1. Capture Antibody 1 mg/mL of mouse anti-Human Complement C1s monoclonal antibody (in PBS, pH 7.4). Dilute to a working concentration of 2 μg/mL in PBS before coating. (Catalog: # 10220-MM02) 2. Detection Antibody 0.2 mg/mL of mouse anti-Human Complement C1s monoclonal antibody conjugated to horseradish-peroxidase (HRP) (in PBS, 50 % HRP-Protector, pH 7.4, store at 4℃). Dilute to working concentration of 0.15 μg/mL in detection antibody dilution buffer before use. (Catalog: # 10220-MM04) 3. Standard Each vial contains 180 ng of recombinant Human Complement C1s. Reconstitute with 1 mL detection antibody dilution buffer. After reconstitution, store at -20℃ to -80℃ in a manual defrost freezer. A seven-point standard curve using 2-fold serial dilutions in sample dilution buffer, and a high standard of 6000 pg/mL is recommended.
This C1s Matched ELISA Antibody Pair Set,Human is a solid phase sandwich ELISA for quantitative determination of Human C1s . It contains Human C1s capture antibody, Human C1s detector antibody
and a highly purified
recombinant Human C1s protein. This Pair Set is at affordable price for researchers.
This Matched ELISA Antibody Pair Set is shipped at ambient temperature.
Capture Antibody: Aliquot and store at -20℃ to -80℃ for up to 6 months from date of receipt. Avoid repeated freeze-thaw cycles. Detection Antibody: Store at 4℃ and protect it from prolonged exposure to light for up to 6 months from date of receipt. DO NOT FREEZE! Standard: Store lyophilized standard at -20℃ to -80℃ for up to 6 months from date of receipt. Aliquot and store the reconstituted Standard at -80℃ for up to 1 month. Avoid repeated freeze-thaw cycles.
Complement is an integral component of the adaptive and innate immune systems and represents one of the major effector systems for the immune responses. The classical complement pathway is triggered by C1, a complex composed of the binding protein C1q and two proenzymes, C1r and C1s. Upon binding of IgG to the head of C1q, C1r undergoes autoactivation and in turn cleaves and activates C1s. C1r and C1s, the proteases responsible for activation and proteolytic activity of the C1 complex of complement, share similar overall structural organizations featuring five nonenzymic protein modules (two CUB modules surrounding a single EGF module, and a pair of CCP modules) followed by a serine protease domain. Besides highly specific proteolytic activities, both proteases exhibit interaction properties associated with their N-terminal regions. In contrast, C1r and C1s widely differ from each other by their glycosylation patterns: both proteins contain Asn-linked carbohydrates, but four glycosylation sites are present on C1r, and only two on C1s. As a highly specific serine protease, C1s executes the catalytic function of the C1 complex: the cleavage of C4 and C2, and thus instigates a sequence of activation steps of other components of the complement system, culminating in the formation of the membrane attack complex which induces cell lysis. Like other complement serine proteases C1s has restricted substrate specificity and it is engaged into specific interactions with other subcomponents of the complement system. The only other protein known to interact with C1s physiologically is SerpinC1, an inhibitor of serine protease, which inhibits C1s activity and thus plays a regulatory role in controlling the function of C1s enzyme.
complement component 1, s subcomponent
Complement Activation Pathways
Arlaud GJ, et al. (1989) Structure and function of C1r and C1s: current concepts. Behring Inst Mitt. (84): 56-64.
Thielens NM, et al. (1999) Structure and functions of the interaction domains of C1r and C1s: keystones of the architecture of the C1 complex. Immunopharmacology. 42(1-3): 3-13.
Gl P, et al. (2002) C1s, the protease messenger of C1. Structure, function and physiological significance. Immunobiology. 205(4-5): 383-94.