Technical Data
Complement 1s (C1s)
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 688aa. 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) comprises 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).

Fusion Partner:

NMRI x BALB/c mice immunized i.p. with immunogen adsorbed onto AI(OH)3

Suitable for use in ELISA. Other applications not tested.

Recommended Dilution:
ELISA: 1:10,000
Optimal dilutions to be determined by the researcher.

Storage and Stability:
For long-term storage, aliquot and store 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.
MabIgG1,k6F44Affinity Purified
100ul-20CBlue IceHumanMouse
C1s proenzyme purified from human plasma
Purified by Protein A/G affinity chromatography from culture supernatant.
Supplied as a liquid in PBS, pH 7.4, 15mM sodium azide, before the addition of glycerol to 40%.
Specific for C1s proenzyme and activated free C1s. 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, G.J., The Complement FactsBook. Morley, B.J. & Walport, M.J., (eds). AP FactsBook Series. Academic Press, London (2000). 2. Strunk, R.C. & Colten, H.R., Complement in Health and Disease, 2nd edition, Whaley, K., Loos, M. & Weiler, J.M., (eds). Kluwer Academic Publications, Dordrecht (1993). 3. Morgan, B.P. & Gasque, P., Immunol. Today 17: 461-466 (1996). 4. Arlaud, G.J. & Thielens, N.M., Methods Enzymol. 223: 61-82 (1993). 5. Arlaud, G.J., et al., Biochem. Soc. Trans. 30: 1001-1006 (2002).