Recombinant Human C4 protein is a Human Full Length protein, in the 1454 to 1744 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
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Non-enzymatic component of C3 and C5 convertases and thus essential for the propagation of the classical complement pathway. Covalently binds to immunoglobulins and immune complexes and enhances the solubilization of immune aggregates and the clearance of IC through CR1 on erythrocytes. C4A isotype is responsible for effective binding to form amide bonds with immune aggregates or protein antigens, while C4B isotype catalyzes the transacylation of the thioester carbonyl group to form ester bonds with carbohydrate antigens. Derived from proteolytic degradation of complement C4, C4a anaphylatoxin is a mediator of local inflammatory process. It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes.
CO4, CPAMD2, C4A, Complement C4-A, Acidic complement C4, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 2
Recombinant Human C4 protein is a Human Full Length protein, in the 1454 to 1744 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
pH: 8
Constituents: 0.32% Tris HCl
The final product was refolded using unique “temperature shift inclusion body refolding” technology and chromatographically purified.
Non-enzymatic component of C3 and C5 convertases and thus essential for the propagation of the classical complement pathway. Covalently binds to immunoglobulins and immune complexes and enhances the solubilization of immune aggregates and the clearance of IC through CR1 on erythrocytes. C4A isotype is responsible for effective binding to form amide bonds with immune aggregates or protein antigens, while C4B isotype catalyzes the transacylation of the thioester carbonyl group to form ester bonds with carbohydrate antigens.
Prior to secretion, the single-chain precursor is enzymatically cleaved to yield non-identical chains alpha, beta and gamma. During activation, the alpha chain is cleaved by C1 into C4a and C4b, and C4b stays linked to the beta and gamma chains. Further degradation of C4b by C1 into the inactive fragments C4c and C4d blocks the generation of C3 convertase. The proteolytic cleavages often are incomplete so that many structural forms can be found in plasma.
Complement component 4 (C4) is a significant protein in the complement system also known as C4 complement. C4 has a molecular mass of approximately 206 kDa and mainly expresses in the liver. It is present in the blood plasma. C4 plays an important role in the immunological response and activates classical and lectin complement pathways. It serves a mechanical function by binding to pathogen surfaces and facilitating the cleavage that leads to the downstream activation of the complement cascade. There's a C4 ELISA test that allows for quantifying C4 levels in serum which is important for clinical diagnostics.
Complement C4 participates in the immune defense by marking pathogens for destruction and enhancing phagocytosis. C4 is a part of a complex with other complement proteins like C3 and C1 to initiate the formation of the C3 convertase enzyme. This action amplifies the immune response leading to the clearance of microorganisms and apoptotic cells. C4 also plays a role in regulating the inflammation process maintaining homeostasis in the immune system.
C4 fits into the complement activation pathway specifically the classical and lectin pathways. These pathways are important for innate immunity and connect with components like complement C3 and complement C1. Through the classical pathway C4 gets activated after binding to antibodies that have recognized antigens leading to a chain reaction that strengthens the immune response. The lectin pathway also requires C4 activation through different stimuli solidifying C4's central role in immune system signaling networks.
Abnormal C4 activity associates with autoimmune diseases like systemic lupus erythematosus (SLE) and rheumatoid arthritis. Low levels of complement C4 in serum can indicate these autoimmune conditions where the immune system mistakenly attacks its own tissues. C4 also connects to other proteins like complement component C1q in the context of SLE. C4 deficiencies or abnormalities may contribute to the development or exacerbation of these diseases highlighting its importance in disease pathogenesis and highlighting its value as a target for diagnostic tests such as C4 ELISA or serum complement tests.
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