Technical Data
C7850-08D
Complement 1s (C1s)
Description:
C1s proenzyme is a 79.8kD glycoprotein produced primarily by hepatocytes (1) but also by other cells (2,3). The proenzyme is produced as a single-chain polypeptide of 688 aa. Upon activation the peptide is cleaved between R437 and I438 giving the activated enzyme consisting of two disulfide-linked chains, A chain (52.2kD) and B chain (27.7kD). The Ca-dependent catalytic subunit of the C1 complex (C1q, C1r, C1s) is comprised of two C1s and two C1r molecules and this serine protease tetramer is responsible for the initial steps in the classical complement pathway, cleavage of C4 and C2 (1,4,5).

Applications:
Suitable for use in ELISA. Other applications not tested.

Recommended Dilution:
ELISA: 1:1000
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. For long-term storage and to avoid repeated freezing and thawing, aliquot and add glycerol (40-50%). Freeze at -20C. Aliquots are stable for at least 12 months at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
TypeIsotypeCloneGrade
MabIgG1,k49Affinity Purified
SizeStorageShippingSourceHost
100ul-20CBlue IceHumanMouse
Concentration:
~1mg/ml
Immunogen:
Human plasma C1s Proenzyme.
Purity:
Purified by Protein A/G affinity chromatography from culture supernatant.
Form
Supplied as a liquid in PBS, pH 7.2, 15mM sodium azide.
Specificity:
Specific for C1s proenzyme and activated free C1s and C1s in complex with C1 inhibitor. Epitope differs from that of clone 6F44. Reacts in ELISA when tested with activated C1s enzyme directly coated onto the microtiter well or in sandwich ELISA in combination with a polyclonal antibody in coat.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Thielens N, Arlaud GJ (2000) The Complement FactsBook. Morley BJ, Walport MJ (eds). AP FactsBook Series. Academic Press, London.
2. Strunk RC, Colten HR (1993) Complement in Health and Disease, 2nd edition, Whaley K, Loos M, Weiler JM (eds). Kluwer Academic Publications, Dordrecht.
3. Morgan BP, Gasque P (1996) Expression of complement in the brain: role in health and disease. Immunol Today 17:461-466.
4. Arlaud GJ, Thielens NM (1993) Human complement serine proteases C1r and C1s and their proenzymes. Methods Enzymol 223:61-82.
5. Arlaud GJ, Gaboriaud C, Thielens NM, Rossi V (2002) Structural biology of C1. Biochem Soc Trans 30:1001-1006.