| Reactivity | MuSpecies Glossary |
| Applications | Enzyme Activity |
| Format | Carrier-Free |
| Details of Functionality | 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. |
| Source | Mouse myeloma cell line, NS0-derived mouse Marapsin/Pancreasin protein Ala23-Thr290, with a C-terminal 6-His tag |
| Accession # | |
| N-terminal Sequence | Ala23 & Met38 |
| Protein/Peptide Type | Recombinant Enzymes |
| Gene | Prss27 |
| Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
| Endotoxin Note | <1.0 EU per 1 μg of the protein by the LAL method. |
| Dilutions |
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| Theoretical MW | 28 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. |
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| SDS-PAGE | 33 kDa, reducing conditions |
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| Publications |
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| Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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| Buffer | Lyophilized from a 0.2 μm filtered solution in MES and NaCl. |
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| Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
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| Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile 25 mM MES and 100 mM NaCl, pH 6.5. |
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| Assay Procedure |
*Adjusted for Substrate Blank **Using the extinction coefficient 13260 M-1cm-1 ***Using the path correction 0.320 cm Note: the output of many spectrophotometers is in mOD. Per Well:
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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.
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