Recombinant Human VEGFB Protein

Name: Recombinant Human VEGFB Protein
Brand: Beta LifeScience
SKU: BL-1720SG
Availability: InStock

Collections: Cytokines and growth factors, Growth factors and receptors, Recombinant proteins

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Product Overview

Tag	N/A
Host Species	Human
Accession	P49765
Background	Vascular endothelial growth factor B (VEGFB) is a homodimeric, heparin-binding glycoprotein member of the VEGF family of growth factors. Compared to VEGFA, VEGFB-€™s main role is the maintenance of newly formed blood vessels and is involved in endothelial cell physiology. It is a ligand for vascular endothelial growth factor receptor 1 (VEGFR1) and neuropilin-1 (NRP1), while the binding of neuropilin-1 to VEGFB186 is proteolysis regulated.
Description	Recombinant Human VEGFB was produced in E. coli. This protein is purified with our unique purification methods.
Source	E.coli
Molecular Weight	19.0 kDa
Purity	For specific purity information on a given lot, see related COA.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability	The recombinant protein is stable for up to 12 months at -70°C
Usage	For Research Use Only
Storage	Recombinant Human VEGFB Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Growth factor for endothelial cells. VEGF-B167 binds heparin and neuropilin-1 whereas the binding to neuropilin-1 of VEGF-B186 is regulated by proteolysis.
Subcellular Location	Secreted. Note=Secreted but remains associated to cells or to the extracellular matrix unless released by heparin.
Protein Families	PDGF/VEGF growth factor family
Database References	HGNC: 12681 OMIM: 601398 KEGG: hsa:7423 STRING: 9606.ENSP00000311127 UniGene: Hs.732095
Tissue Specificity	Expressed in all tissues except liver. Highest levels found in heart, skeletal muscle and pancreas.

Gene Functions References

High plasma VEGF-B levels are associated with type 2 diabetes mellitus. PMID: 28523459
Data from clinical studies point out the changes in circulating or tissue expression levels of VEGF-B in obese compared with lean patients. PMID: 28798193
Cardiac transgenic vascular endothelial growth factor-B overexpression failed to protect heart transplants from ischemia-reperfusion injury. PMID: 27588416
renal VEGF-B expression correlates with the severity of Diabetic Kidney Disease. PMID: 28190774
Data show that metformin treatment reduces serum vascular endothelial growth factor B (VEGF-B) levels and ameliorates insulin resistance. PMID: 26387747
Frameshift mutations of VEGFB gene is associated with stomach and colorectal cancers. PMID: 25633991
fluid shear stress induces the synthesis of Insulin growth factor-2 and vascular endothelial growth factor (VEGF) B and D, which in turn transactivate MMP-12. PMID: 25435370
MMP9 may activate VEGF-B via PI3K/Akt signaling pathway. PMID: 25424698
Roles of vascular endothelial growth factor in amyotrophic lateral sclerosis. PMID: 24987705
Low VEGFB and VEGFD gene expression is associated with early-stage non-small cell lung cancer. PMID: 24145997
Our study suggested that VEGF-B was an angiogenesis factor in vitro and that ERK1/2 and p38-related signaling pathways were involved in these VEGF-B activities. PMID: 24374930
VEGF-B has possible roles in cardiac protection, energy metabolism support, and neuroprotectin [review] PMID: 24987005
High VEGF-B levels might correlate with the presence of hyperlipidemia and target organ damage in type 2 diabetic patients. PMID: 25001655
High VEGFB expression is associated with bone marrow metastasis in neuroblastoma. PMID: 23553333
VEGF-B might be an important ligand in the signalling between the tumor and preexisting blood vessels to ensure a functional blood supply for tumor survival. PMID: 23417498
we report significant associations with overall survival and distant failure for certain VEGF(VEGF-B) family members. PMID: 23728940
Data indicate that three miRs (miR-484, -642, and -217) were able to predict chemoresistance and vasculature of serous epithelial ovarian carcinomas through the regulation of the VEGFB and VEGFR2 pathways. PMID: 23697367
Expression of VEGF-B genes in glioma cell lines U87 is significantly changed under hypoxia and ischemic conditions. PMID: 23350126
In WT1 mutant cells, reduced VEGF(165)b was due to lack of WT1-mediated transcriptional repression of the splicing-factor kinase SRPK1 PMID: 22172722
analysis of binding of vascular endothelial growth factor-B by VEGFR-1(D2) PMID: 20501651
TIMP3 blocks the binding of VEGF to VEGF receptor-2 and inhibits downstream signaling and angiogenesis. PMID: 12652295
Results describe the crystal structure of human vascular endothelial growth factor-B (VEGF-B) and present a predicted model for the association of VEGF-B with the second domain of its receptor, VEGFR-1. PMID: 16616187
Basophils could play a role in angiogenesis and inflammation through the expression of several forms of VEGF-B and their receptors. PMID: 17082651
VEGFB, and receptor were highly expressed in dysplastic neurons. IR in astroglial and balloon cells was observed for VEGFA and its receptors Double-labeling also showed expression of VEGFA, VEGFB and VEGFR-1 in cells of the microglia/macrophage lineage. PMID: 18317782
VEGF-B appears to have a relatively restricted angiogenic activity in the ischemic heart. PMID: 18511699
Increased VEGFB expression is associated with hepatocellular carcinoma PMID: 18537151
Overexpression of vascular endothelial growth factor-B in mouse heart alters cardiac lipid metabolism and induces myocardial hypertrophy. PMID: 18757827
The structural features of the 'highly ordered' interaction of the Fab fragment of the antibody (Fab-2H10) with VEGF-B, is presented. PMID: 18930733
VEGF-B mRNA was not expressed either in normal urothelium or in bladder cancer. PMID: 19424629

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.