ADAM-13 was first described as a protein expressed in somatic mesoderm and neural crest cells, in developing Xenopus embryos. ADAM13 was found in liver, heart and intestines from adult Xenopus. Other papers 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. A member of the metalloproteinase family containing disintegrin-like domains (ADAMs) the functions of ADAM-13 are still poorly understood. ADAM-13 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, as well as disintegrin, cysteine-rich, EFG-like, transmembrane and Cytoplasmic domains. ADAM-13 has been shown to be proteolytically active, cleaving fibronectin after binding it to the EGF-like domain. ADAM-13 is also shed from cells in culture, cleaved aminoterminal from the transmembrane domain, and is released into the culture media. Shed ADAM-13 is a 52 kD protein, and can form complexes with a2-macroglobulin, suggesting it is a competent protease. Xenopus ADAM-13 has greatest homology with human ADAM-33 (51% identical), and is 46% identical with human or mouse ADAM-12 or ADAM-19. It is still unclear if any of these ADAMs are species orthologs of Xenopus ADAM13, but there are significant differences between the related sequences, suggesting that ADAM-13 may be a unique protein. Other ADAMs family members (ADAM-10, ADAM-17) have been more thoroughly studied, and are known to play key roles in inflammation, growth factor maturation and release, and a wide range of other functions. The full length Xenopus ADAM13 sequence codes for a 914 amino acid protein. Predicted mass is 99.749 kD, but glycosylation and cyteine-rich regions give Xenopus ADAM-13 an apparent MW of 120 kD unprocessed, and 97 kD processed forms, on reduced SDS PAGE gels. ADAM-13 contains a putative furin cleavage site, suggesting that a prohormone convertase cleaves the propeptide domain away from the catalytic domain. RP1ADAM-13 recognizes bands of 120 kD (minor band), 92 kD (major band), and cleaved products at 68 kD, 40 kD in reduced Western blots of cell lysates. A recommended starting concentration for Western blots is 1:1000 when using colorimetric substrates such as BCIP/NBT, and 1:5000 for chemiluminescent substrates. Higher concentrations of antibody may be needed for samples from more distantly related species.

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