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Recombinant Human Meprin beta Subunit/MEP1B Protein, CF

Catalog # 2895-ZN | R&D Systems, Inc. a Bio-Techne Brand
Catalog #
Size / Price

Key Product Details



Accession #

Structure / Form

Pro form




Enzyme Activity

Product Specifications


Mouse myeloma cell line, NS0-derived human Meprin beta Subunit/MEP1B protein
Leu21-Ser593 & Thr23-Ser593, both with a C-terminal 10-His tag


>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Endotoxin Level

<1.0 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Leu21 & Thr23

Predicted Molecular Mass

66 kDa


85 kDa, reducing conditions


Measured by its ability to cleave a fluorogenic peptide substrate, Mca-SEVNLDAEFRK(Dpn)RR-NH2 (Catalog # ES004).
The specific activity is >350 pmol/min/µg, as measured under the described conditions.

Formulation, Preparation and Storage

Formulation Supplied as a 0.2 μm filtered solution in Tris, NaCl and Glycerol.
Shipping The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.

Background: Meprin beta Subunit/MEP1B

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 Merpin A (composed of alpha subunits with or without beta subunits) and Merpin 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 701 amino acid sequence of human Merpin beta subunit precursor consists of a signal peptide (residues 1 to 21), a pro region (residues 22 to 61), and a mature chain (residues 62 to 701) containing the following domains, catalytic (residues 62 to 259), MAM (residues 260 to 429), MATH (residues 430 to 585), EGF-like (residues 604 to 644), transmembrane (residues 653 to 673), and cytoplasmic (residues 674 to 701). The pro enzyme terminating at residue 593 was expressed and the secreted protein purified from conditioned medium. 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).


  1. Bond, J.S. and R.J. Beynon (1995) Protein Sci. 4:1247.
  2. Stocker, W. et al. (1995) Protein Sci. 4:823.
  3. Bertenshaw, G.P. et al. (2001) J. Biol. Chem. 276:13248.
  4. Ishmael, F.T. et al. (2005) J. Biol. Chem. 280:13895.

Alternate Names


Entrez Gene IDs

4225 (Human); 17288 (Mouse)

Gene Symbol



Product Documents for Recombinant Human Meprin beta Subunit/MEP1B Protein, CF

Certificate of Analysis

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Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Recombinant Human Meprin beta Subunit/MEP1B Protein, CF

For research use only

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