ADAM-9, also known as MDC9 and Meltrin-g, was first described in muscle cells as a protein with homology to the fertilins (ADAMs 1, 2). Initial observations indicated a role for ADAM9 in myoblast fusion, similar to sperm-egg fusion aided by ADAMs 1 and 2. Later works describe ADAM9 in the lung, heart, brain, kidney, and a wide range of tissues, and examined the ability of ADAM9 to activate TNF-a and HB-EGF, and act as an adhesion molecule with integrin avb5. The Cytoplasmic domain of ADAM9 contains SH3 ligand domains, which are thought to interact with PKC-d, suggesting specific regulation routes for ADAM9. A novel form of ADAM9 was reported in myeloma cells, with truncated amino and carboxyterminal ends, and a 13 amino acid insert in the cysteine-rich domain. A member of the metalloproteinase family containing disintegrin-like domains (ADAMs) the function of ADAM-9 is still poorly understood. ADAM-9 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 ADAM9 sequence codes for an 819 amino acid protein, containing a Type-I transmembrane domain. Predicted mass is 90.5 kD, but glycosylation and cyteine-rich regions make the protein run at 114 kD unprocessed, and 84 kD processed forms. Mouse ADAM9 sequence is 845 AA, predicted at 92 kD. RP1ADAM-9 recognizes bands of 116 kD (minor band), 84 kD (major band), and breakdown products at 50 kD, 34 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. EDTA/EGTA treatment of tissues or lysates is required to see latent zymogen.

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