protein

Human VEGF145

MBS691674

0.02 mg

350 USD

Recombinant Protein

Human VEGF145

[VEGF145]

[VEGF-A, VPF]

[vascular endothelial growth factor A isoform a; Vascular endothelial growth factor A; vascular endothelial growth factor A; vascular permeability factor; vascular endothelial growth factor A; Vascular permeability factor]

[VEGF145]

[VEGFA; VEGFA; VPF; VEGF; MVCD1; VEGF; VEGF-A; VPF]

VEGFA_HUMAN

E.coli

APMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEY
PDEIEYIFKPSCVPLMRCGGCCNDEGLECVPTEESNITM
QIMRIKPHQGQHIGEMSFLQHNKCECRPKKDRARQEKKS
VRGKGKGQKRRKKSRYKSWSVCDKPRR

> 95% by SDS-PAGE & silver stain

Lyophilized; 50 mM acetic acid

Lyophilized samples are stable for greater than six months at -20°C to -70°C. Reconstituted VEGF 145 should be stored in working aliquots at -20°C.

SDS-PAGE

Testing Data

Endotoxin level: 145 . Stabilizer: None. Length (aa): 145. Result by N-terminal sequencing: APMAEGG. Reconstitution: The lyophilized VEGF 145 should be reconstituted in water to a concentration not lower than 50 ug/ml. For long term storage we recommend to add at least 0.1% human or bovine serum albumin. Biological Activity: The ED 50 for stimulation of cell proliferation in human umbilical vein endothelial cells by VEGF 145 has been determined to be in the range of 5-10 ng/ml.

Cytokines & Growth Factors

A vascular endothelial growth factor (VEGF) mRNA species containing exons 1–6 and 8 of the VEGF gene was found to be expressed as a major VEGF mRNA form in several cell lines derived from carcinomas of the female reproductive system. This mRNA is predicted to encode a VEGF form of 145 amino acids (VEGF145). VEGF145 produced in insect cells is a homodimeric, 20,5 kDa protein belonging to the VEGF-A family. Recombinant VEGF145 induced the proliferation of vascular endothelial cells and promoted angiogenesis in vivo. VEGF145 was compared with previously characterized VEGF species with respect to interaction with Heparin-like molecules, cellular distribution, VEGF receptor recognition, and extracellular matrix (ECM) binding ability. VEGF145 shares with VEGF165 the ability to bind to the KDR/flk-1 receptor of endothelial cells. It also binds to heparin with an affinity similar to that of VEGF165. However, VEGF145 does not bind to two additional endothelial cell surface receptors that are recognized by VEGF165 but not by VEGF121. VEGF145 is secreted from producing cells as are VEGF121 and VEGF165. However, VEGF121 and VEGF165 do not bind to the ECM produced by corneal endothelial cells, whereas VEGF145 binds efficiently to this ECM. Basic fibroblast growth factor (bFGF)-depleted ECM containing bound VEGF145 induces proliferation of endothelial cells, indicating that the bound VEGF145 is active. It seems that VEGF145 possesses a unique combination of biological properties distinct from those of previously characterized VEGF species. The other members of this increasing growth factor family are VEGF-B, -C, -D, -E and -F. Another member is the Placenta growth factor PlGF (PlGF-1, -2 and -3).

1. Breier et al., Dev 114:521, 1992 2. Fiebig et al., Eur J Biochem 211:19, 1993 3. Flamme et al., Dev Biol 162:699, 1995 4. Kremer at al., Cancer Res 57:3852, 1997 5. Poltorak et al., JBC 272:7151, 1997

76781480

NP_001191313.1

NM_001171624

P15692-6

34 kDa

Angiogenesis Pathway (198772); Bladder Cancer Pathway (83115); Bladder Cancer Pathway (527); Cellular Response To Hypoxia Pathway (645259); Cellular Responses To Stress Pathway (645258); Cytokine-cytokine Receptor Interaction Pathway (83051); Cytokine-cytokine Receptor Interaction Pathway (460); Endochondral Ossification Pathway (198812); Focal Adhesion Pathway (83067); Focal Adhesion Pathway (478)

This gene is a member of the PDGF/VEGF growth factor family and encodes a protein that is often found as a disulfide linked homodimer. This protein is a glycosylated mitogen that specifically acts on endothelial cells and has various effects, including mediating increased vascular permeability, inducing angiogenesis, vasculogenesis and endothelial cell growth, promoting cell migration, and inhibiting apoptosis. Elevated levels of this protein is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy. Alternatively spliced transcript variants, encoding either freely secreted or cell-associated isoforms, have been characterized. There is also evidence for the use of non-AUG (CUG) translation initiation sites upstream of, and in-frame with the first AUG, leading to additional isoforms. [provided by RefSeq, Jul 2008]

Function: 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. Ref.27 Ref.30 Ref.33. Subunit structure: Homodimer; disulfide-linked. Also found as heterodimer with PGF . By similarity. Subcellular location: Secreted. Note: VEGF121 is acidic and freely secreted. VEGF165 is more basic, has heparin-binding properties and, although a signicant proportion remains cell-associated, most is freely secreted. VEGF189 is very basic, it is cell-associated after secretion and is bound avidly by heparin and the extracellular matrix, although it may be released as a soluble form by heparin, heparinase or plasmin. Ref.26 Ref.28 Ref.32. Tissue specificity: Isoform VEGF189, isoform VEGF165 and isoform VEGF121 are widely expressed. Isoform VEGF206 and isoform VEGF145 are not widely expressed. Induction: Regulated by growth factors, cytokines, gonadotropins, nitric oxide, hypoxia, hypoglycemia and oncogenic mutations. Involvement in disease: Microvascular complications of diabetes 1 (MVCD1) [MIM:603933]: 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.Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Sequence similarities: Belongs to the PDGF/VEGF growth factor family. Sequence caution: The sequence AAC63102.1 differs from that shown. Reason: Erroneous initiation. The sequence AAC63143.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.The sequence CAC19512.2 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.The sequence CAC19516.2 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.

0.02 mg

350 USD