Synthesized peptide derived from the Internal region of Human C1s HC.
Immunogen Species
Homo sapiens (Human)
Conjugate
Non-conjugated
Isotype
IgG
Purification Method
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Tested Applications
WB, ELISA
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Usage
For Research Use Only. Not for use in diagnostic or therapeutic procedures.
C1s B chain is a serine protease that combines with C1q and C1r to form C1, the first component of the classical pathway of the complement system. C1r activates C1s so that it can, in turn, activate C2 and C4.
Gene References into Functions
TNT003, an inhibitor of the serine protease C1s, prevents complement activation induced by cold agglutinins.PMID:24695853
Data indicate that complement C1s mRNA level was low in ICR-derived glomerulonephritis (ICGN) mice liver as compared with age-matched ICR mice.PMID:23989031
A molecular switch governs the interaction between the human complement protease C1s and its substrate, complement C4.PMID:23592783
Four positively charged amino acids on the serine protease domain appear to form a catalytic exosite that is required for efficient cleavage of C4 in the classical pathway of complement.PMID:22855709
Detailed mapping of post-translational modifications and insights into the C1r/C1s binding sites.PMID:20008834
Interaction with the prime side residues at the cleavage point in C1s enhances the affinity of the enzyme for complement 2 and complement 4 substrates; these prime subsite residues mediate positive cooperativity in the cleavage of the substrate.PMID:14674770
full specificity of the enzyme using a randomized phage display libraryPMID:16169853
There are splice variants of C1s mRNA transcripts in normal human cellsPMID:18062908