Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,3- or alpha-2,6-linked sialic acid (By similarity). The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, seems to act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules . Involved in negative regulation of B-cell antigen receptor signaling. The inhibition of B cell activation is dependent on PTPN6/SHP-1 (By similarity). In association with CD24 may be involved in the selective suppression of the immune response to danger-associated molecular patterns (DAMPs) such as HMGB1, HSP70 and HSP90 (By similarity). In association with CD24 may regulate the immune repsonse of natural killer (NK) cells . Plays a role in the control of autoimmunity (By similarity). During initiation of adaptive immune responses by CD8-alpha(+) dendritic cells inhibits cross-presentation by impairing the formation of MHC class I-peptide complexes. The function seems to implicate recruitment of PTPN6/SHP-1, which dephosphorylates NCF1 of the NADPH oxidase complex consequently promoting phagosomal acidification (By similarity). .

Q96LC7

Sialic acid-binding Ig-like lectin 10 (Siglec-10) (Siglec-like protein 2),SIGLEC10 SLG2 UNQ477/PRO940,SIGLEC10, Siglec-10, Sialic acid-binding Ig-like lectin 10, Siglec-like protein 2, SLG2

Human

FC

FC 1:50-1:200

77kD

APC

Mouse

Monoclonal

SA256

IgG1, kappa

0.01M PBS, pH 7.4, 0.2% BSA, 0.05% Proclin 300.

0.5 mg/ml

Store at 4℃ for 12 months. Protect from light. Do not freeze.