VEGF active protein

Recombinant Mouse VEGF (120aa)

Cat. Num. AAA4159970

• Gene Names: Vegfa; Vpf; Vegf
• Purity: >95% as determined by SDS-PAGE
• Synonyms: VEGF; Recombinant Mouse VEGF (120aa); Vascular endothelial growth factor A; VEGF-A; Vascular permeability factor; VPFVascular Endothelial Growth Factor 120AA (VEGFA); VEGF active protein

• Host: E Coli
• Purity/Purification: >95% as determined by SDS-PAGE
• Form/Format: Lyophilized from a 0.2 um filtered solution in 2.5% glycine, 0.5% sucrose, 0.01% Tween80, 5.0 mM glutamic acid, pH 4.5.
• Sequence Length: 392

• Bioactivity: The ED(50) was determined by the dose-dependent proliferation of human umbilical vein endothelial cells and was found to be <0.05ng/mL.
• Endotoxin Level: <1.0 EU/ug of recombinant protein as determined by the LAL method.
• Reconstitution: A quick spin of the vial followed by reconstitution in distilled water to a concentration not less than 0.1 mg/mL. This solution can then be diluted into other buffers.
• Preparation and Storage: The lyophilized protein is stable for at least one year from date of receipt at-70 degree C. Upon reconstitution, this cytokine can be stored in working aliquots at 2-8 degree C for one month, or at-20 degree C for six months, with a carrier protein without detectable loss of activity. Avoid repeated freeze/thaw cycles.

Testing Data

Related Product Information for VEGF active protein

VEGF is a homodimeric heavily glycosylated protein. The human factor occurs in several molecular variants of 120, 162, 145, 148, 164, 183, 189, 206 amino acids, arising by alternative splicing of the mRNA. The splice forms of VEGF differ in biological properties such as the receptor types, which they recognize and their interaction with heparan sulfate proteoglycans. The 165 amino acid form of the factor is the most common form in most tissues. Kaposi sarcomas express VEGF121 and VEGF165. VEGF121 and VEGF165 are soluble secreted forms of the factor while VEGF189 and VEGF206 are mostly bound to heparin-containing proteoglycans in the cell surface or in the basement membrane. A high-affinity glycoprotein receptor of 170-235 kDa is expressed on vascular endothelial cells. The interaction of VEGF with heparin-like molecules of the extracellular matrix is required for efficient receptor binding. Protamine sulfate and suramin are capable of replacing the receptor-bound factor. The high-affinity receptor for VEGF, now known as VEGFR1, has been identified as the gene product of the FLT-1. Another receptor for VEGF, now known as VEGFR2, is KDR, also known as FLK-1. A factor that competes with the 165 amino acid form of VEGF for receptor binding is PLGF. A third receptor type, VEGFR3 is known also as FLT-4. An isoform-specific receptor for VEGF165 has been identified as human Neuropilin-1.

NCBI and Uniprot Product Information

• NCBI GI #: 160358799
• NCBI GeneID: 22339
• NCBI Accession #: NP_001020421.2
• NCBI GenBank Nucleotide #: NP_001020421.2
• UniProt Accession #: Q00731
• Molecular Weight: 28.0 kDa
• 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
• NCBI Official Synonym Symbols: Vpf; Vegf
• NCBI Protein Information: vascular endothelial growth factor A
• UniProt Protein Name: Vascular endothelial growth factor A
• Protein Family: VEGF coregulated chemokine
• UniProt Gene Name: Vegfa
• UniProt Synonym Gene Names: Vegf; VEGF-A; VPF
• UniProt Entry Name: VEGFA_MOUSE

NCBI Description

This gene is a member of the PDGF/VEGF growth factor family. It encodes a heparin-binding protein, which exists as a disulfide-linked homodimer. This growth factor induces proliferation and migration of vascular endothelial cells, and is essential for both physiological and pathological angiogenesis. Disruption of this gene in mice resulted in abnormal embryonic blood vessel formation. This gene is upregulated in many known tumors and its expression is correlated with tumor stage and progression. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. There is also evidence for alternative translation initiation from upstream non-AUG (CUG) codons resulting in additional isoforms. A recent study showed that a C-terminally extended isoform is produced by use of an alternative in-frame translation termination codon via a stop codon readthrough mechanism, and that this isoform is antiangiogenic. Expression of some isoforms derived from the AUG start codon is regulated by a small upstream open reading frame, which is located within an internal ribosome entry site.[provided by RefSeq, Nov 2015]

Uniprot Description

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 adults. 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: Motility/polarity/chemotaxis; Cytokine; Secreted; Secreted, signal peptide

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; cytokine activity; platelet-derived growth factor receptor binding; 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; positive regulation of cell adhesion; macrophage differentiation; 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; positive regulation of signal transduction; monocyte differentiation; mRNA stabilization; positive regulation of blood vessel endothelial cell migration; activation of CREB transcription factor; positive regulation of protein amino acid autophosphorylation; positive regulation of vascular permeability; regulation of endothelial cell differentiation; patterning of blood vessels; regulation of transcription from RNA polymerase II promoter; eye photoreceptor cell development; positive regulation of angiogenesis; positive regulation of peptidyl-tyrosine phosphorylation; camera-type eye morphogenesis; branching morphogenesis of a tube; cell migration during sprouting angiogenesis; cardiac muscle fiber development; positive regulation of cell division; positive regulation of axon extension involved in axon guidance; activation of protein kinase activity; blood vessel morphogenesis; endothelial cell migration; neuron development; positive regulation of transcription from RNA polymerase II promoter; positive regulation of endothelial cell proliferation; regulation of cGMP metabolic process; surfactant homeostasis; alveolus development; 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; epithelial cell differentiation; ovarian follicle development; vasculature development; lymphangiogenesis; positive regulation of cell proliferation; 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; positive regulation of protein amino acid phosphorylation; sprouting angiogenesis; vascular endothelial growth factor receptor signaling pathway; lung development; growth; positive regulation of cell migration