Mouse Meprin  alpha  Subunit/MEP1A Alexa Fluor® 594-conjugated Antibody

Applications

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Preparation and Storage

Background: Meprin alpha Subunit/MEP1A

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 hetero-oligomers, 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 760 amino acid sequence of mouse meprin alpha  subunit precursor consists of a signal peptide (residues 1‑33), a pro region (residues 34‑77), and a mature chain (residues 78‑760) containing the following domains, catalytic (residues 78‑275), MAM (residues 276‑445), MATH (residues 447‑607), EGF-like (residues 684‑724), transmembrane (residues 727‑754), and cytoplasmic (residues 755‑760) (5). The pro enzyme terminating at residue 615 was expressed and the secreted protein purified from conditioned medium. The molecular masses of recombinant mouse MEP1A are similar to those observed for the alpha  subunit of rat Meprin A (6).

Product Datasheets

Related Research Areas

• Metalloproteases and Regulators
• Search Bioprocessing Enzymes