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Siglec-10 is immune system-restricted and highly expressed in peripheral blood leukocytes. Siglec-10 preferably binds to α-2,3- or α-2,6-linked sialic acid (similarity). Siglec10 is involved in the negative regulation of B cell antigen receptor signal transduction. The inhibition of B cell activation depends on PTPN6/SHP-1 (by similarity). The binding of Siglec10 to CD24 may be involved in the selective suppression of the immune response (by similarity) to risk-related molecular patterns (DAMPs) (such as HMGB1, HSP70 and HSP90). The combination of Siglec10 and CD24 may regulate the immune response of natural killer (NK) cells. Play a role in controlling autoimmunity (by similarity). In the process of initiating an adaptive immune response by CD8-α+ dendritic cells, cross-presentation is inhibited by weakening the formation of MHC class I peptide complexes. The function seems to imply the recruitment of PTPN6/SHP-1, which dephosphorylates NCF1 of the NADPH oxidase complex, thereby promoting phagosome acidification (by similarity).

Siglec-10 is immune system-restricted and highly expressed in peripheral blood leukocytes. Siglec-10 preferably binds to α-2,3- or α-2,6-linked sialic acid (similarity). Siglec10 is involved in the negative regulation of B cell antigen receptor signal transduction. The inhibition of B cell activation depends on PTPN6/SHP-1 (by similarity). The binding of Siglec10 to CD24 may be involved in the selective suppression of the immune response (by similarity) to risk-related molecular patterns (DAMPs) (such as HMGB1, HSP70 and HSP90). The combination of Siglec10 and CD24 may regulate the immune response of natural killer (NK) cells. Play a role in controlling autoimmunity (by similarity). In the process of initiating an adaptive immune response by CD8-α+ dendritic cells, cross-presentation is inhibited by weakening the formation of MHC class I peptide complexes. The function seems to imply the recruitment of PTPN6/SHP-1, which dephosphorylates NCF1 of the NADPH oxidase complex, thereby promoting phagosome acidification (by similarity).

Siglec-15 preferentially recognizes the Neu5Acalpha2-6GalNAcalpha- structure. Siglec-15 associates with the activating adaptor proteins DNAX activation protein (DAP)12 and DAP10 via its lysine residue in the transmembrane domain. Siglec-15 is the second human Siglec identified to have an activating signaling potential; unlike Siglec-14, however, it does not have an inhibitory counterpart.

Siglec-15 preferentially recognizes the Neu5Acalpha2-6GalNAcalpha- structure. Siglec-15 associates with the activating adaptor proteins DNAX activation protein (DAP)12 and DAP10 via its lysine residue in the transmembrane domain. Siglec-15 is the second human Siglec identified to have an activating signaling potential; unlike Siglec-14, however, it does not have an inhibitory counterpart.

Siglec-15 preferentially recognizes the Neu5Acalpha2-6GalNAcalpha- structure. Siglec-15 associates with the activating adaptor proteins DNAX activation protein (DAP)12 and DAP10 via its lysine residue in the transmembrane domain. Siglec-15 is the second human Siglec identified to have an activating signaling potential; unlike Siglec-14, however, it does not have an inhibitory counterpart.

CD22, or cluster of differentiation-22, is a molecule belonging to the SIGLEC family of lectins. It is found on the surface of mature B cells and to a lesser extent on some immature B cells. CD22 a member of the immunoglobulin superfamily. CD22 functions as an inhibitory receptor for B cell receptor (BCR) signaling. It is also involved in the B cell trafficking to Peyer’s patches in mice.

Interleukin-6 Receptor (IL-6R) is a single trans-membrane protein that is the receptor for Interleukin-6 (IL-6). IL-6R forms a hexameric complex upon binding 2 molecules of IL-6 and two molecules of glycoprotein 130 (gp130) which activates intracellular JAK/STAT pathways. Although the normal form of IL-6R is the membrane-bound 80 kDa subunit, a soluble form of IL-6R (sIL-6R) can be generated physiologically by limited proteolysis or alternative splicing. sIL-6R binds to both IL-6 and gp130 generating intracellular signaling. In the immune system, sIL-6R is produced by both naïve and memory CD4 T-cells and strongly augments IL-6 ligand’s induction of Th-17 cells.

Interleukin-6 Receptor (IL-6R) is a single trans-membrane protein that is the receptor for Interleukin-6 (IL-6). IL-6R forms a hexameric complex upon binding 2 molecules of IL-6 and two molecules of glycoprotein 130 (gp130) which activates intracellular JAK/STAT pathways. Although the normal form of IL-6R is the membrane-bound 80 kDa subunit, a soluble form of IL-6R (sIL-6R) can be generated physiologically by limited proteolysis or alternative splicing. sIL-6R binds to both IL-6 and gp130 generating intracellular signaling. In the immune system, sIL-6R is produced by both naïve and memory CD4 T-cells and strongly augments IL-6 ligand’s induction of Th-17 cells.

Interleukin-6 Receptor (IL-6R) is a single trans-membrane protein that is the receptor for Interleukin-6 (IL-6). IL-6R forms a hexameric complex upon binding 2 molecules of IL-6 and two molecules of glycoprotein 130 (gp130) which activates intracellular JAK/STAT pathways. Although the normal form of IL-6R is the membrane-bound 80 kDa subunit, a soluble form of IL-6R (sIL-6R) can be generated physiologically by limited proteolysis or alternative splicing. sIL-6R binds to both IL-6 and gp130 generating intracellular signaling. In the immune system, sIL-6R is produced by both naïve and memory CD4 T-cells and strongly augments IL-6 ligand’s induction of Th-17 cells.