Recombinant Human Complement Component C1s Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Enzyme Activity
Format
Carrier-Free

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Recombinant Human Complement Component C1s Protein, CF Summary

Details of Functionality
Measured by its ability to cleave a colorimetric peptide substrate, N-carbobenzyloxy-Lys-ThioBenzyl ester (Z-Lys-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 >20,000 pmol/min/µg, as measured under the described conditions.
Source
Mouse myeloma cell line, NS0-derived human Complement Component C1s protein
Met1-Asp688, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Glu16 (A chain) & Ile438 (B chain)
Structure / Form
Disulfide-linked heterodimer
Protein/Peptide Type
Recombinant Enzymes
Gene
C1S
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.

Applications/Dilutions

Theoretical MW
47 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.
SDS-PAGE
62 kDa and 32 kDa, reducing conditions
Publications
Read Publication using
2060-SE in the following applications:

Packaging, Storage & Formulations

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 opening.
Buffer
Supplied as a 0.2 μm filtered solution in Tris, NaCl, CaCl2 and Glycerol.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Assay Procedure
  • Assay Buffer: 50 mM Tris, 250 mM NaCl, pH 8.0
  • Recombinant Human Complement Component C1s (rhC1s) (Catalog # 2060-SE)
  • Substrate: N-Carbobenzyloxy-Lys-ThioBenzyl ester (Z-K-SBzl) (Bachem, Catalog # M-1300), 10 mM stock in DMSO
  • 5,5’Dithio-bis(2-nitrobenzoic acid) (DTNB) (Sigma, Catalog # D-8130), 10 mM stock in DMSO
  • 96-well Clear Plate (Costar, Catalog # 92592)
  • Plate Reader (Model: SpectraMax Plus by Molecular Devices) or equivalent
  1. Dilute rhC1s to 0.2 ng/μL in Assay Buffer.
  2. Dilute Substrate to 1000 μM containing 200 μM DTNB in Assay Buffer.
  3. Load in plate, 50 μL of 0.2 ng/μL rhC1s, and start the reaction by adding 50 μL of 1000 μM Substrate/200 μM DTNB mixture to wells. Include a Substrate Blank containing 50 μL Assay Buffer and 50 μL of 1000 μM Substrate/200 μM DTNB mixture.
  4. Read in kinetic mode for 5 minutes at absorbance of 405 nM.
  5. Calculate Specific Activity:

     Specific Activity (pmol/min/µg) =

Adjusted Vmax* (OD/min) x well volume (L) x 1012 pmol/mol
ext. coeff** (M-1cm-1) x path corr.*** (cm) x amount of enzyme (µg)

     *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:
  • rhC1s: 0.010 μg
  • DTNB: 100 μM
  • Substrate: 500 μM

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Complement Component C1s Protein, CF

  • basic proline-rich peptide IB-1
  • C1 esterase
  • C1S
  • complement C1s subcomponent
  • Complement component 1 subcomponent s
  • complement component 1, s subcomponent
  • Complement Component C1s
  • EC 3.4.21
  • EC 3.4.21.42
  • FLJ44757

Background

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 1-688) of human C1s was expressed (3-5). The purified protein corresponded to the processed active form, with A and B chains starting at residue Glu16 and Ile438, respectively.

  1. Arlaud, G.J. et al. (2002) Biochem. Soc. Trans. 30:1001.
  2. Lacroix, M. et al. (2001) J. Biol. Chem. 276:36233.
  3. Tosi, M. et al. (1987) Biochemistry 26:8516.
  4. Mackinnon, C.M. et al. (1987) Eur. J. Biochem. 169:547.
  5. Kusumoto, H. et al. (1988) Proc. Natl. Acad. Sci. USA 85:7307.

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Publications for Complement Component C1s (2060-SE)(1)

We have publications tested in 1 confirmed species: Human.

We have publications tested in 1 application: Competitive Binding Assay.


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Competitive Binding Assay
(1)
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Bioinformatics

Gene Symbol C1S
Uniprot