| Product description |
Rabbit polyclonal to ADAM33ADAM13 was also found in liver, heart, and intestines from adult Xenopus. Other papers have investigated SH3 ligand domains in the cytoplasmic portion of ADAM13, demonstrating regulation routes for ADAM13 via Src and Src tyrosine kinase. ADAM13 may also act as a cell-attachment molecule, by binding integrins through the cysteine-rich domain. ADAM13 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, as well as disintegrin, cysteine-rich, EFG-like, transmembrane and cytoplasmic domains. ADAM13 cleaves fibronectin after binding to the EGF-like domain. ADAM-13 is also shed from cells in culture, cleaved N-terminally from the transmembrane domain, and released into the culture media. Shed ADAM13 is a 52 kDa protein, and forms complexes with alpha 2-macroglobulin. Xenopus ADAM13 has the greatest homology with human ADAM33 (51% identical), and is 46% identical with human or mouse ADAM12 or ADAM19. It is unclear if any of these ADAMs (ADAM12, ADAM19 or ADAM33) are species orthologs of Xenopus ADAM13, but there are significant differences among the related sequences, suggesting that ADAM13 may be a unique protein. Full length Xenopus ADAM13 is a 914 amino acid protein with a predicted mass is 99.7 kDa. Glycosylation and cyteine-rich regions give Xenopus ADAM13 an apparent molecular weight of 120 kDa (unprocessed) and 97 kDa (processed) on reduced SDS PAGE gels. ADAM13 contains a putative furin cleavage site, suggesting that a prohormone convertase cleaves the propeptide domain from the catalytic domain. |
