Mouse HGFR/c-MET Antibody

Catalog #: MAB527
1 Citation Datasheet / COA / SDS

Catalog #	Availability	Size / Price	Qty
MAB527
MAB527-SP

All HGFR/c-MET Antibodies

Product Details

Citations (1)

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Summary Preparation and Storage Reconstitution Calculator Background Product Datasheets Related Research Areas

Mouse HGFR/c-MET Antibody Summary

Species Reactivity

Mouse

Specificity

Detects the alpha subunit of mouse HGF R/c‑MET in direct ELISAs and Western blots.

Source

Monoclonal Rat IgG_2A Clone # 118624

Purification

Protein A or G purified from hybridoma culture supernatant

Immunogen

S. frugiperda insect ovarian cell line Sf 21-derived recombinant mouse HGF R/c‑MET
Glu25-Asn929
Accession # P16056

Formulation

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.

Label

Unconjugated

Applications

Recommended Concentration

Sample

Western Blot

1 µg/mL

Recombinant Mouse HGF R/c-MET Fc Chimera (Catalog # 527-ME)

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Reconstitution Calculator

Preparation and Storage

Reconstitution

Reconstitute at 0.5 mg/mL in sterile PBS.

Shipping

Lyophilized product is shipped at ambient temperature. Liquid small pack size (-SP) is shipped with polar packs. Upon receipt, store immediately at the temperature recommended below.

Stability & Storage

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.

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.

Background: HGFR/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). 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.

References

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. 100:12039.
Chan, A.M. et al. (1988) Oncogene 2:593.
Lee, C-C. and K.M. Yamada (1994) J. Biol. Chem. 269:19457.
Lee, C-C., et al. (1995) J. Biol. Chem. 270:507.
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.

Long Name

Hepatocyte Growth Factor Receptor

Entrez Gene IDs

4233 (Human); 17295 (Mouse)

Alternate Names

AUTS9; cMET; c-MET; EC 2.7.10; EC 2.7.10.1; hepatocyte growth factor receptor; HGF R; 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

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Citation for Mouse HGFR/c-MET Antibody

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.

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