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H9166

Sigma-Aldrich

Vascular Endothelial Growth Factor 165 human

≥95% (SDS-PAGE), recombinant, expressed in HEK 293 cells, lyophilized powder, suitable for cell culture

Synonym(s):

Endothelial Growth Factor, Vascular Growth Factor

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About This Item

MDL number:
UNSPSC Code:
12352202
NACRES:
NA.77

product name

Vascular Endothelial Growth Factor 165 human, VEGF165, recombinant, expressed in HEK 293 cells, HumanKine®, suitable for cell culture

biological source

human

Quality Level

recombinant

expressed in HEK 293 cells

Assay

≥95% (SDS-PAGE)

form

lyophilized powder

potency

≤5 ng/mL EC50

quality

endotoxin tested

mol wt

dimer 45 kDa (glycosylated)

packaging

pkg of 5x10 μg
pkg of 10 μg

manufacturer/tradename

HumanZyme

storage condition

avoid repeated freeze/thaw cycles

technique(s)

cell culture | mammalian: suitable

impurities

≤1 EU/μg

UniProt accession no.

storage temp.

−20°C

Gene Information

human ... VEGFA(7422)

General description

Vascular endothelial growth factor 121 (VEGF121) belongs to the PDGF(platelet derived growth factor)/VEGF growth factor family. The VEGFA gene is mapped to human chromosome 6p21.1. The encoded protein is a dimeric glycoprotein consisting two monomers antiparallel to each other. There are five types of VEGF ligands identified in mammals, which exists as different splice variants. Vascular endothelial growth factor 165 (VEGF165) belongs to the PDGF(platelet derived growth factor)/VEGF growth factor family and VEGF is secreted by many cell types.HumanKine VEGF165 is expressed in human HEK 293 cells as a glycosylated homodimer with an apparent molecular mass of 45 kDa. Production in human HEK 293 cells offers authentic glycosylation. Glycosylation contributes to stability in cell growth media and other applications.

Biochem/physiol Actions

VEGF (vascular endothelial growth factor) acts as a potent angiogenic factor and mitogen that stimulates proliferation, migration and formation of endothelial cells. VEGF stimulates permeabilization of blood vessels and is present in some tumors of the nervous system. VEGFA is known to interact with VEGFR co-receptors such as heparan sulphate proteoglycans and neuropilins. Mutation in the VEGFA gene results in defective vascular development. VEGF is induced by hypoxia, oncogene mutations, and cytokines such as (interleukin) IL-1, IL-8, TNF-α (tumor necrosis factor α).

Physical form

Lyophilized from a 0.2 μm filtered solution of 1X PBS

Analysis Note

The specific activity was determined by the dose-dependent stimulation of the proliferation of HUVEC cells (human umbilical vein endothelial cells).

Legal Information

HumanKine is a registered trademark of Proteintech Group, Inc. and Humanzyme, Inc

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Genetic variants on chromosome 6p21.1 and 6p22.3
are associated with type 2 diabetes risk: a case?control
study in Han Chinese
Lu F, et al.
Journal of Human Genetics, 57.5 (2012)
Chunming Li et al.
Molecular and cellular biochemistry, 346(1-2), 173-178 (2010-09-30)
Cell adhesion is an important process during morphogenesis, differentiation, and homeostasis in cell biology. The role of vascular endothelial growth factor (VEGF) in cell adhesion of keratinocytes is unclear. In our study, a human keratinocyte cell line, HaCaT cells, which
Satsuki Mochizuki et al.
Biochemical and biophysical research communications, 402(4), 651-657 (2010-10-26)
ADAM28, a member of the ADAM (a disintegrin and metalloproteinase) gene family, is over-expressed by carcinoma cells and the expression correlates with carcinoma cell proliferation and progression in human lung and breast carcinomas. However, information about substrates of ADAM28 is
Predominant role of endothelial nitric oxide synthase in vascular endothelial growth factor-induced angiogenesis and vascular permeability
Fukumura D, et al.
Proceedings of the National Academy of Sciences of the USA, 98.5, 2604-2609 (2001)
VEGF receptor signalling ? in control of vascular function
Olsson AK, et al.
Nature Reviews in Molecular and Cell Biology, 7.5 (2006)

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