Recombinant Human VEGF-B 167 Protein, CF

Name: Recombinant Human VEGF-B 167 Protein, CF
Brand: R&D Systems
SKU: 751-VE
Rating: 3 (1 reviews)

Catalog #: 751-VE
7 Citations 1 Review Datasheet / COA / SDS

Newer Version Available: 751-VEB

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751-VE has been discontinued and is replaced by 751-VEB.

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Citations (7)

FAQs

Reviews (1)

Summary Product Datasheets Carrier Free Data Images Reconstitution Calculator Background Related Research Areas

Recombinant Human VEGF-B 167 Protein, CF Summary

Product Specifications

Purity

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Endotoxin Level

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

Activity

Measured by its binding ability in a functional ELISA. Immobilized recombinant rat Neuropilin-1 Fc Chimera at 4 µg/mL (100 µL/well) can bind
recombinant human VEGF-B₁₆₇ with a linear range of 0.3-20 ng/mL.

Source

E. coli-derived human VEGF-B protein
Pro22-Arg188

Accession #

AAA91463

N-terminal Sequence
Analysis

Pro22

Structure / Form

Disulfide-linked homodimer

Predicted Molecular Mass

19 kDa (monomer)

Product Datasheets

751-VE

Product Datasheet

COA

SDS

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

751-VE

Formulation	Lyophilized from a 0.2 μm filtered solution in HCl.
Reconstitution	Reconstitution in 4 mM HCl at 500 ug/mL.
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.

Reconstitution Calculator

Background: VEGF-B

Vascular endothelial growth factor B (VEGF-B), also known as vascular endothelial growth factor-related factor (VRF), is a member of the VEGF family of growth factors that share structural and functional similarity (1, 2). Five mammalian members, including VEGF-A, -B, -C, -D and PlGF, have been identified. VEGF family members are disulfide-linked dimeric proteins that are important regulators of physiological and pathological vasculogenesis, angiogenesis and lymphangiogenesis. VEGF-B is expressed in most tissues, especially in heart, skeletal muscle and pancreas. In many tissues, VEGF-B is co-expressed and can heterodimerize with VEGF (3). By alternative splicing, two isoforms of mature VEGF-B containing 167 or 186 amino acid (aa) residues exist (3, 4). The two VEGF-B isoforms have identical amino-terminal cysteine-knot VEGF homology domains but the carboxyl end of VEGF-B₁₆₇ differs from that of VEGF-B₁₈₆ by the presence of a highly basic cysteine-rich heparin binding domain. Whereas VEGF-B₁₈₆ is a secreted diffusible protein, VEGF-B₁₆₇ is sequestered into the cell matrix after secretion. Both VEGF-B isoforms bind VEGF receptor 1 (VEGF R1), but not VEGF R2 or VEGF R3 (5). 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. VEGF-B₁₆₇ and a proteolytically processed form of VEGF-B₁₈₆ (VEGF-B₁₂₇) also bind neuropilin-1 (NP-1), a type I transmembrane receptor for semaphorins/collapsins, ligands involved in neuron guidance (6). Besides VEGF-B, NP‑1 has been shown to bind PLGF-2, VEGF₁₆₅ and VEGF R1 (6, 7). The many interactions of NP-1 with VEGF ligands and receptor suggests that NP-1 may function as a regulator of angiogenesis (7).

References

Li, X. and U. Eriksson (2001) Int. J. Biochem Cell Biol. 33:421.
Olofsson, B. et al. (1999) Curr. Opin. Biotechnol. 10:528.
Olofsson, B. et al. (1996) Proc. Nat. Acad. Sci. USA 93:2576.
Grimmond, S. et al. (1996) Benome Res. 6:124.
Olofsson, B. et al. (1998) Proc. Nat. Acad. Sci. USA 95:11709.
Makinen, T. et al. (1999) J. Biol. Chem. 274:21217.
Fuh, G. et al. (2000) J. Biol. Chem. 275:26690.

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

Related Research Areas

Citations for Recombinant Human VEGF-B 167 Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

7 Citations: Showing 1 - 7
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Systemic VEGF-A neutralization ameliorates diet-induced metabolic dysfunction.
Authors: Wu L, Meoli C, Mangiafico S, Fazakerley D, Cogger V, Mohamad M, Pant H, Kang M, Powter E, Burchfield J, Xirouchaki C, Mikolaizak A, Stockli J, Kolumam G, van Bruggen N, Gamble J, Le Couteur D, Cooney G, Andrikopoulos S, James D
Diabetes, 2014-04-02;63(8):2656-67.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay
Placental growth factor neutralising antibodies give limited anti-angiogenic effects in an in vitro organotypic angiogenesis model.
Authors: Brave SR, Eberlein C, Shibuya M, Wedge SR, Barry ST
Angiogenesis, 2010-10-16;13(4):337-47.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay
The 12th-14th type III repeats of fibronectin function as a highly promiscuous growth factor-binding domain.
Authors: Martino MM, Hubbell JA
FASEB J., 2010-07-29;24(12):4711-21.
Species: Human
Sample Types: Recombinant Protein
Applications: Surface Plasmon Resonance
Multiple receptor tyrosine kinases regulate HIF-1alpha and HIF-2alpha in normoxia and hypoxia in neuroblastoma: implications for antiangiogenic mechanisms of multikinase inhibitors.
Authors: Nilsson MB, Zage PE, Zeng L, Xu L, Cascone T, Wu HK, Saigal B, Zweidler-McKay PA, Heymach JV
Oncogene, 2010-03-08;29(20):2938-49.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay
Modulation of angiogenesis by a tetrameric tripeptide that antagonizes vascular endothelial growth factor receptor 1.
Authors: Ponticelli S, Marasco D, Tarallo V, Albuquerque RJ, Mitola S, Takeda A, Stassen JM, Presta M, Ambati J, Ruvo M, De Falco S
J. Biol. Chem., 2008-10-15;283(49):34250-9.
Species: Human
Sample Types: N/A
Applications: ELISA (Standard)
Ligand-induced internalization selects use of common receptor neuropilin-1 by VEGF165 and semaphorin3A.
Authors: Narazaki M, Tosato G
Blood, 2006-01-19;107(10):3892-901.
Applications: ELISA (Standard)
Vascular endothelial growth factor-B promotes in vivo angiogenesis.
Authors: Silvestre JS, Tamarat R, Ebrahimian TG, Le-Roux A, Clergue M, Emmanuel F, Duriez M, Schwartz B, Branellec D, Levy BI
Circ. Res., 2003-06-12;93(2):114-23.
Species: Mouse
Sample Types: In Vivo
Applications: In Vivo