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ADAM12  Protein, Antibody, ELISA Kit, cDNA Clone

Description: Active  
Expression host: Human Cells  
10896-H08H-50
10896-H08H-20
50 µg 
20 µg 
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ADAM12 Related Area

ADAM12 Related Pathways

ADAM12 Related Protein, Antibody, cDNA Gene, and ELISA Kits

ADAM12 Related Protein, Antibody, cDNA Gene, and ELISA Kits

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ADAM12 Summary & Protein Information

ADAM12 Background

Cofactor: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; ; Note=Binds 1 zinc ion per subunit.;
Subunit structure: Interacts with alpha-actinin-2 and with syndecans (By similarity). Interacts with SH3PXD2A. Interacts with FST3. Interacts with GNB2L1/RACK1; the interaction is required for PKC-dependent translocation of ADAM12 to the cell membrane. {ECO:0000250, ECO:0000269|PubMed:10831617, ECO:0000269|PubMed:12615925, ECO:0000269|PubMed:15574124, ECO:0000269|PubMed:18621736}.
Domain: The cysteine-rich domain supports cell adhesion through syndecans and triggers signaling events that lead to beta-1 integrin-dependent cell spreading. In carcinomas 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. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Subcellular location: Isoform 1: Cell membrane; Single-pass type I membrane protein.; Isoform 2: Secreted.; Isoform 3: Secreted {ECO:0000305}.; Isoform 4: Secreted {ECO:0000305}.
Tissue specificity: Isoform 1 is expressed in placenta and skeletal, cardiac, and smooth muscle. Isoform 2 seems to be expressed only in placenta or in embryo and fetus. Both forms were expressed in some tumor cells lines. Not detected in brain, lung, liver, kidney or pancreas.
Post-translational: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.
Sequence similarity: Contains 1 disintegrin domain. {ECO:0000255|PROSITE-ProRule:PRU00068}.; Contains 1 EGF-like domain. {ECO:0000255|PROSITE-ProRule:PRU00076}.; Contains 1 peptidase M12B domain. {ECO:0000255|PROSITE-ProRule:PRU00276}.
General information above from UniProt

The ADAMs (a disintegrin and metalloprotease) comprise a family of multidomain proteins with metalloprotease, cell adhesion, and signaling activities. Human ADAM12, which is implicated in diseases such as cancer, is expressed in two splice forms, the transmembrane ADAM12-L and the shorter and soluble ADAM12-S. ADAM12, also known as and Meltrin alpha, is a member of the ADAM protein family, which contains one disintegrin domain, one EGF-like domain and one peptidase M12B domain. ADAM12 is synthesized as a zymogen with the prodomain keeping the metalloprotease inactive through a cysteine-switch mechanism. Maturation and activation of the protease involves the cleavage of the prodomain in the trans-Golgi or possibly at the cell surface by a furin-peptidase. It is a membrane-anchored metalloprotease, which has been implicated in activation-inactivation of growth factors that play an important role in wound healing, including heparin-binding epidermal growth factor (EGF)-like growth factor (HB-EGF) and IGF binding proteins. ADAM12 may also regulate cell-cell and cell-extracellular matrix contacts through interactions with cell surface receptors - integrins and syndecans - potentially influencing the actin cytoskeleton. Moreover, ADAM12 interacts with several cytoplasmic signaling and adaptor molecules through its intracellular domain, thereby directly transmitting signals to or from the cell interior. These ADAM12-mediated cellular effects appear to be critical events in both biological and pathological processes. In addition to protease activity, ADAM12 possesses cell binding and cell signaling properties. In many studies, ADAM12 overexpression has been correlated with disease, and ADAM12 has been shown to promote tumor growth and progression in cancer. On the other hand, protective effects of ADAM12 in disease have also been reported.

ADAM12 Alternative Name

MCMP,MLTN,CAR10,MLTNA,MCMPMltna,ADAM12-OT1, [homo-sapiens]
ADAM12-OT1,CAR10, [Human]
Adam12,KIAA4001,mKIAA4001,Mltna, [mouse]
Mltna,mKIAA4001, [mus-musculus]

ADAM12 Related Studies

  • Wewer UM, et al. (2006) ADAM12 is a four-leafed clover: the excised prodomain remains bound to the mature enzyme. J Biol Chem. 281(14): 9418-22.
  • Kveiborg M, et al. (2008) Cellular roles of ADAM12 in health and disease. Int J Biochem Cell Biol. 40(9): 1685-702.
  • Harsha A, et al. (2008) ADAM12: a potential target for the treatment of chronic wounds. J Mol Med. 86(8): 961-9.
  • Jacobsen J, et al. (2009) Targeting ADAM12 in human disease: head, body or tail? Curr Pharm Des. 15(20): 2300-10.
  • Baertling F, et al. (2010) ADAM12 is expressed by astrocytes during experimental demyelination. Brain Res. 1326: 1-14.
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