LAIR1 Protein, Mouse (HEK293, Fc)

The LAIR1 protein functions as an inhibitory receptor, negatively regulating NK cells, B-cells, and T-cells. Activated by tyrosine phosphorylation, LAIR1 recruits PTPN6 and PTPN11, exerting downstream inhibitory effects. It diminishes intracellular calcium increase triggered by B-cell receptor ligation and independently modulates cytokine production in CD4+ T-cells, down-regulating IL2 and IFNG while inducing TGF-beta secretion. LAIR1 also regulates IgG and IgE production, inhibits proliferation, induces apoptosis in myeloid leukemia cells, prevents NF-kappa-B p65 subunit translocation, and inhibits I-kappa-B alpha phosphorylation. LAIR1 associates with SH2 domains of PTPN6 and PTPN11 and binds with high affinity to extracellular matrix collagens, signifying a functionally significant interaction. LAIR1 Protein, Mouse (HEK293, Fc) is the recombinant mouse-derived LAIR1 protein, expressed by HEK293 , with C-hFc labeled tag. The total length of LAIR1 Protein, Mouse (HEK293, Fc) is 112 a.a., with molecular weight of 49-53 kDa.

The LAIR1 protein operates as an inhibitory receptor, constitutively exerting a negative regulatory influence on the cytolytic function of natural killer (NK) cells, B-cells, and T-cells. Upon activation through tyrosine phosphorylation, LAIR1 recruits and activates phosphatases PTPN6 and PTPN11, leading to downstream inhibitory effects. Notably, it diminishes the increase in intracellular calcium triggered by B-cell receptor ligation. Beyond its role with SH2-containing phosphatases, LAIR1 independently modulates cytokine production in CD4+ T-cells, down-regulating IL2 and IFNG while inducing the secretion of transforming growth factor beta. It further regulates IgG and IgE production in B-cells, as well as the secretion of IL8, IL10, and TNF. LAIR1's impact extends to inhibiting proliferation, inducing apoptosis in myeloid leukemia cell lines, preventing nuclear translocation of NF-kappa-B p65 subunit/RELA, and inhibiting the phosphorylation of I-kappa-B alpha/CHUK in these cells. Moreover, it hinders the differentiation of peripheral blood precursors into dendritic cells. Interaction-wise, LAIR1 associates with the SH2 domains of tyrosine-protein phosphatases PTPN6 and PTPN11 constitutively and binds with high affinity to extracellular matrix collagens, a functionally significant interaction.

Mouse

HEK293

C-hFc

Q8BG84-6 (Q22-S133)

52855  [NCBI]

49-53 kDa

Greater than 95% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.