PRODUCT NUMBER:

MW: ~ 570,000 Da (whole molecule)
~ 70,000-75,000 Da (alpha chains)
~ 40,000-45,000 Da (beta chain)
Extinction Coefficient: 1.4

Lyophilized from 10 mM Tris pH 7.4, 100 mM NaCl, 0.05% NaN3
Free of Protein S

Storage: -20°C

Buy Purified C4b Binding Protein, Free of Protein S, Human Plasma.
Bulk Qty Available.

C4b-binding protein is a regulatory protein of the Complement Cascade that possesses decay-accelerating activity. Circulating in plasma, it aids in the control of fluid-phase and surface-associated activation of C3 and C5 and serves as a cofactor to Factor 1 in the proteolytic degradation of C4b.
There are three isoforms circulating in plasma; 7 alpha chains and 1 Beta chain, 6 alpha chains and 1 Beta chain, and 7 alpha chains without a Beta chain. The 7 alpha, 1 Beta form is the most abundant. All C4BP molecules that contain a Beta chain circulate in plasma in a high-affinity, calcium-dependent complex with vitamin K-dependent, anticoagulant Protein S.

C4b-binding protein has been investigated for its role in Alzheimer's Disease, Psoriasis, as well as autoimmune diseases including Rheumatoid Arthritis, and different types of Cancer.

Purity: >=95% by SDS-PAGE.

Prepared from plasma shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests.

Athens Research & Technology products are laboratory reagents and are not to be administered to humans or used for any drug purpose. For research or further manufacturing use only.

Product Citation:

Sanderson-Smith, Martina, David MP De Oliveira, Julien Guglielmini, David J. McMillan, Therese Vu, Jessica K. Holien, Anna Henningham et al. "A systematic and functional classification of Streptococcus pyogenes that serves as a new tool for molecular typing and vaccine development."Journal of Infectious Diseases?(2014): jiu260.

Sanjay K. Singh et al.
Functional transformation of C-reactive protein by hydrogen peroxide.
J Biol Chem. 2017 Feb 24;292(8):3129-3136. doi: 10.1074/jbc.M116.773176. Epub 2017 Jan 17.