Human Plasma.
C4bp, C4BP, C4b-binding protein alpha chain, Proline-rich protein, PRP, C4BPA
Sterile filtered solution.
Greater than 90% as determined by SDS-PAGE.
C4BP Human produced in Human Plasma having a molecular mass of 540 kDa.
C4BP, structured like a flower, comprises alpha chains radiating from a central core. Disulfide bonds link these arms centrally, and their ends bind to C4b. Acting as a cofactor, C4BP facilitates Factor I in breaking down and permanently deactivating C4b. It regulates complement activation in both the classical and lectin pathways. By binding to C4b, C4BP accelerates the separation of C2a from the C3/C5 convertase (C4b,C2a), effectively inactivating the central enzyme of both pathways. Research indicates that on surfaces densely populated with C4b, C4BP can bind up to four C4b molecules concurrently.
Human-derived C4BP produced in Human Plasma with a molecular mass of 540 kDa.
A sterile solution that has been filtered.
The C4BP solution, at a concentration of 1mg/ml, is prepared in a PBS buffer with a pH of 7.2.
C4BP Human remains stable at a temperature of 4°C for a period of 2-4 weeks, provided the entire vial is utilized within this timeframe. For extended storage, it is recommended to freeze the solution below -20°C. The addition of a carrier protein (0.1% HSA or BSA) is advisable for long-term storage. It is crucial to avoid subjecting the solution to repeated cycles of freezing and thawing.
Purity exceeds 90% as determined by SDS-PAGE analysis.
Plasma samples from each donor have undergone rigorous testing and are confirmed to be negative for antibodies against HIV-1, HIV-2, HCV, HTLV-I & II, STS, and HBSAG.
C4bp, C4BP, C4b-binding protein alpha chain, Proline-rich protein, PRP, C4BPA
Human Plasma.
C4BP is a large glycoprotein with a molecular weight of approximately 500 kDa. It has an octopus-like structure, consisting of a central stalk and multiple branching chains. The main form of C4BP in human blood is composed of seven identical alpha-chains and one unique beta-chain . The beta-chain binds to anticoagulant, vitamin K-dependent protein S .
The genes coding for the alpha-chain (C4BPA) and beta-chain (C4BPB) of C4BP are located on the long arm of chromosome 1, within the regulators of complement activation (RCA) gene cluster . This cluster also contains other complement inhibitors, highlighting the coordinated regulation of the complement system.
C4BP acts as an inhibitor in the complement system, particularly in the classical and lectin pathways. It binds to complement components C4b and C3b, accelerating the decay of C3-convertase and serving as a cofactor for serine protease factor I, which cleaves C4b and C3b . This action prevents the over-activation of the complement system, protecting host cells from unintended damage.
Additionally, C4BP binds to apoptotic and necrotic cells, as well as DNA, aiding in the cleanup process after cellular injury . This interaction is mediated by the Gla domain of protein S and does not interfere with C4BP’s ability to inhibit complement.
C4BP has been studied for its potential as a biomarker in various clinical settings. For instance, elevated levels of C4BP alpha-chain (C4BPα) have been associated with resistance to the antiplatelet drug clopidogrel in patients with coronary artery disease . This suggests that measuring plasma C4BPα levels could help predict clopidogrel resistance and guide personalized treatment strategies.