The ADAM family is composed of zinc-binding proteins that can function as adhesion proteins and/or endopeptidases.The prototypic ADAM protein has a prodomain, a metalloprotease domain, a disintegrin domain, a cysteine-rich region, a transmembrane domain, and a variable cytoplasmic tail.
ADAMDEC1 belongs to a novel ADAM subfamily due to its partial lack of a disintegrin domain and its total lack of a cysteine-rich domain.ADAMDEC1 protein has 2 unique features compared with other ADAM proteins: the third histidine residue in its zinc-binding site is replaced with an aspartate, and it prematurely terminates in the disintegrin domain, deleting half the disintegrin domain as well as the cysteine-rich domain, the transmembrane domain, and the intracellular tail.
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