Recombinant Human VEGF 165b Protein, CF


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Reactivity HuSpecies Glossary
Applications Bioactivity

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Recombinant Human VEGF 165b Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. Serially diluted Recombinant Human (rh) VEGF165b is added to a Recombinant Human VEGF R2/KDR/Flk‑1 Fc Chimera (Catalog # 357-KD) coated plate (2 μg/mL, 100 μL/well). Bound rhVEGF165b is detected by a human VEGF165b specific antibody (Catalog # MAB3045). The concentration of rhVEGF165b that produces half-maximum response is approximately 0.12-0.6 nM.
Spodoptera frugiperda, Sf 21 (stably transfected)-derived human VEGF protein
Accession #
N-terminal Sequence
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.


Theoretical MW
19.1 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.
20-21 kDa, reducing conditions
Read Publications using
3045-VE/CF in the following applications:

Packaging, Storage & Formulations

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.
Lyophilized from a 0.2 μm filtered solution in PBS.
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in PBS.


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

Alternate Names for Recombinant Human VEGF 165b Protein, CF

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


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 two sets of 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 of the angiogenic isoform set, followed by VEGF121 and VEGF189 (3, 4). The anti-angiogenic or “b” set of isoforms is differentially spliced to contain six alternate amino acids at the C-terminus, and are the more highly expressed isoforms in normal adult tissue (5). VEGF165b, like VEGF121 but unlike most angiogenic isoforms, does not bind heparins and is therefore diffusible (4, 6). Human VEGF165b 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 VEGF165b, respectively. VEGFs bind 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). The affinity of VEGF165b for VEGF R2 is similar to that of VEGF165, but VEGF165b only partially activates VEGF R2 such that the kinase regulatory site Y1054 is not phosphorylated (6). VEGF165b also does not bind neuropilin-1, suggesting that the functional difference between VEGF165 and VEGF165b maybe due to either the lack of neuropilin-1 co-signaling or unique downstream signaling activated by VEGF165b (8). Since VEGF165b may compete with angiogenic VEGFs for VEGF R2 sites, its ectopic expression in tumors has been shown to inhibit their growth (7).

  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. Nowak, D.G. et al. (2008) J. Cell Sci. 121:3487.
  6. Kawamura, H. et al. (2008) Cancer Res. 68:4683.
  7. Rennel, E.S. et al. (2008) Br. J. Cancer 98:1250.
  8. Harper S.J. and Bates D.O. (2008) Nat. Rev. Cancer 8(11):880.

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Publications for VEGF (3045-VE/CF)(5)

We have publications tested in 4 confirmed species: Human, Rat, Bovine, N/A.

We have publications tested in 3 applications: Bioassay, In Vivo, Western Blot.

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Showing Publications 1 - 5 of 5.
Publications using 3045-VE/CF Applications Species
A Boudria, C Abou Fayca, T Jia, S Gout, M Keramidas, C Didier, N Lemaître, S Manet, JL Coll, AC Toffart, D Moro-Sibil, C Albiges-Ri, V Josserand, E Faurobert, C Brambilla, E Brambilla, S Gazzeri, B Eymin VEGF165b, a splice variant of VEGF-A, promotes lung tumor progression and escape from anti-angiogenic therapies through a ?1 integrin/VEGFR autocrine loop Oncogene, 2018;0(0):. 2018 [PMID: 30194450] (Bioassay, Human) Bioassay Human
A Jahangiri, A Nguyen, A Chandra, MK Sidorov, G Yagnik, J Rick, SW Han, W Chen, PM Flanigan, D Schneidman, S Mascharak, M De Lay, B Imber, CC Park, K Matsumoto, K Lu, G Bergers, A Sali, WA Weiss, MK Aghi Cross-activating c-Met/?1 integrin complex drives metastasis and invasive resistance in cancer Proc. Natl. Acad. Sci. U.S.A., 2017;0(0):. 2017 [PMID: 28973887] (Bioassay, Human) Bioassay Human
HL Deissler, GK Lang, GE Lang Inhibition of Single Routes of Intracellular Signaling is Not Sufficient to Neutralize the Biphasic Disturbance of a Retinal Endothelial Cell Barrier Induced by VEGF-A165 Cell. Physiol. Biochem., 2017;42(4):1493-1513. 2017 [PMID: 28719888] (Bioassay, Bovine) Bioassay Bovine
The control of alternative splicing by SRSF1 in myelinated afferents contributes to the development of neuropathic pain Neurobiol Dis, 2016;96(0):186-200. 2016 [PMID: 27616424] (In Vivo, Rat) In Vivo Rat
Bates, David O, Mavrou, Athina, Qiu, Yan, Carter, James G, Hamdollah-Zadeh, Maryam, Barratt, Shaney, Gammons, Melissa, Millar, Ann B, Salmon, Andrew H, Oltean, Sebastia, Harper, Steven J Detection of VEGF-A(xxx)b isoforms in human tissues. PLoS ONE, 2013;8(7):e68399. 2013 [PMID: 23935865] (Western Blot, N/A) Western Blot N/A

Reviews for VEGF (3045-VE/CF) (0)

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FAQs for VEGF (3045-VE/CF). (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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Gene Symbol VEGFA