Human Hepatocyte Growth Factor alpha chain Recombinant
Catalog #
90157-B
$205
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Description
Recombinant HGF alpha is a non-glycosylated disulfide-linked protein consisting of the alpha chain (463) amino acid residues, and migrates as an approximately 54 kDa protein under non-reducing and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding Human Hepatocyte Growth Factor alpha chain was expressed in E. coli.
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Synonyms
HGFA, Human Hepatocyte Growth Factor alpha chain, Hepapoietin A, Scatter Factor, HPTA
Product Info
Storage and Usage
Citations
Species
Human
Host Species/Expression System
E. coli
Purity
≥97% by SDS-PAGE and HPLC
Format
lyophilized protein
Formulation
Lyophilized from 0.2 µm filtered solution in Tris, pH 8.0.
MW
54 kDa
Endotoxin Level
<0.1 ng/µg (1 EU/µg), using the LAL gel clot method.
Amino Acids
32–494
Genbank #
P14210
UniProt #
P14210
Background
Hepatocyte growth factor (HGF) is a multifunctional cytokine that was originally described as a mesenchymal- derived factor that regulates cell growth, cell motility, morphogenesis and angiogenesis through activation of its receptor, the transmembrane tyrosine kinase encoded by the c-Met proto-oncogene. HGF and c- Met are often co-expressed or over-expressed in a variety of human malignancies including glioblastoma and medullablastoma. The multifunctional effects of HGF:c-Met signaling in tumor cells are mediated by a network of signal transduction pathways including mitogen-activated protein kinase (MAPK) and phosphoinositide 3-kinase (PI3K). HGF consists of two subunits held by a disulfide bond. The alpha subunit (69 kDa) has a length of 440 amino acids. The beta subunit (34 kDa) has a length of 234 amino acids. The beta chain of the factor shows approximately 38% homology at the protein level to the serine protease domain of plasminogen. A variant of the beta chain has been shown to function as a subunit of a hybrid cytokine known as PPBSF [pre-pro-B- cell growth stimulating factor]. HGF is a glycoprotein, the non-glycosylated factor is also bioactive.
References
1. J. Biol. Chem., 2009 , 284, 28510-28521.
2. Am J Physiol Cell Physiol, Aug 2009, 297: C238 - C252.
3. Clin. Cancer Res., Jun 2009, 15: 3740 - 3750.
2. Am J Physiol Cell Physiol, Aug 2009, 297: C238 - C252.
3. Clin. Cancer Res., Jun 2009, 15: 3740 - 3750.