Recombinant Human Hepatocyte Growth Factor Receptor/HGF R/cMet (C-6His-Avi) Biotinylated | PKSH033970

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SKU:
575-PKSH033970
Weight:
1.00 KGS
€720.00
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Description

Recombinant Human Hepatocyte Growth Factor Receptor/HGF R/cMet (C-6His-Avi) Biotinylated | PKSH033970 | Gentaur US, UK & Europe Disrtribition

Synonyms: Hepatocyte growth factor receptor; HGF receptor; HGF/SF receptor; Proto-oncogene c-Met; Scatter factor receptor; SF receptor; Tyrosine-protein kinase Met; MET

Active Protein: N/A

Activity: Biotinylated Recombinant Human Hepatocyte Growth Factor Receptor is produced by our Mammalian expression system and the target gene encoding Glu25-Thr932 is expressed with a 6His, Avi tag at the C-terminus.

Protein Construction: Biotinylated Recombinant Human Hepatocyte Growth Factor Receptor is produced by our Mammalian expression system and the target gene encoding Glu25-Thr932 is expressed with a 6His, Avi tag at the C-terminus.

Fusion Tag: C-6His-Avi

Species: Human

Expressed Host: Human Cells

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 95 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per µg as determined by the LAL method.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 104.4 kDa

Formulation: Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.

Reconstitution: Please refer to the printed manual for detailed information.

Background: Hepatocyte growth factor receptor (HGF R) is a glycosylated receptor tyrosine kinase that plays a central role in epithelial morphogenesis and cancer development. HGF R is synthesized as a single chain precursor which undergoes cotranslational proteolytic cleavage. Mature HGF R is a disulfide-linked dimer composed of a 50 kDa extracellular α chain and a 145 kDa transmembrane β chain. Proteolysis and alternate splicing generate additional forms of human HGF R which either lack of the kinase domain, consist of secreted extracellular domains, or are deficient in proteolytic separation of the α and β chains. The sema domain, which is formed by both α and β chains of HGF R, mediates both ligand binding and receptor dimerization. HGF stimulation induces HGF R downregulation via internalization and proteasomedependent degradation. Paracrine induction of epithelial cell scattering and branching tubulogenesis results from the stimulation of HGF R on undifferentiated epithelium by HGF released from neighboring mesenchymal cells.

Research Area: Signal Transduction, Cancer, epigenetics and nuclear signal,

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