Recombinant Human Hepatocyte Growth Factor Receptor/HGF R/cMet (C-6His-Avi) Biotinylated
SKU: PKSH033970-100
Recombinant Human Hepatocyte Growth Factor Receptor/HGF R/cMet (C-6His-Avi) Biotinylated
| SKU # | PKSH033970 |
| 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-Thr932 |
| Accession | P08581 |
| Calculated Molecular Weight | 104.4 kDa |
| Observed Molecular Weight | 75-95&40-50 kDa |
| Tag | C-His-Avi |
| 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.