Recombinant Human Complement Component C1r Protein, CF
R&D Systems, part of Bio-Techne | Catalog # 1807-SE
Key Product Details
Source
NS0
Accession #
Structure / Form
Disulfide-linked heterodimer
Conjugate
Unconjugated
Applications
Enzyme Activity
Product Specifications
Source
Mouse myeloma cell line, NS0-derived human Complement Component C1r protein
Met1-Asp705, with a C-terminal 10-His tag
Met1-Asp705, with a C-terminal 10-His tag
Purity
>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
Ser18 (A chain) & Ile464 (B chain)
Predicted Molecular Mass
51 kDa (A chain) & 28 kDa (B chain)
SDS-PAGE
60 kDa & 40 kDa, reducing conditions
Activity
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.
The specific activity is >1,500 pmol/min/µg, as measured under the described conditions.
Reviewed Applications
Read 1 review rated 5 using 1807-SE in the following applications:
Formulation, Preparation and Storage
1807-SE
| Formulation | Lyophilized from a 0.2 μm filtered solution in Tris and NaCl. |
| Reconstitution | Reconstitute at 100 μg/mL in sterile 50 mM Tris and 150 mM NaCl, pH 7.5. |
| Shipping | 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.
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Background: Complement Component C1r
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.
References
- Arlaud, G.J. et al. (2002) Biochem. Soc. Trans. 30:1001.
- Lacroix, M. et al. (2001) J. Biol. Chem. 276:36233.
- Journet A. and M. Tosi (1986) Biochem. J. 240:783.
Alternate Names
C1r
Entrez Gene IDs
715 (Human)
Gene Symbol
C1R
UniProt
Additional Complement Component C1r Products
Product Documents for Recombinant Human Complement Component C1r Protein, CF
Product Specific Notices for Recombinant Human Complement Component C1r Protein, CF
For research use only
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