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ADAM 12, Mouse anti-Human, Clone: 8F8, Millipore Sigma™
Mouse Monoclonal Antibody
Supplier: MilliporeSigma MABT1330100UG
Description
Anti-ADAM 12, clone 8F8, Cat. No. MABT1330, is a mouse monoclonal antibody that detects Disintegrin and metalloproteinase domain-containing protein 12 (ADAM12) and has been tested for use in Flow Cytometry, Immunocytochemistry, Immunoprecipitation, Inhibition Assays, and Western Blotting.
Disintegrin and metalloproteinase domain-containing protein 12 (UniProt: O43184, also known as ADAM 12, Meltrin-alpha) is encoded by the ADAM12 (also known as MLTN, UNQ346/PRO545) gene (Gene ID: 8038) in human. ADAM (A disintegrin and metalloprotease) family consists of multidomain cell-surface proteins that are synthesized in their proform. Four isoforms of ADAM12 have been described that are produced by alternative splicing. Isoform 1 is a single-pass transmembrane protein and isoforms 2,3, and 4 are secreted proteins. ADM12 is synthesized with a signal peptide (aa 1-28) and a propeptide (aa 29-207), which are subsequently cleaved off in the mature form. Isoform 1 shown to be expressed in placenta and in skeletal, cardiac, and smooth muscle. Isoform 2 is reported to be expressed only in placenta or in embryo and fetus. ADAM12 contains a cysteine rich domain (aa 514-649) that support cell adhesion through syndecans and triggers signaling events that lead to beta-1 integrin-dependent cell spreading. However, in carcinoma cells the binding of this domain to syndecans does not allow the integrin-mediated cell spreading. The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. Dissociation of the cysteine from the zinc ion activates the enzyme. Upregulation of ADAM12 has been reported in malignant tumors. In human breast cancer cells expressing ADAM12, MMP-14 is shown to be recruited to the cell surface which results in ADAM12 activation and accelerates tumor progression. ADAM12 does not affect tumor cell proliferation, but it causes a diminution in tumor cell apoptosis and increases stromal cell apoptosis. (Ref.: Sundberg, C., et al. (2004). J. Biol. Chem. 279(49); 51601 51611; Albrechtsen, R., et al. (2013). J. Cell Sci. 126(20); 4707 4720; Kveiborg, M., et al. (2005). Cancer Res. 65(11); 4754-4761).
Specifications
ADAM 12 | |
Monoclonal | |
Unconjugated | |
Purified mouse monoclonal antibody IgG1 in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide. | |
ADAM12;MLTN;UNQ346/PRO545 | |
A full-length recombinant human ADAM12 secreted expressed in HEK293 cells. | |
100 μg | |
Apoptosis & Cancer | |
NP_001275903 | |
Human | |
Purified |
Flow Cytometry, Immunocytochemistry, Immunoprecipitation, Inhibition Assays, Western Blot | |
8F8 | |
Immunoprecipitation Analysis: A representative lot immunoprecipitated ADAM 12 in Immunoprecipitation applications (Kveiborg, M., et. al. (2005). Cancer Res. 65(11):4754-61).Inhibition Analysis: A representative inhibited ADAM 12 induced gelatin degradation. (Albrechtsen, R., et. al. (2013). J Cell Sci. 126(Pt 20):4707-20). Flow Cytometry Analysis: 1μg from a representative lot detected ADAM 12 in one million ADAM 12-DeltaCyt MCF-7 cells.Immunocytochemistry Analysis: A representative lot detected ADAM 12 in Immunocytochemistry applications (Sundberg, C., et. al. (2004). J Biol Chem. 279(49):51601-11).Western Blotting Analysis: A representative lot detected ADAM 12 in Western Blotting applications (Kveiborg, M., et. al. (2005). Cancer Res. 65(11):4754-61). | |
Disintegrin and metalloproteinase domain-containing protein 12;Meltrin-alpha | |
Mouse | |
Protein G purified | |
RUO | |
Primary | |
Clone 8F8 detects ADAM 12-DeltaCyt secreted form in human cells. It targets an epitope with in the prodomain region. | |
Stable for 1 year at 2-8°C from date of receipt. | |
IgG1 κ |
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