|Calculated MW||26722 Da|
|Other Names||Complement C1q subcomponent subunit B, C1QB|
|Target/Specificity||A synthetic peptide corresponding to residues on human C1q (subunit B) was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||C1q Antibody (subunit B) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes.|
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Provided below are standard protocols that you may find useful for product applications.
The complement component C1 is a protein complex that consists of six subunits of C1q. Each C1q subunit of the complex is known to bind to immune complexes, which often are deposited in the basement membrane. C1q is a versatile recognition protein that triggers activation of the classical pathway of complement, where the first step involves the binding of the globular domain of Clq to the Fc regions of aggregated IgG or IgM. The C1q globular domain is a heterotrimer of the C-terminal halves of one A, one B, and one C chain, held together mainly by non-polar interactions, with a Ca2+ ion bound at the top. A modular organization has been suggested of the globular domain, consistent with the view that A, B, and C chains are functionally autonomous modules and have distinct and differential ligand-binding properties (1-3).
1. J F Bohnsack, et al. Proc Natl Acad Sci 82(11):3824-3828, 1985
2. Gaboriaud C, et al. J Biol Chem. 278(47):46974-82, 2003
3. KOJOUHAROVA M S, et al. The Journal of immunology 172(7), 4351-4358, 2004
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