ADAM-15, also known as Metargidin and MDC15, was first described in mammary epithelial carcinoma cells as a membrane-anchored Metalloprotease-Disintegrin with RGD sequence (MetaRGiDin). Mouse ADAM15 does not contain the RGD sequence: instead the mouse ADAM15 has a TDD in its place. Like ADAM9 and ADAM12, there are SH3 ligand domains in the Cytoplasmic portion of ADAM15, suggesting regulation routes for ADAM15 via Src and Src tyrosine kinase. ADAM15 is widely expressed in normal tissues and tumor cell lines, and is expressed on the cell surface, anchored by the transmembrane domain. ADAM15 is also elevated in osteoarthric and rheumatoid synovial tissues, suggesting an inflammatory role. ADAM15 may also act as a cell-attachment molecule, by binding the integrins αvβ3, α9β1 and αvβ5 through the cysteine-rich domain and/or RGD sequence. A member of the metalloproteinase family containing disintegrin-like domains (ADAMs) the functions of ADAM-15 are still poorly understood. ADAM-15 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, and has been shown to be proteolytically active. 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 ADAM15 sequence codes for a 814 amino acid protein. Predicted mass is 85 kD, but glycosylation and cyteine-rich regions make the reduced protein run at 110 kD unprocessed, and 84 kD processed forms. RP2ADAM-15 recognizes bands of 110 kDand, the zymogen but not the 90 kD furin-processed form of ADAM15. A series of cleaved products at 55, 48 kD, 40 kD can also be seen 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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