Human VEGF165

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Cat-Nr.300-035S
Size2 µg
Price70 €
SourceInsect cells
Formulationlyophilized
Purity Confirmation> 95% by SDS-PAGE
Length [aa]165
Molecular Weight45.0 kDa
N Terminal SequenceAPMAEGG
Biological ActivityThe ED50 for stimulation of cell proliferation by human umbilical vein endothelial cells for VEGF165 has been determined to be in the range of 1-4 ng/ml.
Species ReactivityHuman
Buffer50mM acetic acid
ReconstitutionThe lyophilized VEGF165 should be reconstituted in 50 mM acetic acid to a concentration not lower than 50 µg/ml. For long term storage we recommend to add at least 0.1% human or bovine serum albumin.
Stability and StorageLyophilized samples are stable for greater than six months at -20°C to -70°C. Reconstituted VEGF165 should be stored in working aliquots at -20°C.
Synonymsvascular endothelial growth factor A; VEGFA; VPF; VEGF; MVCD1
DescriptionHuman Vascular Endothelial Growth Factor VEGF165, a 23 kDa protein consisting of 165 amino acid residues, is produced as a homodimer. VEGF is a polypeptide growth factor and a member of the platelet-derived growth factor family. It is a specific mitogen for vascular endothelial cells and a strong angiogenic factor in vivo. Two high-affinity tyrosine kinase receptors for VEGF165 have been identified, VEGFR-1 (FLT-1), and VEGFR-2 (KDR). Consistent with the endothelial cell-specific action of VEGF165, expression of both receptor genes has been found predominantly but not exclusively on endothelial cells. Expression of VEGFR-1 was also found on human monocytes, neutrophils (PMNs), bovine brain pericytes and villous and extra villous trophoblast. In addition to its action as a mitogen it is a potent vascular permeability factor (VPF) in vivo. VEGF165 is also a chemo attractant molecule for monocytes and endothelial cells. 5 different proteins are generated by differential splicing: VEGF121, VEGF145, VEGF165, VEGF189 and VEGF206. The most abundant form is VEGF165. Whereas VEGF121 and VEGF165 are secreted proteins, VEGF145, VEGF189 and VEGF206 are strongly cell-associated. The isoforms VEGF145, VEGF165 and VEGF189 bind to heparin with high affinity. VEGF165 is apparently a homo-dimer, but preparations of VEGF165 show some heterogeneity on SDS gels, depending on the secretion of different glycosylation patterns. All dimeric forms have similar biological activities but their bioavailability is very different. There is good evidence that different cells and tissues express different VEGF isoforms. The other members of this increasing growth factor family are VEGF-B, -C, -D and -E. Another member is the Placenta growth factor PlGF
Protein SequenceAPMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLECVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKDRARQENPCGPCSERRKHLFVQDPQTCKCSCKNTDSRCKARQLELNERTCRCDKPRR
Uniprot IDP15692
Protein RefSeqNP_001020537.2
mRNA RefSeqNM_001025366.2

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Reference

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