Recombinant Human Vascular Endothelial Growth Factor B (VEGFB) Protein (His-GST&Myc)

Product Overview Description Recombinant Human Vascular Endothelial Growth Factor B (VEGFB) Protein (His-GST&Myc) is produced by our E.coli expression system. This is a full length protein. Purity Greater than 85% as determined by SDS-PAGE. Uniprotkb P49765 Target Symbol VEGFB Synonyms VEGF-related factor ;VRF Species Homo sapiens (Human) Expression System E.coli Tag N-10His-GST&C-Myc Target Protein Sequence PVSQPDAPGHQRKVVSWIDVYTRATCQPREVVVPLTVELMGTVAKQLVPSCVTVQRCGGCCPDDGLECVPTGQHQVRMQILMIRYPSSQLGEMSLEEHSQCECRPKKKDSAVKPDRAATPHHRPQPRSVPGWDSAPGAPSPADITHPTPAPGPSAHAAPSTTSALTPGPAAAAADAAASSVAKGGA Expression Range 22-207aa Protein Length Full Length of Mature Protein Mol. Weight 54.5 kDa Research Area Cancer Form Liquid or Lyophilized powder Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%. Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C. Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week. 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