Anti-Human gC1qR Monoclonal Antibody (clone 60.11), FITC, -100 µg (CAT#: CB-P226-K) Datasheet

Antibody

Monoclonal antibody 60.11 recognizes the cell membrane C1q binding molecule, which recognizes the spherical head of C1q. It is also found in plasma and extracellular matrix. This molecule is an abnormally acidic single-chain protein with an apparent molecular weight of 33 kDa. It is It does not have conventional sequence motifs compatible with the transmembrane segment, and there is no GPI-anchored common site; gC1q-R migrates as a single strand under both reducing and non-reducing conditions, but it exhibits low levels of gel filtration Under non-dissociation conditions, the formation of multimers may be a key process. Through this process, gC1q-R molecules can increase their affinity for multivalent ligands (such as C1q).
It has been shown that gC1q-R can inhibit complement activation by preventing the binding of C1q to antibodies, which indicates that the binding site of gC1q-R and the binding site of immune complexes that may exist on the spherical "head" of C1q are at the same position. gC1q-R can interact with several proteins related to coagulation, namely thrombin, prothrombin, heparin-bound form of vitronectin, ternary complex, vitronectin-thrombin-antithrombin, and high molecular weight Kininogen and Hageman factor. In addition to its role in the complement pathway, gC1q-R is also involved in the enhancement of Fc receptor and CR1-mediated phagocytosis, the procoagulant activity of platelets, and the effect on mast cells, eosinophils, neutrophils and fibroblasts Chemotactic activity of cells. gC1q-R is expressed in a variety of cells and can be used as a binding site for plasma and microbial proteins. Its antigenic sites may be recessive in suspension cells, but are exposed when the cells are fixed by a bifunctional crosslinker. Perhaps it is also expressed on the cell membrane as a tetramer. Therefore, cross-linking or activation can cause the assembly of the tetramer of gClq-R, and then a conformational change occurs in the molecule, thereby exposing the originally hidden epitope. A form of GC1q-R was also found inside the battery. It has been shown that intracellular gC1q-R binds to the cytoplasmic tail of α1B-adrenergic receptor and binds to PKCμ.
Monoclonal antibody 60.11 is directed against an epitope located within the NH2 terminal fragment of gClq-R (corresponding to residues 76-93). Clone 60.11 recognizes the putative Clq binding site and reacts with the mature form, but has poor or no reactivity with the truncated form, lacking residues 74-95. "