详细说明
- Purity>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
- Endotoxin Level<0.01 EU per 1 μg of the protein by the LAL method.
- ActivityMeasured by its binding ability in a functional ELISA. Immobilized rrNeuropilin-1/Fc Chimera at 4 µg/mL (100 µL/well) can bind rmVEGF-B 167 with a linear range of 0.8‑50 ng/mL.
- SourceE. coli-derived Pro22-Lys188
- Accession #
- N-terminal Sequence
AnalysisPro22 - Structure / FormDisulfide-linked homodimer
- Predicted Molecular Mass19 kDa (monomer)
| 2595-VE | | 2595-VE/CF |
| Formulation Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA with BSA as a carrier protein. | Formulation Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA. | |
| Reconstitution Reconstitute at 100 μg/mL in sterile 4 mM HCl containing at least 0.1% human or bovine serum albumin. | Reconstitution Reconstitute at 100 μg/mL in sterile 4 mM HCI. | |
| Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. | 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.
| Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Vascular endothelial growth factor B (VEGF-B; also known as VFR) is a member of the VEGF-PDGF supergene family of growth factor molecules (1 - 4). Five mouse members have been identified, including VEGF-A, -B, -C, -D, and PlGF(-2) (1, 5). VEGF family members are disulfide-linked homo- and heterodimeric proteins that are important regulators of vasculogenesis and lymphangiogenesis. Mouse VEGF-B has two isoforms, a 32 kDa single chain and a 21 kDa single chain form (6, 7). The long form (VEGF-B186) is 207 amino acids (aa) in length, with a 21 aa signal sequence and a 186 aa mature region. The short form (VEGF-B167) is 188 aa in length, with a 21 aa signal sequence and a 167 aa mature segment. Each mature isoform shows the same N-terminal 94 aa that contains a cysteine knot VEGF homology domain (6 - 8). VEGF-B186 is O-glycosylated; VEGF-B167 is not. VEGF-B167 binds heparin; VEGF-B186 does not. Thus, VEGF-B186 is secreted and freely diffusible in tissues (7). However, the VEGF-B167 isoform is the predominant form in tissue (9). Mouse VEGF-B186 is 93% and 87% aa identical to bovine and human VEGF-B186, respectively; mouse VEGF-B167 is 90% and 88% aa identical to bovine and human VEGF-B167, respectively. The mouse VEGF-B167 homodimer is 42 kDa in size, while the VEGF-B186 homodimer is 62 kDa in size. Unlike VEGF167, VEGF-B186 undergoes proteolytic processing that creates a partially processed 48 kDa homodimer and a fully processed 32 kDa homodimer. Processing appears to occur at Arg127 of the mature form (10). Both forms of VEGF-B can heterodimerize with VEGF (7). Both VEGF-B isoforms bind to VEGF receptor 1 (VEGF R1), but not VEGF R2 or VEGF R3 (11). VEGF-B167 also binds neuropilin-1, but only the 127 aa processed form of VEGF-B186 binds neuropilin-1 (10). As a dimer, full length VEGF-B186 does not interact with neuropilin-1, while any dimer that contains the processed VEGF-B127 subunit will interact with neuropilin-1 (10). The importance of differential neuropilin binding is unclear. VEGF-B deficient mice display an atrial conduction deficit (12). On endothelial cells, ligation of VEGF R1 by VEGF-B has been shown to regulate the expression and activity of urokinase type plasminogen activator and plasminogen activator inhibitor 1 (11).
- References:
- Li, X. and U. Eriksson (2001) Int. J. Biochem Cell Biol. 33:421.
- Olofsson, B. et al. (1999) Curr. Opin. Biotechnol. 10:528.
- Clauss, M. (2000) Semin. Thromb. Hemost. 26:561.
- Matsumoto, T. and L. Claesson-Welsh (2001) Sci STKE Dec. 11(112):RE21.
- DiPalma, T. et al. (1996) Mamm. Genome 7:6.
- Olofsson, B. et al. (1996) Proc. Natl. Acad. Sci. USA 93:2576.
- Olofsson, B. et al. (1996) J. Biol. Chem. 271:19310.
- Twonson, S. et al. (1996) Biochem. Biophys. Res. Commun. 220:922.
- Li, X. et al. (2001) Growth Factors 19:49.
- Makinen, T. et al. (1999) J. Biol. Chem. 274:21217.
- Olofsson, B. et al. (1998) Proc. Nat. Acad. Sci. USA 95:11709.
- Aase, K. et al. (2001) Circulation 104:358.
- Long Name:Vascular Endothelial Growth Factor B
- Entrez Gene IDs:7423 (Human); 22339 (Mouse)
- Alternate Names:vascular endothelial growth factor B; VEGFB; VEGF-B; VEGF-related factor; VRFVEGFL
400-6226-992