ADAM-19, also known as Meltrin-beta, was first described in muscle cells as a protein with homology to the fertilins (ADAMs 1, 2). Initial observations indicated a role for ADAM19 in myoblast fusion, similar to sperm-egg fusion aided by ADAMs 1 and 2. Later works describe ADAM19 in the bone, muscle, lung, heart, brain, kidney, and a wide range of tissues. The Cytoplasmic domain of ADAM19, like ADAMs 9, 12 and 15, contains SH3 ligand domains, which are thought to interact with PKC-d, suggesting specific regulation routes for ADAM19. Also reported is a sequence of ADAM19 lacking the transmembrane and cytoplasmic domains, suggesting that a soluble form is produced. A member of the metalloproteinase family containing disintegrin-like domains (ADAMs) the function of ADAM-19 is still poorly understood. ADAM-19 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 ADAM19 sequence codes for a 956 amino acid protein, containing a Type-I transmembrane domain, with a predicted mass is 105 kD. Two shorter sequences have been reported: a 918 amino acid sequence that differs at the carboxyterminal end, and the soluble form, a 538 amino acid version with predicted mass of 59.9 kD. Mouse ADAM19 sequence is 920 AA, predicted at 100.86 kD. RP1ADAM-19 recognizes bands of 95 kD, 84 kD (major band), and breakdown products at 50 kD, 34 kD in reduced Western blots of cell lysates. A strong band at 30 kD is often seen, most likely the propeptide domain cleaved after furin activation of ADAM19. 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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