Key Product Details
Product Summary for Human HGFR/c‑MET Biotinylated Antibody
Accession # P08581
Scientific Data Images for Human HGFR/c‑MET Biotinylated Antibody
Detection of HGF R/c‑MET in MDA‑MB‑231 Human Cell Line by Flow Cytometry.MDA-MB-231 human breast cancer cell line was stained with Human HGF R/c-MET Biotinylated Antigen Affinity-purified Polyclonal Antibody (Catalog # BAF358, filled histogram) or control antibody (Catalog # BAF108, open histogram), followed by Streptavidin-Allophycocyanin (Catalog # F0050).
Applications for Human HGFR/c‑MET Biotinylated Antibody
Sample: MDA‑MB‑231 human breast cancer cell line
Sample: Recombinant Human HGF R/c-MET Fc Chimera (Catalog # 358-MT)
Human HGF R/c-MET Sandwich Immunoassay
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Formulation, Preparation and Storage
Stability & Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
HGF R, also known as Met (from N-methyl-N’-nitro-N-nitrosoguanidine induced), 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. This generates a mature HGF R that is a disulfide-linked dimer composed of a 50 kDa extracellular alpha chain and a 145 kDa transmembrane beta chain (1, 2). The extracellular domain (ECD) contains a seven bladed beta-propeller sema domain, a cysteine-rich PSI/MRS, and four Ig-like E-set domains, while the cytoplasmic region includes the tyrosine kinase domain (3, 4). Proteolysis and alternate splicing generate additional forms of human HGF R which either lack the kinase domain, consist of secreted extracellular domains, or are deficient in proteolytic separation of the alpha and beta chains (5-7). The sema domain, which is formed by both the alpha and beta chains of HGF R, mediates both ligand binding and receptor dimerization (3, 8). Ligand-induced tyrosine phosphorylation in the cytoplasmic region activates the kinase domain and provides docking sites for multiple SH2-containing molecules (9, 10). HGF stimulation induces HGF R downregulation via internalization and proteasome-dependent degradation (11). In the absence of ligand, HGF R forms noncovalent complexes with a variety of membrane proteins including CD44v6, CD151, EGF R, Fas, Integrin alpha6/ beta4, Plexins B1, 2, 3, and MSP R/Ron (12-19). Ligation of one complex component triggers activation of the other, followed by cooperative signaling effects (12-19). Formation of some of these heteromeric complexes is a requirement for epithelial cell morphogenesis and tumor cell invasion (12, 16, 17). 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 (20). Genetic polymorphisms, chromosomal translocation, overexpression, and additional splicing and proteolytic cleavage of HGF R have been described in a wide range of cancers (1). Within the ECD, human HGF R shares 86-88% aa sequence identity with canine, mouse, and rat HGF R.
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Product Specific Notices for Human HGFR/c‑MET Biotinylated Antibody
For research use only