Leukocyte-Associated Immunoglobulin-Like Receptor 1 (LAIR1) Rat Recombinant Protein

Function: Functions as an inhibitory receptor that plays a constitutive negative regulatory role on cytolytic function of natural killer (NK) cells, B-cells and T-cells. Activation by Tyr phosphorylation results in recruitment and activation of the phosphatases PTPN6 and PTPN11. It also reduces the increase of intracellular calcium evoked by B-cell receptor ligation. May also play its inhibitory role independently of SH2-containing phosphatases. Modulates cytokine production in CD4+ T-cells, down-regulating IL2 and IFNG production while inducing secretion of transforming growth factor beta. Down-regulates also IgG and IgE production in B-cells as well as IL8, IL10 and TNF secretion. Inhibits proliferation and induces apoptosis in myeloid leukemia cell lines as well as prevents nuclear translocation of NF-kappa-B p65 subunit/RELA and phosphorylation of I-kappa-B alpha/CHUK in these cells. Inhibits the differentiation of peripheral blood precursors towards dendritic cells

By similarity.

Subunit structure: Interacts with SH2 domains of tyrosine-protein phosphatases PTPN6 and PTPN11. The interaction with PTPN6 is constitutive. Interacts with the SH2 domain of CSK

By similarity.

Subcellular location: Membrane; Single-pass membrane protein

Potential.

Tissue specificity: Expressed in lymphoid and non-lymphoid organs. Ref.1

Domain: ITIM (immunoreceptor tyrosine-based inhibitor motif) motif is a cytoplasmic motif present in 2 copies in the intracellular part of LAIR1. When phosphorylated, ITIM motif can bind the SH2 domain of several SH2-containing phosphatases, leading to down-regulation of cell activation. Ref.1

Post-translational modification: Phosphorylation at Tyr-227 and Tyr-257 activates it. May be phosphorylated by LCK

By similarity.N-glycosylated

By similarity.

Sequence similarities: Contains 1 Ig-like C2-type (immunoglobulin-like) domain.