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 ADAM-15 does not contain the RGD sequence; instead the mouse ADAM-15 has a TDD in its place. Like ADAM-9 and ADAM-12, there are SH3 ligand domains in the cytoplasmic portion of ADAM-15, suggesting regulation routes for ADAM-15 via Src and Src tyrosine kinase. ADAM-15 is widely expressed in normal tissues and tumor cell lines, and is expressed on the cell surface, anchored by the transmembrane domain. ADAM-15 is also elevated in osteoarthric and rheumatoid synovial tissues, suggesting an inflammatory role. ADAM-15 may also act as a cell-attachment molecule, by binding the integrins ?v?3, ?9?1 and ?v?5 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 ADAM-15 sequence codes for an 814 amino acid protein. Predicted mass is 85 kD, but glycosylation and cyteine-rich regions make the reduced protein run at 110 kD for unprocessed, and at 84 kD for processed forms. RP3-ADAM-15 recognizes bands at 110 kD (the zymogen) and 90 kD (the furin-processed form). A series of cleaved products at 55 kD and 40 kD can also be seen in reduced Western blots of cell lysates. A recommended starting concentration for Western blots is 1:1,000 when using colorimetric substrates such as BCIP/NBT, and 1:5,000 for chemiluminescent substrates. Higher concentrations of antibody may be needed for samples from more distantly related species.

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