HGFR/c-MET Antibody (95106) [Unconjugated] Summary
Immunogen |
Mouse myeloma cell line NS0-derived recombinant human HGF R/c-MET Glu25-Thr932 Accession # P08581 |
Specificity |
Detects human HGF R/c-MET. |
Source |
N/A |
Isotype |
IgG1 |
Clonality |
Monoclonal |
Host |
Mouse |
Gene |
MET |
Purity Statement |
Protein A or G purified from hybridoma culture supernatant |
Innovator's Reward |
Test in a species/application not listed above to receive a full credit towards a future purchase. |
Applications/Dilutions
Dilutions |
- CyTOF-ready
- Flow Cytometry 2.5 ug/10^6 cells
|
Publications |
Read Publications using MAB3582 in the following applications:
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Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 6 months, -20 to -70 degreesC under sterile conditions after reconstitution. |
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS. |
Preservative |
No Preservative |
Concentration |
LYOPH |
Reconstitution Instructions |
Reconstitute at 0.5 mg/mL in sterile PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for HGFR/c-MET Antibody (95106) [Unconjugated]
Background
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.
- Birchmeier, C. et al. (2003) Nat. Rev. Mol. Cell Biol. 4:915.
- Corso, S. et al. (2005) Trends Mol. Med. 11:284.
- Gherardi, E. et al. (2003) Proc. Natl. Acad. Sci. USA 100:12039.
- Park, M. et al. (1987) Proc. Natl. Acad. Sci. USA 84:6379.
- Crepaldi, T. et al. (1994) J. Biol. Chem. 269:1750.
- Prat, M. et al. (1991) Mol. Cell. Biol. 12:5954.
- Rodrigues, G.A. et al. (1991) Mol. Cell. Biol. 11:2962.
- Kong-Beltran, M. et al. (2004) Cancer Cell 6:75.
- Naldini, L. et al. (1991) Mol. Cell. Biol. 11:1793.
- Ponzetto, C. et al. (1994) Cell 77:261.
- Jeffers, M. et al. (1997) Mol. Cell. Biol. 17:799.
- Orian-Rousseau, V. et al. (2002) Genes Dev. 16:3074.
- Klosek, S.K. et al. (2005) Biochem. Biophys. Res. Commun. 336:408.
- Jo, M. et al. (2000) J. Biol. Chem. 275:8806.
- Wang, X. et al. (2002) Mol. Cell 9:411.
- Trusolino, L. et al. (2001) Cell 107:643.
- Giordano, S. et al. (2002) Nat. Cell Biol. 4:720.
- Conrotto, P. et al. (2004) Oncogene 23:5131.
- Follenzi, A. et al. (2000) Oncogene 19:3041.
- Sonnenberg, E. et al. (1993) J. Cell Biol. 123:223.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are
guaranteed for 1 year from date of receipt.
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Product General Protocols
Find general support by application which include: protocols, troubleshooting, illustrated assays, videos and webinars.
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