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Human C4b-Binding Protein
Native whole molecule
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Proteins Synonyms: C4bBP, C4BP Source: Human Plasma Purity: ≥ 95% by SDS-PAGE. Free of Protein S Physical State: Lyophilized from 10 mM Tris pH 7.4, 100 mM NaCl, 0.05% NaN3 Free of Protein S Manufacturer: |
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Athens Research & Technology
Produktdetails
Synonyms
C4bBP, C4BP
Description of Human C4b-Binding Protein
C4b-binding protein (C4BP) is a glycoprotein synthesized in the liver, circulating at ~200 µg/mL in plasma, and functioning as a key inhibitor of the classical and lectin complement pathways. Its octopus-like structure comprises seven α-chains (70 kDa each) and one β-chain (40 kDa) in the predominant isoform (α7β1), though β-deficient isoforms (α7β0, α6β1) exist, with α7β0 upregulated during acute inflammation. The α-chain complement control protein (CCP) domains 1–3 mediate binding to C4b and heparin, while the β-chain interacts with protein S, forming a calcium-dependent complex critical for anticoagulant activity. C4BP accelerates decay of C3/C5 convertases and acts as a cofactor for factor I in proteolytic cleavage of C4b/C3b, preventing excessive complement activation. Clinically, C4BP is implicated in neurodegenerative, autoimmune, and oncological disorders. In Alzheimer’s disease, C4BP binds amyloid-β plaques and apoptotic neurons, mitigating neuroinflammation by limiting complement-mediated damage. Elevated plasma C4BP correlates with psoriasis severity, where it modulates alternative pathway activation in skin lesions. Therapeutic administration of C4BP in murine rheumatoid arthritis models reduced joint inflammation by inhibiting classical and alternative pathways. Paradoxically, reduced C4BPA expression in breast and lung cancers associates with poor prognosis, suggesting tumor-suppressive roles via immune regulation.
Source
Human plasma non-reactive for HBsAG, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests
Storage
For long term, store Human C4b-Binding Protein at -20°C.
Applications
Complement System, Inflammation, Antimicrobial, Autoimmune, Cancer, Alzheimer's.
Citations/Publications
Alves, L. A., et al., (2020), 'PepO is a target of the two-component systems VicRK and CovR required for systemic virulence of Streptococcus mutans', VIRULENCE., 11(1): pp 521–536. Available at: https://doi.org/10.1080/21505594.2020.1767377
Singh, S. K., et al., (2017), 'Functional Transformation of C-reactive Protein by Hydrogen Peroxide', THE JOURNAL OF BIOLOGICAL CHEMISTRY, 292(8): pp. 3129–3136. Available at:DOI 10.1074/jbc.M116.773176.
Shipped with ice packs
Gel Scan of Human C4b-Binding Protein
| Fig. 1: SDS-PAGE Gel |
Usage: For research use only. Not for use in diagnostic or therapeutic procedures. Not for human use.
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Payment Methods
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