJ;Kim, JK;Kim, J;Choi, JS;Won, SY;Park, K;Lee, SHS; An examination of the mechanisms driving the therapeutic effects of an AAV expressing a soluble variant of VEGF receptor-1 PloS one 2024-07-11 [PMID: 38990973] (ELISA Capture, Human) ELISA Capture Human
Landau, S;Zhao, Y;Hamidzada, H;Kent, GM;Okhovatian, S;Lu, RXZ;Liu, C;Wagner, KT;Cheung, K;Shawky, SA;Vosoughi, D;Beroncal, EL;Fernandes, I;Cummins, CL;Andreazza, AC;Keller, GM;Epelman, S;Radisic, M; Primitive macrophages enable long-term vascularization of human heart-on-a-chip platforms Cell stem cell 2024-06-20 [PMID: 38908380] (Bioassay, Human) Bioassay Human
??, Ö;Wang, X;Reddy, JS;Min, Y;Yilmaz, E;Bhattarai, P;Patel, T;Bergman, J;Quicksall, Z;Heckman, MG;Tutor-New, FQ;Can Demirdogen, B;White, L;Koga, S;Krause, V;Inoue, Y;Kanekiyo, T;Cosacak, MI;Nelson, N;Lee, AJ;Vardarajan, B;Mayeux, R;Kouri, N;Deniz, K;Carnwath, T;Oatman, SR;Lewis-Tuffin, LJ;Nguyen, T;Alzheimer’s Disease Neuroimaging Initiative, ;Carrasquillo, MM;Graff-Radford, J;Petersen, RC;Jr Jack, CR;Kantarci, K;Murray, ME;Nho, K;Saykin, AJ;Dickson, DW;Kizil, C;Allen, M;Ertekin-Taner, N; Gliovascular transcriptional perturbations in Alzheimer's disease reveal molecular mechanisms of blood brain barrier dysfunction Nature communications 2024-06-20 [PMID: 38902234] (Bioassay, Human) Bioassay Human
Paul, SK;Oshima, M;Patil, A;Sone, M;Kato, H;Maezawa, Y;Kaneko, H;Fukuyo, M;Rahmutulla, B;Ouchi, Y;Tsujimura, K;Nakanishi, M;Kaneda, A;Iwama, A;Yokote, K;Eto, K;Takayama, N; Retrotransposons in Werner syndrome-derived macrophages trigger type I interferon-dependent inflammation in an atherosclerosis model Nature communications 2024-06-10 [PMID: 38858384] (Bioassay, Human) Bioassay Human
Show All 449 Publications.

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FAQs for VEGF (293-VE). (Showing 1 - 1 of 1 FAQs).

  1. Why is the molecular weight of VEGF different from the similar antibody, for some companies the the molecular weight is 40KD)?
    • I can't comment on another company's antibody because I don't have any information about their products. I can tell you that VEGF is expressed in a variety of isoforms and is subject to various post-translational modifications that influence its apparent molecular weight in an SDS-PAGE gel compared to the theoretical molecular weight.

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Understanding ‘Y’ in Breast Cancer: Crucial Role of DNA/RNA-binding Protein YB-1 in the Development, Pre-Invasive, and Metastatic Phases
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Detecting HIF alpha and beyond: Best controls for hypoxia Western blot analysis
By Rosa Moreno, PhD. Detecting HIF alpha and beyond: Best controls for hypoxia Western blot analysisPhysiological low levels of oxygen induce normal hypoxic events across biological systems. This hypoxic state activ...  Read full blog post.

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By Jamshed Arslan, Pharm. D., PhD. Stroke    is a leading cause of mortality and morbidity worldwide. Cellular players – neurons, astrocytes, endothelial and stromal cells – involved in post-stroke repair t...  Read full blog post.

mTOR Signaling and the Tumor Microenvironment
By Yoskaly Lazo-Fernandez, PhD The mammalian target of rapamycin (mTOR) is a conserved serine/threonine kinase that, as a member of two distinct intracellular protein complexes, mTORC1 and mTORC2, regulates protein ...  Read full blog post.

Chemotherapy-induced metastasis: An unexpected foe?
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Getting Physical: Link between Lipid Metabolism and Hypoxia Target Genes
By Jamshed Arslan Pharm.D. von Hippel-Lindau (VHL) disease is associated with tumors arising in multiple organs. Activation of hypoxia-inducible factor (HIF)-alpha underlies the VHL disease pathogenesis. In normoxia...  Read full blog post.

The role of HIF-2 alpha in the progression and therapy of clear cell renal cell carcinoma
HIF-2 alpha, also known as hypoxia-inducible factor 2, endothelial PAS domain protein-1, and member of PAS superfamily 2 is part of the HIF family of proteins.  The HIF family is composed of HIF-1, HIF-2 and HIF-3, where HIF-2 is a dimeric protein ...  Read full blog post.

The application of CD31/Pecam-1 (MEC 7.46) in breast cancer research
CD31/PECAM-1, or platelet endothelial cell adhesion molecule 1, is a 130-kDa glycoprotein expressed on vascular and hematopoietic cells.  Depending on the cell type, CD31/PECAM-1 expression can be largely localized to cell junctions, playing a rol...  Read full blog post.

The dynamic use of a PCNA antibody in fish, porcine and primate species
Proliferating cell nuclear antigen (PCNA) plays a crucial role in nucleic acid metabolism as it pertains to DNA replication and repair.  Most noted for its activation of subunits of DNA polymerase, it has also been found to interact with cell-cycl...  Read full blog post.

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Bioinformatics

Gene Symbol VEGFA
Uniprot