Recombinant Human VEGF 165 Biotinylated Protein, CF

R&D Systems, part of Bio-Techne | Catalog # BT293/CF

R&D Systems, part of Bio-Techne
Discontinued Product
BT293/CF has been discontinued. An alternative/replacement product is available: AVI293, BT10543. View all VEGF products.

Key Product Details

Source

Sf 21 (baculovirus)

Accession #

NP_001165097

Structure / Form

Disulfide-linked homodimer; Biotinylated protein via sugars

Conjugate

Biotin

Applications

Bioactivity

View all VEGF Proteins and Enzymes »

Product Specifications

Source

Spodoptera frugiperda, Sf 21 (baculovirus)-derived human VEGF protein
Ala27-Arg191

Purity

>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

Predicted Molecular Mass

19 kDa

Activity

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.

Scientific Data Images for Recombinant Human VEGF 165 Biotinylated Protein, CF

Both Biotinylated Recombinant Human VEGF 165 (Catalog # BT293/CF) and unlabeled Recombinant Human VEGF 165 (Catalog # 293-VE) stimulate HUVEC human umbilical vein endothelial cell proliferation. The ED50 for this effect is 1-6 ng/mL. The similarity in activity highlights that the biotinylayed protein is fully functional.

Formulation, Preparation and Storage

BT293/CF
Formulation Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA.
Reconstitution Reconstitute at 100 μg/mL in 4 mM HCl.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.

Background: VEGF

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, 2). It is a member of the PDGF family that is characterized by the presence of eight conserved cysteine residues and a cystine knot structure (3). Humans express two sets of alternatively spliced isoforms of 121, 145, 165, 183, 189, and 206 amino acids (aa) in length (3, 4). Isoforms other than VEGF121 contain basic heparin-binding regions and are not freely diffusible (3, 4). VEGF165 appears to be the most abundant and potent of the angiogenic isoform set, followed by VEGF121 and VEGF189 (3, 5). The anti-angiogenic or “b” set of isoforms is differentially spliced to contain five alternative amino acids at the C-terminus, and are the more highly expressed isoforms in normal adult tissue (6). VEGF165b, like VEGF121 but unlike most angiogenic isoforms, does not bind heparins and is therefore diffusible (3). 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 VEGF165, respectively. In addition to alternatively spliced VEGF isoforms, multiple fragments of VEGF can be generated by extracellular proteolysis (4). VEGFs bind the type I transmembrane receptor tyrosine kinases VEGF R1 (also called Flt-1) and VEGF R2 (Flk-1/KDR) on endothelial cells (3). Although VEGF affinity is highest for binding to VEGF R1, VEGF R2 appears to be the primary mediator of VEGF angiogenic activity (3, 5). VEGF165 binds the semaphorin receptor, Neuropilin-1 and promotes complex formation with VEGF R2 (7). VEGF is required during embryogenesis to regulate the proliferation, migration, and survival of endothelial cells (3, 5). In adults, VEGF functions mainly in wound healing and the female reproductive cycle (5). Pathologically, it is involved in tumor development and tumor vascular leakage (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 (5, 10).

References

  1. Leung, D.W. et al. (1989) Science 246:1306.
  2. Keck, P.J. et al. (1989) Science 246:1309. 
  3. Robinson, C.J. and S.E. Stringer (2001) J. Cell. Sci. 114:853.
  4. Vempati, P. et al. (2014) Cytokine Growth Factor Rev. 25:1.
  5. Byrne, A.M. et al. (2005) J. Cell. Mol. Med. 9:777. 
  6. Nowak, D.G. et al. (2008) J. Cell Sci. 121:3487.
  7. Pan, Q. et al. (2007) J. Biol. Chem. 282:24049.
  8. Goel, H.L. and A.M. Mercurio (2013) Nat. Rev. Cancer 13:871.
  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.

Long Name

Vascular Endothelial Growth Factor

Alternate Names

MVCD1, VAS, Vasculotropin, VEGF-A, VEGFA, VPF

Entrez Gene IDs

7422 (Human); 22339 (Mouse); 83785 (Rat); 281572 (Bovine); 403802 (Canine); 493845 (Feline); 30682 (Zebrafish)

Gene Symbol

VEGFA

UniProt

NP_001165097

Additional VEGF Products

Product Documents for Recombinant Human VEGF 165 Biotinylated Protein, CF

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Product Specific Notices for Recombinant Human VEGF 165 Biotinylated Protein, CF

For research use only

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