Recombinant Human C4 protein is a Human Full Length protein, in the 1454 to 1744 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.
View Alternative Names
CO4, CPAMD2, C4A, Complement C4-A, Acidic complement C4, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 2
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
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.
Pathways
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.
Specifications
Form
Liquid
Additional notes
The final product was refolded using unique “temperature shift inclusion body refolding” technology and chromatographically purified.
General info
Function
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.
Post-translational modifications
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.. N- and O-glycosylated. O-glycosylated with a core 1 or possibly core 8 glycan.
Target data
Complementary Products
Product promise
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