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Recombinant Human HGFR/c-MET Protein (aa 25-519, His Tag)– MSE Supplies LLC

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Recombinant Human HGFR/c-MET Protein (aa 25-519, His Tag)

SKU: PKSH032537-50

  • $ 26795



Recombinant Human HGFR/c-MET Protein (aa 25-519, His Tag)

 

SKU # PKSH032537
Expression Host HEK293 Cells

 

 

Description

Synonyms HGF receptor, HGF/SF receptor, Hepatocyte growth factor receptor, MET , Proto-oncogene c-Met, SF receptor, Scatter factor receptor, Tyrosine-protein kinase Met
Species Human
Expression Host HEK293 Cells
Sequence Glu25-Gly519
Accession P08581
Calculated Molecular Weight 56.9 kDa
Observed Molecular Weight 32&35-57 kDa
Tag C-His
Bio-activity Not validated for activity
  

 

Properties

Purity > 95 % as determined by reducing SDS-PAGE.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method.
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.
Shipping This product is provided as lyophilized powder which is shipped with ice packs.
Formulation Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.
Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the printed manual.
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.