抗HGF Receptor/c-MET抗体(Anti-HGF Receptor/c-MET, Mouse-Mono, PE antibody)

• 価格
• Product Details
• Applications and Data
• Related Product & Information
• Citations

価格

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Product Details

Species Reactivity	Human
Label	Phycoerythrin
Immunogen	Mouse myeloma cell line NS0-derived recombinant human HGF R/c-METGlu25-Thr932Accession # P08581
Source	Monoclonal Mouse IgG1 Clone # 95106
Purification	Protein A or G purified from hybridoma culture supernatant
Specificity	Detects human HGF R/c-MET.

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Applications and Data

	Recommended Concentration	Sample
Flow Cytometry	10 µL/106 cells	See below

Flow Cytometry
	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 Mouse Anti-Human HGF R/c‑MET PE‑conjugated Monoclonal Antibody (Catalog # FAB3582P, filled histogram) or isotype control antibody (Catalog # IC002P, open histogram). View our protocol for Staining Membrane-associated Proteins.

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Related Product & Information

Background

HGF R/c-MET

background_content

Background: HGF R/c-MET 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 of 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 non-covalent 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 (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, over-expression, 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% amino acid sequence identity with canine, mouse, and rat HGF R.

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Citations

1. An essential receptor for adeno-associated virus infection.
   Authors: Pillay S, Meyer N, Puschnik A, Davulcu O, Diep J, Ishikawa Y, Jae L, Wosen J, Nagamine C, Chapman M, Carette J
   Nature, 2016;530(7588):108-12.
   Species: Human
   Sample Type: Whole Cells
   Application: Flow


2. Deregulated hepsin protease activity confers oncogenicity by concomitantly augmenting HGF/MET signalling and disrupting epithelial cohesion.
   Authors: Tervonen T, Belitskin D, Pant S, Englund J, Marques E, Ala-Hongisto H, Nevalaita L, Sihto H, Heikkila P, Leidenius M, Hewitson K, Ramachandra M, Moilanen A, Joensuu H, Kovanen P, Poso A, Klefstrom J
   Oncogene, 2015;0(0):ePub.
   Species: Human
   Sample Type: Whole Cells
   Application: Flow


3. Impact of Cell-surface Antigen Expression on Target Engagement and Function of an Epidermal Growth Factor Receptor x c-MET Bispecific Antibody.
   Authors: Jarantow S, Bushey B, Pardinas J, Boakye K, Lacy E, Sanders R, Sepulveda M, Moores S, Chiu M
   J Biol Chem, 2015;290(41):24689-704.
   Species: Human
   Sample Type: Whole Cells
   Application: Flow


4. Three-dimensional lung tumor microenvironment modulates therapeutic compound responsiveness in vitro--implication for drug development.
   Authors: Ekert, Jason E, Johnson, Kjell, Strake, Brandy, Pardinas, Jose, Jarantow, Stephen, Perkinson, Robert, Colter, David C
   PLoS ONE, 2014;9(3):e92248.
   Species: Human
   Sample Type: Whole Cells
   Application: Flow


5. Phenotyping of human melanoma cells reveals a unique composition of receptor targets and a subpopulation co-expressing ErbB4, EPO-R and NGF-R.
   Authors: Mirkina I, Hadzijusufovic E, Krepler C, Mikula M, Mechtcheriakova D, Strommer S, Stella A, Jensen-Jarolim E, Holler C, Wacheck V, Pehamberger H, Valent P
   PLoS ONE, 2014;9(1):e84417.
   Species: Human
   Sample Type: Whole Cells
   Application: Flow

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