Product Specifications for Recombinant Mouse Marapsin/Pancreasin Protein, CF
Mouse myeloma cell line, NS0-derived mouse Marapsin/Pancreasin protein Ala23-Thr290, with a C-terminal 6-His tag
>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.
N-terminal sequence Analysis
Ala23 & Met38
Predicted Molecular Mass
33 kDa, reducing conditions
Measured by its ability to cleave a colorimetric peptide substrate, N-carbobenzyloxy-Gly-Arg-ThioBenzyl ester (Z-GR-SBzl), in the presence of 5,5’Dithio-bis (2-nitrobenzoic acid) (DTNB). Edwards, K.M. et al. (1999) J. Biol. Chem. 274:30468. The specific activity is >1,200 pmol/min/µg, as measured under the described conditions.
Formulation, Preparation and Storage
What does CF mean?
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our
Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant
protein to be stored at a more dilute concentration.
The carrier free version does not contain BSA.
What formulation is right for me?
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or
as an ELISA standard.
In contrast, the carrier free protein is recommended for applications, in which the presence of BSA
Lyophilized from a 0.2 μm filtered solution in MES and NaCl.
Reconstitute at 100 μg/mL in sterile 25 mM MES and 100 mM NaCl, pH 6.5.
The product is shipped at ambient temperature. 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, -20 to -70 °C as supplied.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Marapsin, Pancreasin, and channel-activating protease 2 (CAP-2), encoded by the Prss27 gene, are different names given for the same serine protease that is expressed strongly in the pancreas (1). The mouse protein is synthesized with a signal peptide (amino acid residues 1‑22), a pro peptide (residues 23‑37) and a mature chain (residues 38‑290) corresponding to the serine protease domain. The full-length protein was expressed and the secreted protein purified. The N-terminal sequencing results indicate that the purified protein is a disulfide bond-linked dimer formed between the pro peptide and the mature chain. The active enzyme has low activity against peptide substrates tested, but high activity against thioester substrates. The peptidase activity is inhibited by 20 mM benzamidine.
Bhagwandin, V.J. et al. (2003) J. Biol. Chem. 278:3363.
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