|Protein Name||Species||Fusion Tag||Catalog Code|
|FcγRI||Human||Glutathione S Transferase (GST)||P131D|
|FcγRIIa, H131||Human||Glutathione S Transferase (GST)||P501D|
|FcγRIIa, R131||Human||Glutathione S Transferase (GST)||P133D|
|FcγRIIb||Human||Glutathione S Transferase (GST)||P134D|
|FcγRIII, F158||Human||Glutathione S Transferase (GST)||P135D|
|FcγRIII, V158||Human||Glutathione S Transferase (GST)||P502D|
|FcγRI||Mouse||Glutathione S Transferase (GST)||M131D|
|FcγRIIb||Mouse||Glutathione S Transferase (GST)||M134D|
|FcγRIII||Mouse||Glutathione S Transferase (GST)||M135D|
|FcγRIV||Mouse||Glutathione S Transferase (GST)||M511D|
Human FcγR first quarter of antibodies contain variable regions capable of recognizing a great variety of antigens. The second half of antibodies contains the Fc domain with limited variation and is critical for bringing together the bound-antigen with cellular effector functions. The IgG Fc receptors which mediate the effector functions are expressing on leukocytes and are composed of three major classes: FcγR1 (CD64), FcγRII (CD32) and FcγRIII (CD16). In human, the latter two contain subgroups: FcγRIIA and FcγRIIB, as well as FcγRIIIA and FcγRIIIB. Structurally, each FcγR contains the α chain which is a member of Ig superfamily and is directly interacting with the Ig Fc.
While Human FcγRs share same name and CD as mouse FcγRs, they are however quite different in the binding specificities toward each IgG subclasses. Together, there are four mouse FcγRs: the FcγRI, FcγRIIB, FcγRIII, and FcγRIV, with FcγRIIB as the only inhibitory receptor and is the only one carries the intrinsic ITIM motif just like the human FcγRIIB.