货号 | MAB527-SP |
别名 | AUTS9; c-MET; EC 2.7.10; EC 2.7.10.1; hepatocyte growth factor receptor; HGF receptor; HGF/SF receptor; HGFR; Met (c-Met); met proto-oncogene (hepatocyte growth factor receptor); met proto-oncogene tyrosine kinase; MET; oncogene MET; Proto-oncogene c-Met; RCCP2; Scatter factor receptor; SF receptor; Tyrosine-protein kinase Met | 全称 | Hepatocyte Growth Factor Receptor |
反应种属 | Mouse |
应用 | Western Blot |
目标/特异性 | Detects the alpha subunit of mouse HGF R/c‑MET in direct ELISAs and Western blots. |
使用方法 | Western Blot: 1 µg/mL |
来源 | Reconstitute at 0.5 mg/mL in sterile PBS. |
产品组分 |
供应商 | R&D Systems |
Entrez Gene IDs | 4233 (Human); 17295 (Mouse) |
应用文献 | |
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions. Neuritogenic activity of chondroitin/dermatan sulfate hybrid chains of embryonic pig brain and their mimicry from shark liver. Involvement of the pleiotrophin and hepatocyte growth factor signaling pathways. | |
纯化方式 | Protein A or G purified from hybridoma culture supernatant |
免疫原 | S. frugiperda insect ovarian cell line Sf 21-derived recombinant mouse HGF R/c‑MET Glu25-Asn929 Accession # P16056 |
内毒素水平 | <0.10 EU per 1 μg of the antibody by the LAL method. |
生物活性 | Mouse |
标记 | Unconjugated |
溶解方法 | Reconstitute at 0.5 mg/mL in sterile PBS. |
背景 | 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). An alternately spliced form of mouse HGF R lacks a cytoplasmic juxtamembrane region important for regulation of signal transduction (5, 6). The sema domain, which is formed by both the alpha and beta chains of HGF R, mediates both ligand binding and receptor dimerization (3, 7). Ligand-induced tyrosine phosphorylation in the cytoplasmic region activates the kinase domain and provides docking sites for multiple SH2-containing molecules (8, 9). HGF stimulation induces HGF R down‑regulation via internalization and proteasome-dependent degradation (10). In the absence of ligand, HGF R forms noncovalent complexes with a variety of membrane proteins including CD44v6, CD151, EGF R, Fas, integrin alpha 6/ beta 4, plexins B1, 2, 3, and MSP R/Ron (11‑18). Ligation of one complex component triggers activation of the other, followed by cooperative signaling effects (11‑18). Formation of some of these heteromeric complexes is a requirement for epithelial cell morphogenesis and tumor cell invasion (11, 15, 16). 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 (19). 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, mouse HGF R shares 87%, 87%, and 94% amino acid sequence identity with canine, human, and rat HGF R, respectively. |
运输条件 | Blue Ice |
存放说明 | 4℃ |
参考文献 |
|