This antibody has a functional binding affinity to erythrocytes of 8.7 x 107 M-1. The antigen is pronase and trypsin resistant and chymotrypsin sensitive. BRIC 216 recognises the consensus region 3 of the DAF molecule, which contains the functional site, and the antibody blocks the function of DAF
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Use at an assay dependent concentration. Predicted molecular weight: 41 kDa.
Use at an assay dependent concentration. ab170190-Mouse monoclonal IgG1, is suitable for use as an isotype control with this antibody.
Use at an assay dependent concentration.
This protein recognizes C4b and C3b fragments that condense with cell-surface hydroxyl or amino groups when nascent C4b and C3b are locally generated during C4 and c3 activation. Interaction of daf with cell-associated C4b and C3b polypeptides interferes with their ability to catalyze the conversion of C2 and factor B to enzymatically active C2a and Bb and thereby prevents the formation of C4b2a and C3bBb, the amplification convertases of the complement cascade.
Expressed on the plasma membranes of all cell types that are in intimate contact with plasma complement proteins. It is also found on the surfaces of epithelial cells lining extracellular compartments, and variants of the molecule are present in body fluids and in extracellular matrix.
Belongs to the receptors of complement activation (RCA) family. Contains 4 Sushi (CCP/SCR) domains.
The first Sushi domain (SCR1) is not necessary for function. SCR2 and SCR4 provide the proper conformation for the active site on SCR3.
The Ser/Thr-rich domain is heavily O-glycosylated.