Additional Information:
inaccessionQ8BG84|express systemHEK293|product tagC-His|purity> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC|backgroundLAIR1 (leukocyte-associated Ig-like receptor-1, designated CD305) is an approximately 40 kDa type I transmembrane inhibitory glycoprotein belonging to the Ig superfamily.LAIR1 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.|molecular weightThe protein has a predicted MW of 14.6 kDa. Due to glycosylation, the protein migrates to 30-42 kDa based on Tris-Bis PAGE result.|available size100 g, 500 g|endotoxinLess than 1EU per g by the LAL method.|Mouse LAIR1/CD305 Protein 3937proteinSize and concentration100, 500g and lyophilizedFormLyophilizedStorage InstructionsValid for 12 months from date of receipt when stored at -80C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.Storage bufferShipped at ambient temperature.Purity> 95% as determined by Tris-Bis PAGEtarget relevanceLAIR1 (leukocyte-associated Ig-like receptor-1, designated CD305) is an approximately 40 kDa type I transmembrane inhibitory glycoprotein belonging to the Ig superfamily.LAIR1 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.Protein namesLeukocyte-associated immunoglobulin-like receptor 1 (LAIR-1) (mLAIR1) (CD antigen CD305)Gene namesLair1,Lair1Mass10090DaFunctionFunctions 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).Subellular locationCell membrane ; Single-pass type I membrane protein .TissuesExpressed in lymphoid organs and in cell lines of hemopoietic origin.StructureInteracts with SH2 domains of tyrosine-protein phosphatases PTPN6 and PTPN11. The interaction with PTPN6 is constitutive. Interacts with the SH2 domain of CSK. Binds with high affinity to extracellular matrix collagens, the interaction is functionally important (By similarity).Post-translational modificationPhosphorylation at Tyr-228 and Tyr-257 activates it. May be phosphorylated by LCK (By similarity).; N-glycosylated.DomainITTarget Relevance information above includes information from UniProt accession: Q8BG84The UniProt Consortium|