C1S Human
Human Plasma.
Complement C1s subcomponent, C1 esterase, Complement component 1 subcomponent s, C1S.
Sterile Filtered solution.
Greater than 95.0% as determined by SDS-PAGE.
Description
Human Complement C1s produced in Human plasma having a molecular mass of 86 kDa.
Product Specs
The complement C1s enzyme, a subunit of the C1 complex, is the active form of the C1s proenzyme. This proenzyme is the initial complement component in the complement's classical pathway. It remains inactive as a zymogen until the C1 complex is activated. The C1 complex itself is a calcium-dependent structure held together by non-covalent bonds and comprises one C1q molecule, two C1r molecules, and two C1s molecules. When multiple arms of the complex bind to immune complexes, it triggers the generation of two proteases. These proteases, facilitated by the C1r proteins, then cleave and activate the two C1s protease zymogens within the complex. This activation process results in the cleavage of the C1s proenzyme into two C1s chains, with molecular weights of 58,000 and 28,000 Daltons.
Human Complement C1s, derived from human plasma, has a molecular weight of 86 kDa.
Presented as a sterile, filtered solution.
The protein solution is buffered with PBS.
Human C1s maintains stability at 4°C for a period of 2 to 4 weeks, provided the entire vial is utilized within that timeframe. For storage exceeding this period, freezing at temperatures below -20°C is recommended. To enhance long-term storage stability, consider adding a carrier protein such as 0.1% HSA or BSA. It is crucial to minimize exposure to repeated freeze-thaw cycles.
Purity exceeds 95.0% as determined by SDS-PAGE analysis.
Plasma samples from each donor undergo rigorous testing to ensure they are negative for antibodies against HIV-1, HIV-2, HCV, HTLV-I and II, syphilis (STS), and hepatitis B surface antigen (HBsAG).
Complement C1s subcomponent, C1 esterase, Complement component 1 subcomponent s, C1S.
Human Plasma.
Product Science Overview
Complement C1s is a subcomponent of the C1 complex, which also includes C1q and C1r. The C1 complex is the first component of the classical pathway of the complement system. C1s is initially synthesized as an inactive zymogen and becomes activated through cleavage by C1r . Once activated, C1s cleaves complement components C4 and C2, leading to the formation of the C3 convertase, which is essential for the subsequent steps in the complement cascade .
The activation of C1s is a critical step in the classical pathway, which is typically triggered by the binding of antibodies to antigens. This pathway plays a vital role in immune responses, including cell lysis, opsonization, degranulation of mast cells and basophils, activation of B lymphocytes, and clearance of immune complexes and apoptotic cells .
Deficiencies or dysregulations in C1s can lead to various diseases. For instance, C1s deficiency is associated with early-onset systemic lupus erythematosus and increased susceptibility to bacterial infections . Additionally, gain-of-function variants of C1s can lead to periodontal Ehlers-Danlos syndrome . Due to its involvement in various pathological conditions, C1s is being explored as a diagnostic marker and therapeutic target for diseases such as autoimmune disorders and cancer .
Recent research has focused on developing small molecules, peptides, and monoclonal antibodies targeting C1s. Some of these therapeutic agents are currently undergoing clinical trials, and one monoclonal antibody has been approved by the US FDA for the treatment of cold agglutinin disease, an autoimmune hemolytic anemia .
