Product Name
Vascular Endothelial Growth Factor (rmVEGF), Recombinant Protein
Popular Item
Full Product Name
Recombinant Mouse Vascular Endothelial Growth Factor
Product Synonym Names
VEGF Mouse; Vascular Endothelial Growth Factor Mouse Recombinant; Vascular endothelial growth factor A; VEGF-A; Vascular permeability factor; VPF; VEGF; MGC70609
Product Gene Name
rmVEGF recombinant protein
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Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
Sequence
MAPTTEGEQK SHEVIKFMDV YQRSYCRPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCAGC CNDEALECVP TSESNITMQI MRIKPHQSQH IGEMSFLQHS RCECRPKKDR TKPEKHCEPC SERRKHLFVQ DPQTCKCSCK NTDSRCKARQ LELNERTCRC DKPRR
3D Structure
ModBase 3D Structure for Q00731
Purity/Purification
Greater than 95.0% as determined by: (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.
Form/Format
The protein was lyophilized from a concentrated (1mg/ml) solution with no additives.
Sterile Filtered White lyophilized (freeze-dried) powder.
Solubility
It is recommended to reconstitute the lyophilized Vascular Endothelial Growth Factor in sterile 18M Omega -cm H2O not less than 100 ug/ml, which can then be further diluted to other aqueous solutions.
Biological Activity
The
biological activity is determined by the dose-dependent stimulation of the proliferation of human umbilical vein endothelial cells (HUVEC) using a concentration range of 1.0-5.0 ng/ml corresponding to a specific activity of 0.2-1,000,000IU/mg.
Preparation and Storage
Lyophilized Vascular Endothelial Growth Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18 degree C. Upon reconstitution VEGF should be stored at 4 degree C between 2-7 days and for future use below -18 degree C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Other Notes
Small volumes of rmVEGF recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
Related Product Information for
rmVEGF recombinant protein
Description: Vascular Endothelial Growth Factor Mouse Recombinant produced in E Coli is a double, non-glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 39035 Dalton.The VEGF is purified by proprietary chromatographic techniques.
Introduction: Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/ macrophagemigration, neurons, cancer cells, kidney epithelial cells). VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.Elevated levels of this protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.
Product Categories/Family for rmVEGF recombinant protein
CYTOKINES AND GROWTH FACTORS; Growth Factors; VEGF
NCBI/Uniprot data below describe general gene information for rmVEGF. It may not necessarily be applicable to this product.
NCBI Accession #
NP_001020421.2
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NCBI GenBank Nucleotide #
NM_001025250.3
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UniProt Primary Accession #
Q00731
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UniProt Secondary Accession #
O70123; Q66S31; Q6GT23; Q6WZL9[Other Products]
UniProt Related Accession #
Q00731[Other Products]
Molecular Weight
40,288 Da
NCBI Official Full Name
vascular endothelial growth factor A isoform 1
NCBI Official Synonym Full Names
vascular endothelial growth factor A
NCBI Official Symbol
Vegfa [Similar Products]
NCBI Official Synonym Symbols
Vpf; Vegf
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NCBI Protein Information
vascular endothelial growth factor A; vascular permeability factor
UniProt Protein Name
Vascular endothelial growth factor A
UniProt Synonym Protein Names
Vascular permeability factor; VPF
Protein Family
Vascular endothelial growth factor
UniProt Gene Name
Vegfa [Similar Products]
UniProt Synonym Gene Names
Vegf; VEGF-A; VPF [Similar Products]
UniProt Entry Name
VEGFA_MOUSE
NCBI Summary for rmVEGF
This gene product is a member of the PDGF/VEGF growth factor family. It is a mitogen that specifically acts on endothelial cells and has various effects, including mediating increased vascular permeability, inducing angiogenesis, vasculogenesis, endothelial cell growth, promoting cell migration, and inhibiting apoptosis. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. Also, alternative translation initiation from non-AUG (CUG) and AUG start sites in some transcript variants, give rise to additional isoforms. The expression of some isoforms derived from AUG start codon is affected by a small upstream open reading frame, which is located within an internal ribosome entry site. [provided by RefSeq, Nov 2013]
UniProt Comments for rmVEGF
VEGF: Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. Binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. NRP1/Neuropilin-1 binds isoforms VEGF-165 and VEGF-145. Isoform VEGF165B binds to KDR but does not activate downstream signaling pathways, does not activate angiogenesis and inhibits tumor growth. Defects in VEGFA are a cause of susceptibility to microvascular complications of diabetes type 1 (MVCD1). These are pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic *****s. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. Belongs to the PDGF/VEGF growth factor family. 13 isoforms of the human protein are produced by alternative promoter.
Protein type: Secreted, signal peptide; Secreted; Motility/polarity/chemotaxis; Cytokine
Cellular Component: extracellular space; cell surface; membrane; cytoplasm; plasma membrane; extracellular region; basement membrane; secretory granule
Molecular Function: heparin binding; identical protein binding; protein homodimerization activity; growth factor activity; extracellular matrix binding; platelet-derived growth factor receptor binding; cytokine activity; vascular endothelial growth factor receptor 1 binding; vascular endothelial growth factor receptor binding; receptor agonist activity; protein binding; vascular endothelial growth factor receptor 2 binding; protein heterodimerization activity; fibronectin binding; receptor binding; chemoattractant activity
Biological Process: heart morphogenesis; macrophage differentiation; positive regulation of cell adhesion; positive regulation of positive chemotaxis; multicellular organismal development; cell maturation; positive regulation of receptor internalization; basophil chemotaxis; regulation of cell shape; positive regulation of MAP kinase activity; positive chemotaxis; positive regulation of mesenchymal cell proliferation; mesoderm development; negative regulation of neuron apoptosis; kidney development; positive regulation of neuroblast proliferation; nervous system development; T-helper 1 type immune response; monocyte differentiation; positive regulation of signal transduction; mRNA stabilization; positive regulation of blood vessel endothelial cell migration; activation of CREB transcription factor; positive regulation of protein amino acid autophosphorylation; regulation of endothelial cell differentiation; positive regulation of vascular permeability; regulation of transcription from RNA polymerase II promoter; patterning of blood vessels; positive regulation of angiogenesis; positive regulation of peptidyl-tyrosine phosphorylation; eye photoreceptor cell development; camera-type eye morphogenesis; cell migration during sprouting angiogenesis; branching morphogenesis of a tube; cardiac muscle fiber development; positive regulation of cell division; positive regulation of axon extension involved in axon guidance; activation of protein kinase activity; endothelial cell migration; neuron development; blood vessel morphogenesis; positive regulation of transcription from RNA polymerase II promoter; positive regulation of endothelial cell proliferation; regulation of cGMP metabolic process; alveolus development; surfactant homeostasis; positive regulation of epithelial cell proliferation; negative regulation of apoptosis; lactation; post-embryonic camera-type eye development; positive regulation of smooth muscle cell proliferation; negative regulation of caspase activity; negative regulation of transcription from RNA polymerase II promoter; positive regulation of vascular endothelial growth factor receptor signaling pathway; induction of positive chemotaxis; positive regulation of focal adhesion formation; ovarian follicle development; vasculature development; epithelial cell differentiation; positive regulation of cell proliferation; lymphangiogenesis; negative regulation of programmed cell death; angiogenesis; cell differentiation; negative regulation of bone resorption; blood vessel development; cell migration; in utero embryonic development; lumen formation; positive regulation of cell motility; positive regulation of peptidyl-serine phosphorylation; positive regulation of protein kinase B signaling cascade; cell proliferation; positive regulation of protein complex assembly; response to hypoxia; artery morphogenesis; blood vessel remodeling; negative regulation of cell-cell adhesion; sprouting angiogenesis; positive regulation of protein amino acid phosphorylation; vascular endothelial growth factor receptor signaling pathway; growth; positive regulation of cell migration; lung development
Research Articles on rmVEGF
1. the brain VGEF-A and cerebral MVD were increased in AD mice, possibly representing an adaptive response to cerebrovascular impairment.
Precautions
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