Measured by its ability to cleave a fluorogenic peptide substrate, Mca-SEVNLDAEFRK(Dpn)RR-NH2 (Catalog # ES004). The specific activity is >3,000 pmol/min/µg, as measured under the described conditions.
Mouse myeloma cell line, NS0-derived mouse Meprin beta Subunit/MEP1B protein Leu21-Ser594 (Thr75Ile and Ile432Val), with a C-terminal 10-His tag Accession # Q61847
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
<1.0 EU per 1 μg of the protein by the LAL method.
67 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
80-83 kDa doublet, reducing conditions
Read Publication using 3300-ZN in the following applications:
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 704 amino acid sequence of mouse meprin beta subunit precursor consists of a signal peptide (residues 1 to 20), a pro region (residues 21 to 62), and a mature chain (residues 63 to 704) containing following domains, catalytic (residues 63 to 260), MAM (residues 261 to 430), MATH (residues 431 to 586), EGF-like (residues 607 to 647), transmembrane (residues 655 to 678), and cytoplasmic (residues 679 to 704). The pro enzyme terminating at residue 594 was expressed and the secreted protein purified from conditioned medium. The amino acid sequence has Ile and Val at position 75 and 432 instead of Thr and Ile, respectively. After trypsin treatment, the activated enzyme cleaved a flurogenic peptide, which contains Asp and Glu, the preferred residues found in the P1’ and P1 sites (3).
Bond, J.S. and R.J. Beynon (1995) Protein Sci. 4:1247.
Stocker, W. et al. (1995) Protein Sci. 4:823.
Bertenshaw, G.P. et al. (2001) J. Biol. Chem. 276:13248.
Ishmael, F.T. et al. (2005) J. Biol. Chem. 280:13895.
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