| Reactivity | HuSpecies 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 >1,500 pmol/min/µg, as measured under the described conditions. |
| Source | Mouse myeloma cell line, NS0-derived human Complement Component C1r protein Met1-Asp705, with a C-terminal 10-His tag |
| Accession # | |
| N-terminal Sequence | Ser18 (A chain) & Ile464 (B chain) |
| Structure / Form | Disulfide-linked heterodimer |
| Protein/Peptide Type | Recombinant Enzymes |
| Gene | C1R |
| 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 | 51 kDa (A chain) & 28 kDa (B chain). 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 | 60 kDa & 40 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 Tris 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 50 mM Tris and 150 mM NaCl, pH 7.5. |
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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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The classical complement pathway plays a major role in innate immunity against infection. This pathway is triggered by C1, a multimolecular complex composed of the recognition protein C1q and two serine proteases, C1r and C1s. Following the C1q recognition, C1r is autoactivated, and in turn activates C1s, which cleaves C4 and C2, the C1 substrates (1). Both C1r and C1s activation involve cleavage of a specific Arg-Ile bond, converting single-chain proenzymes into active proteases of disulfide bond-linked chains (A and B) (2). The A chains contain multiple domains in the order of CUB1-EGF-CUB2-CCP1-CCP2-Activation Peptide. The B chains contain the serine protease catalytic domain. The full-length (amino acid residues 1-705) of human C1r was expressed, which had the Leu152 natural variant (3). The purified protein corresponded to the processed active form, with A and B chains starting at residue Ser18 and Ile464, respectively.
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