Recombinant Human VEGF 121 (aa 207-327) Protein

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Summary
Reactivity HuSpecies Glossary
Applications Bioactivity

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Recombinant Human VEGF 121 (aa 207-327) 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 0.5-3 ng/mL.
Source
E. coli-derived human VEGF protein
Ala207-Arg327, with an N-terminal Met & Pro208-Arg327
Accession #
N-terminal Sequence
Met & Pro208
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
VEGFA
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
14 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.
Publications
Read Publications using
4644-VS 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 HCl with BSA as a carrier protein.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile 4 mM HCl.

Notes

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

Alternate Names for Recombinant Human VEGF 121 (aa 207-327) 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 cysteine-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). VEGF121 is the only form that lacks a basic heparin-binding region and is freely diffusible (4). Mouse embryos expressing only the corresponding isoform (VEGF120) do not survive to term, and show defects in skeletogenesis (5). Human VEGF121 shares 87% aa sequence identity with corresponding regions of mouse and rat, 93% with feline, equine and bovine, and 91%, 95% and 96% with ovine, canine and porcine 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; VEGF121 binding has also been reported (6). 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 (7, 8). Circulating VEGF levels correlate with disease activity in autoimmune diseases such as rheumatoid arthritis, multiple sclerosis and systemic lupus erythematosus (9). VEGF is induced by hypoxia and cytokines such as IL-1, IL-6, IL-8, oncostatin M and TNF-alpha (3, 4, 10).

  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. Zelzer, E. et al. (2002) Development 129:1893.
  6. Pan, Q. et al. (2007) J. Biol. Chem. 282:24049.
  7. Weis, S.M. and D.A. Cheresh (2005) Nature 437:497.
  8. Thurston, G. (2002) J. Anat. 200:575.
  9. Carvalho, J.F. et al. (2007) J. Clin. Immunol. 27:246.
  10. Angelo, L.S. and R. Kurzrock (2007) Clin. Cancer Res. 13:2825.

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4644-VS
Species: Hu
Applications: Bioactivity

Publications for VEGF (4644-VS)(10)

We have publications tested in 3 confirmed species: Human, Mouse, Hamster.

We have publications tested in 3 applications: Bioassay, Surface Plasmon Resonance, Western Blot.


Filter By Application
Bioassay
(7)
Surface Plasmon Resonance
(1)
Western Blot
(1)
All Applications
Filter By Species
Human
(6)
Mouse
(1)
Hamster
(1)
All Species
Showing Publications 1 - 10 of 10.
Publications using 4644-VS Applications Species
C Abou Fayca, S Gazzeri, B Eymin A VEGF-A/SOX2/SRSF2 network controls VEGFR1 pre-mRNA alternative splicing in lung carcinoma cells Sci Rep, 2019;9(1):336. 2019 [PMID: 30674935] (Bioassay, Human) Bioassay Human
S Stephenson, MA Care, I Fan, A Zougman, DR Westhead, GM Doody, RM Tooze Growth Factor-like Gene Regulation Is Separable from Survival and Maturation in Antibody-Secreting Cells J. Immunol., 2019;202(4):1287-1300. 2019 [PMID: 30642980] (Bioassay, Human) Bioassay Human
N Patel, S Able, D Allen, E Fokas, B Cornelisse, FV Gleeson, AL Harris, KA Vallis Monitoring response to anti-angiogenic mTOR inhibitor therapy in vivo using (111)In-bevacizumab EJNMMI Res, 2017;7(1):49. 2017 [PMID: 28560583] (Western Blot) Western Blot
S Kapur, AP Silverman, AZ Ye, N Papo, D Jindal, MS Blumenkran, JR Cochran Engineered ligand-based VEGFR antagonists with increased receptor binding affinity more effectively inhibit angiogenesis Bioeng Transl Med, 2017;2(1):81-91. 2017 [PMID: 28516164] (Bioassay, Human) Bioassay Human
Ahmadova Z, Yagublu V, Forg T, Hajiyeva Y, Jesenofsky R, Hafner M, Keese M Fluorescent resonance energy transfer imaging of VEGFR dimerization. Anticancer Res, 2014;34(5):2123-33. 2014 [PMID: 24778014] (Bioassay, Hamster) Bioassay Hamster
Chen P, Qin L, Zhuang Z, Tellides G, Lax I, Schlessinger J, Simons M The docking protein FRS2alpha is a critical regulator of VEGF receptors signaling. Proc Natl Acad Sci U S A, 2014;111(15):5514-9. 2014 [PMID: 24706887]
Esquibies A, Karihaloo A, Quaggin S, Bazzy-Asaad A, Cantley L Heparin binding VEGF isoforms attenuate hyperoxic embryonic lung growth retardation via a FLK1-neuropilin-1-PKC dependent pathway. Respir Res, 2014;15(0):32. 2014 [PMID: 24641672] (Bioassay, Mouse) Bioassay Mouse
Tannetta D, Dragovic R, Gardiner C, Redman C, Sargent I Characterisation of syncytiotrophoblast vesicles in normal pregnancy and pre-eclampsia: expression of Flt-1 and endoglin. PLoS ONE, 2013;8(2):e56754. 2013 [PMID: 23437230] (Bioassay, Human) Bioassay Human
Martino MM, Hubbell JA The 12th-14th type III repeats of fibronectin function as a highly promiscuous growth factor-binding domain. FASEB J., 2010;24(12):4711-21. 2010 [PMID: 20671107] (Surface Plasmon Resonance, Human) Surface Plasmon Resonance Human
Rennel ES, Varey AH, Churchill AJ, Wheatley ER, Stewart L, Mather S, Bates DO, Harper SJ VEGF(121)b, a new member of the VEGF(xxx)b family of VEGF-A splice isoforms, inhibits neovascularisation and tumour growth in vivo. Br. J. Cancer, 2009;101(7):1183-93. 2009 [PMID: 19707198] (Bioassay, Human) Bioassay Human

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FAQs for VEGF (4644-VS). (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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Blogs on VEGF. Showing 1-10 of 19 blog posts - Show all blog posts.

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?
By Yoskaly Lazo-Fernandez, PhD IntroductionEvidence has accumulated recently indicating that common cancer therapies might stimulate metastasis in a significant number of cancer patients1. In fact, neoadjuvant che...  Read full blog post.

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.

The role of HIF-1 Alpha signaling in the retina under hypoxic conditions
Hypoxia inducible factor 1 (HIF-1) is a protein that plays an essential role in hypoxia, or low levels of cellular oxygen. HIF-1 is a heterodimeric protein that consists of a constitutively expressed beta subunit and oxygen related alpha subunit. ...  Read full blog post.

Using SCP3/SYCP3 Antibodies as Meiosis Markers in Gametogenesis and DNA Repair Studies
The synaptonemal complex (SC) is a protein structure that forms during the synapsis of homologous chromosomes during meiosis. This structure is involved in the processes of chromosome synapsis, genetic recombination and subsequent chromosome segregati...  Read full blog post.

Understanding the relationship between HIF-1 alpha, Hypoxia and Epithelial-Mesenchymal Transition
Epithelial-mesenchymal transition (EMT) is a natural process by which epithelial cells lose their polarity and intercellular adhesion, and gain the migratory invasive properties of mesenchymal stem cells that can differentiate into a variety of cel...  Read full blog post.

Integrin alpha v beta 3 - a target for inhibiting tumor angiogenesis
Integrins are a family of transmembrane proteins involved in diverse processes including cell adhesion, signal transduction, cell migration, and differentiation. They exist as heterodimers consisting of noncovalently linked alpha and beta subunits....  Read full blog post.

Showing 1-10 of 19 blog posts - Show all blog posts.

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Bioinformatics

Gene Symbol VEGFA
Uniprot