rhHGFR is fused with a polyhistidine tag at the C-terminal. The mature form of HGFR is a disulfide-linked heterodimer composed of proteolytically cleaved α and β chain. Each α and β chain has a calculated MW of 32.5 kDa (α chain) and 60 kDa (β chain). The predicted N-terminal is Glu25 (α chain) & Ser308 (β chain). Protein migrates as 45 kDa (α chain) and 85-90 kDa (β chain) in reduced SDS-PAGE resulting from glycosylation.
MET
Spezies: Human
Wirt: Mammalian Cells
Recombinant
The purity of the protein is greater than 85 % as determined by SDS-PAGE and Coomassie blue staining.
MET
Spezies: Human
Wirt: Baculovirus infected Insect Cells
Recombinant
> 90 % as determined by reducing SDS-PAGE.
Active
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Lyophilized
Buffer
PBS, pH 7.4
Handhabung
Please avoid repeated freeze-thaw cycles.
Lagerung
-20 °C
Informationen zur Lagerung
No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C-8 °C), After reconstitution under sterile conditions for 1 month (4 °C-8 °C) or 3 months (-20 °C to -70 °C).
Hepatocyte growth factor receptor (HGFR) is also known as mesenchymal-epithelial transition factor (MET), c-Met, and is a glycosylated receptor tyrosine kinase that plays a central role in epithelial morphogenesis and cancer development. HGFR protein possesses tyrosine-kinase activity. The primary single chain precursor protein is post-translationally cleaved to produce the alpha and beta subunits, which are disulfide linked to form the mature receptor. HGFR is normally expressed by cells of epithelial origin, while expression of HGF is restricted to cells of mesenchymal origin. Upon HGF stimulation, HGFR induces several biological responses that collectively give rise to a program known as invasive growth. Abnormal HGFR activation in cancer correlates with poor prognosis, where aberrantly active HGFR triggers tumor growth, formation of new blood vessels (angiogenesis) that supply the tumor with nutrients, and cancer spread to other organs (metastasis). HGFR is deregulated in many types of human malignancies, including cancers of kidney, liver, stomach, breast, and brain. Normally, only stem cells and progenitor cells express HGFR, However, cancer stem cells are thought to hijack the ability of normal stem cells to express HGFR, and thus become the cause of cancer persistence and spread to other sites in the body. Various mutations in the HGFR gene are associated with papillary renal carcinoma. HGFR mediates a complex program known as invasive growth. Activation of HGFR triggers mitogenesis, and morphogenesis.