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.
Pack Size | Availability | Price/USD | Quantity |
---|---|---|---|
20 μg | 5 days | $ 355.00 | |
100 μg | 5 days | $ 963.00 |
Description | 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. |
Species | Human |
Expression System | Human Cells |
Tag | C-6His-Avi |
Accession Number | P08581 |
Synonyms | SF receptor, HGF receptor, Scatter factor receptor, Tyrosine-protein kinase Met, Hepatocyte growth factor receptor, HGF/SF receptor, MET, Proto-oncogene c-Met |
Amino Acid | Glu25-Thr932 |
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. |
Protein Purity | Greater than 95% as determined by reducing SDS-PAGE. (QC verified) |
Molecular Weight | 75-95&40-50 KDa, reducing conditions |
Endotoxin | Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test. |
Formulation | Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4. |
Reconstitution | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
Stability & Storage |
Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
Shipping |
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below. |
Research 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. |
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HGFR/c-Met Protein, Human, Recombinant (aa 25-932, His & Avi), Biotinylated SF receptor HGF receptor Scatter factor receptor Tyrosine-protein kinase Met Hepatocyte growth factor receptor HGF/SF receptor MET Proto-oncogene c-Met recombinant recombinant-proteins proteins protein