Reactivity | CaSpecies Glossary |
Applications | WB, ELISA(Det) |
Clonality | Polyclonal |
Host | Goat |
Conjugate | Biotin |
Concentration | LYOPH |
Immunogen | Mouse myeloma cell line NS0-derived recombinant canine HGF R Glu25-Leu935 Accession # Q75ZY9 |
Specificity | Detects canine HGF R in ELISAs and Western blots. In sandwich immunoassays, less than 7% cross-reactivity with recombinant mouse HGF R is observed and less than 0.2% cross-reactivity with recombinant human HGF R is observed. |
Source | N/A |
Isotype | IgG |
Clonality | Polyclonal |
Host | Goat |
Gene | MET |
Purity Statement | Antigen Affinity-purified |
Innovator's Reward | Test in a species/application not listed above to receive a full credit towards a future purchase. |
Dilutions |
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Application Notes | ELISA Capture: Canine HGF R/c-MET Antibody (Catalog # AF4140) Standard: Recombinant Canine HGF R/c-MET (Catalog # 4140-ME) |
Readout System |
Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
Preservative | No Preservative |
Concentration | LYOPH |
Reconstitution Instructions | Reconstitute at 0.2 mg/mL in sterile PBS. |
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 posttranslational 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 region, and four Ig-like E-set domains, while the cytoplasmic region includes a tyrosine kinase domain (3). The sema domain, which is formed by both the alpha and beta chains of HGF R, mediates both ligand binding and receptor dimerization (3, 4). Ligand-induced tyrosine phosphorylation in the cytoplasmic region activates the kinase domain and provides docking sites for multiple SH2-containing molecules (5, 6). HGF stimulation induces HGF R downregulation via internalization and proteasome-dependent degradation (7). 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, B2, and B3, and MSP R/Ron (8‑15). Ligation of one complex component triggers activation of the other, followed by cooperative signaling effects (8‑15). Formation of some of these heteromeric complexes is a requirement for epithelial cell morphogenesis and tumor cell invasion (8, 12, 13). HGF released from neighboring mesenchymal cells stimulates HGF R on undifferentiated epithelium and induces epithelial cell scattering and branching tubulogenesis (16). 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, canine HGF R shares 85%‑88% amino acid sequence identity with human, mouse and rat HGF R.
Secondary Antibodies |
Isotype Controls |
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