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Active Native Human C1S Enzyme

Cat.No. : C1S-550H
Product Overview : C1s enzyme is a high molecular weight, two chain, trypsin-like protease composed of disulfide-linked chains of 58,000 and 28,000 daltons. C1s is present in plasma at 31 μg/mL. C1s proenzyme is a high molecular weight, single chain, trypsin-like zymogen (86,000 daltons). C1s proenzyme is activated by C1r enzyme. Two C1r form a C1r-C1r complex in the presence of calcium which in turn forms a stable complex with two C1s molecules in the presence of calcium. This tetramer can exist in solution, but in the presence of C1q it binds to C1q forming the C1 complex which is stable in the presence of calcium. C1r self-activation, and subsequent C1s activation, is controlled by a weak association of C1r with C1esterase inhibitor (C1-INH) when it is in the C1 complex and similar stabilization occurs with purified C1r. C1s and C1r enzymes, however, are irreversibly inactivated by binding to C1-INH.
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Description : C1s enzyme is the activated form of C1s proenzyme. C1s is a subunit of the C1 complex which is the first complement component in the classical pathway of complement. C1s proenzyme is an inactive zymogen until C1 is activated. C1s proenzyme is activated when C1 binds to and is activated by antibodies bound to antigens (immune complexes) yielding C1r enzyme, the first protease that initiates the cascade. C1r enzyme in the C1 complex activates C1s proenzyme generating C1s enzyme. C1 complex is a non-covalent calcium-dependent complex of one C1q, two C1r and two C1s molecules. C1q binds by two or more of its six arms to the Fc domains of IgG or IgM. The binding of multiple arms to immune complexes causes the two C1r proteins in the complex (protease zymogens) to activate producing two proteases that cleave and activate the two C1s proenzymes in the complex. This activation of C1s proenzyme results in its cleavage into the two chain C1s enzyme with 58,000 and 28,000 dalton fragments. Activated C1s enzyme cleaves complement component C4 releasing C4a and initiating covalent attachment of C4b to the activating surface. Activated C1s also cleaves C2 and the larger fragment of C2 binds to the surface-attached C4b forming C4b,C2a, the C3/C5 convertase of the classical pathway.
Species : Human
Form : Frozen liquid
Bio-activity : >90 % C1s will bind with excess C1-INH.
Molecular Mass : 86,000 Da (2 chains)
Endotoxin : This protein is purified from human serum and therefore precautions appropriate for handling any blood-derived product must be used even though the source was shown by certified tests to be negative for HBsAg, HTLV-I/II, STS, and for antibodies to HCV, HIV-1 and HIV-II.
Purity : ≥90 % by SDS PAGE (Note: C1s enzyme is 86,000 unreduced, but upon reduction runs as 58,000 and 28,000 chains on SDS PAGE).
Storage : Store it at -70°C or below. Avoid freeze/thaw.
Concentration : 1.0 mg/mL
Storage Buffer : 50 mM sodium phosphate, 130 mM NaCl, pH 7.2.
Preservative : None, 0.22 μm filtered.
Gene Name : C1S complement component 1, s subcomponent [ Homo sapiens ]
Official Symbol : C1S
Synonyms : C1S; complement component 1, s subcomponent; complement C1s subcomponent; C1 esterase; basic proline-rich peptide IB-1; complement component 1 subcomponent s; FLJ44757;
Gene ID : 716
mRNA Refseq : NM_001734
Protein Refseq : NP_001725
MIM : 120580
UniProt ID : P09871
Chromosome Location : 12p13
Pathway : Classical antibody-mediated complement activation, organism-specific biosystem; Complement Activation, Classical Pathway, organism-specific biosystem; Complement and Coagulation Cascades, organism-specific biosystem; Complement and coagulation cascades, organism-specific biosystem; Complement and coagulation cascades, conserved biosystem; Complement cascade, organism-specific biosystem; Creation of C4 and C2 activators, organism-specific biosystem;
Function : calcium ion binding; peptidase activity; serine-type endopeptidase activity;

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For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.

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Q&As (5)

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Is C1S protein deficiency a rare condition? 10/07/2022

Yes, C1S protein deficiency is rare, but it is more common in patients with a family history of HAE.

What are the potential side effects or risks associated with C1S replacement therapy? 08/13/2022

Side effects can include infusion site reactions or hypersensitivity reactions, so treatment is typically administered under medical supervision.

How is C1S protein replacement therapy administered to patients with HAE? 10/02/2021

C1S protein replacement therapy is usually given intravenously, and the frequency of administration may vary depending on the patient's needs.

Can C1S protein be used in the treatment of conditions other than HAE? 01/09/2018

C1S replacement therapy is primarily used for HAE, but researchers are investigating its potential use in other complement-related disorders.

Are there any ongoing research efforts related to C1S protein in clinical applications? 11/20/2016

Yes, ongoing research aims to better understand the role of C1S in HAE and explore new treatment options, such as gene therapy.

Customer Reviews (3)

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Reviews
12/07/2018

    This level of sensitivity and specificity has streamlined my research and allowed for precise protein characterization.

    09/28/2018

      The protein bands detected were exceptionally distinct, enabling easy interpretation and accurate analysis of protein expression patterns.

      09/16/2018

        To summarize, the C1S protein is a highly recommended asset for various research endeavors, including ELISA, protein electron microscopy structure analysis, and Western blotting.

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