ADAM10
ADAM10 (ADAM metallopeptidase domain 10, also known as kuz, MADM, HsT18717 and CD156C) is a cell surface metalloproteinase of the ADAM family. It combines adhesion and protease domains and cleaves a range of proteins, including TNF-alpha and E-cadherin. Browse Assay Genie's current range of ADAM10 research reagents below, or read on for the biology behind the target.
ADAM10 belongs to the ADAM family, whose members are cell surface proteins with a distinctive structure that carries both potential adhesion and protease domains. The enzyme is classified as EC 3.4.24.81. According to the NCBI Gene summary, it cleaves many proteins, among them TNF-alpha and E-cadherin, which places it in the shedding of membrane-bound substrates and in the regulation of cell adhesion.
UniProt records the protein at several sites: the cell membrane, the Golgi apparatus membrane, clathrin-coated vesicles, axons, dendrites, adherens junctions and the cytoplasm. The human ADAM10 gene is a member of the HGNC groups for ADAM metallopeptidase domain containing genes and CD molecules, and the protein carries the CD designation CD156c. Alternate splicing gives multiple transcript variants that encode different proteins, which may undergo similar processing. Mouse and rat both have an Adam10 ortholog.
UniProt also describes a role in microbial infection. ADAM10 promotes the cytotoxic activity of the Staphylococcus aureus toxin hly by binding to the toxin at the zonula adherens and promoting the formation of toxin pores. The protein has also been catalogued under the names kuz, MADM and HsT18717, and the earlier HGNC name was a disintegrin and metalloproteinase domain 10. Researchers studying ADAM10 often work alongside related family members such as ADAM17 and ADAM9.
ADAM10 cleaves membrane proteins including TNF-alpha, making it a relevant protease for studying how cell surface proteins are released and processed.
Cleavage of E-cadherin and localisation at adherens junctions link ADAM10 to the study of cell-cell adhesion.
ADAM10 binds S. aureus hly at the zonula adherens and promotes toxin pore formation, a route into toxin biology.
As a member of the ADAM family with adhesion and protease domains, ADAM10 is a reference point for comparing family functions.
ADAM10 is a cell surface metalloproteinase that cleaves many proteins, including TNF-alpha and E-cadherin. UniProt also notes that it promotes the cytotoxic activity of S. aureus hly by binding the toxin at the zonula adherens and promoting toxin pore formation.
ADAM10 is also called kuz, MADM, HsT18717 and CD156C, and was formerly named a disintegrin and metalloproteinase domain 10. Alternate splicing produces multiple transcript variants that encode different proteins, which may undergo similar processing.
Yes. Mouse and rat each have an Adam10 ortholog of the human gene. For antibody or ELISA work, check the datasheet of any product for its validated reactivity before choosing a species.
Other ADAM family metalloproteinases and ADAMTS enzymes with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt O14672; product specifications from Assay Genie datasheets.