Human Meprin  alpha Subunit/MEP1A Biotinylated Antibody

Meprins are multimeric proteases composed of alpha and beta subunits, which are members of the astacin family of zinc endopeptidases (1, 2). Both subunits form disulfide‑linked homo- or heterooligomers, which are also referred to as Meprin A (composed of alpha subunits with or without beta subunits) and Meprin B (composed of beta subunits only) (3). Although the two subunits share 42% identity in their amino acid sequence, they differ significantly in their oligomeric structure, post-translational processing and subsequently cellular location, and substrate and peptide bond specificity (4). The 746 amino acid sequence of human meprin alpha subunit precursor consists of a signal peptide (residues 1 to 21), a pro region (residues 22 to 65), and a mature chain (residues 66 to 746) containing following domains, catalytic (residues 62 to 263), MAM (residues 264 to 433), MATH (residues 434 to 593), EGF-like (residues 670 to 710), transmembrane (residues 713 to 740), and cytoplasmic (residues 741 to 746). The pro enzyme terminating at residue 601 was expressed and the secreted protein purified from conditioned medium. The molecular masses of rhMEP1A are similar to those observed for the alpha subunit of rat Meprin A (5).