FCRL6 Research Reagents

FcRL6 was identified by its homology to other Fc receptor homologs and to FcγRI, although it retained some residues important for binding IgG, FcRL6-expressing cells were not detected with soluble or thermally aggregated human IgM or IgG binding. This suggests that the molecule is not an Fc receptor and the ligand for its ectodomain is undefined. The cytoplasmic tail of FcRL6 recruits SHP-2, suggesting that this protein functions in regulating certain aspects of cellular activation through ligand-induced cross-linking. SHP-2 has been shown to act as a negative regulator in the signaling pathways of several inhibitory receptors. However, SHP-2 also acts as a positive regulator in many growth factor receptor and cytokine receptor signaling pathways, such as promoting Ras-ERK activation, leading to proliferation and survival. The effect of FcRL6 recruitment of SHP-2 on NK cell and CD8+ T cell function remains to be further investigated. In addition to the defined canonical signaling motif, FcRL6 also contains a repetitive CxEVxC motif at the C-terminus of the protein. Although we have no precedent for finding this motif in other proteins, the repeated cysteine ​​and acidic residues are reminiscent of the Zn binding sites found in proteins containing zinc or ring fingers.

The following FCRL6 reagents supplied by CUSABIO are manufactured under a strict quality control system. Multiple applications have been validated and solid technical support is offered.