Cynomolgus Siglec-3/CD33 Protein 2963

Additional Information:
accession XP_005590138|express systemHEK293|product tagC-His|purity> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC|backgroundSialic-acid-binding immunoglobulin-like lectin (Siglec) that plays a role in mediating cell-cell interactions and in maintaining immune cells in a resting state.They are sialoadhesin/CD169/Siglec-1, CD22/Siglec-2, CD33/Siglec-3, Myelin-Associated Glycoprotein (MAG/Siglec-4a) and Siglecs 5 to 11. To date, no Siglec has been shown to recognized any cell surface ligand other than sialic acids, suggesting that interactions with glycans containing this carbohydrate are important in mediating the biological functions of Siglecs.|molecular weightThe protein has a predicted MW of 26.83 kDa. Due to glycosylation, the protein migrates to 40-50 kDa based on Tris-Bis PAGE result.|available size100 g, 500 g|endotoxinLess than 1EU per g by the LAL method.|Cynomolgus Siglec-3/CD33 Protein 2963proteinSize 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 relevanceSialic-acid-binding immunoglobulin-like lectin (Siglec) that plays a role in mediating cell-cell interactions and in maintaining immune cells in a resting state.They are sialoadhesin/CD169/Siglec-1, CD22/Siglec-2, CD33/Siglec-3, Myelin-Associated Glycoprotein (MAG/Siglec-4a) and Siglecs 5 to 11. To date, no Siglec has been shown to recognized any cell surface ligand other than sialic acids, suggesting that interactions with glycans containing this carbohydrate are important in mediating the biological functions of Siglecs.Protein namesMyeloid cell surface antigen CD33 (Sialic acid-binding Ig-like lectin 3) (Siglec-3) (gp67) (CD antigen CD33)Gene namesCD33,CD33 SIGLEC3Protein familyImmunoglobulin superfamily, SIGLEC (sialic acid binding Ig-like lectin) familyMass9606DaFunctionSialic-acid-binding immunoglobulin-like lectin (Siglec) that plays a role in mediating cell-cell interactions and in maintaining immune cells in a resting state (PubMed:10611343, PubMed:11320212, PubMed:15597323). Preferentially recognizes and binds alpha-2,3- and more avidly alpha-2,6-linked sialic acid-bearing glycans (PubMed:7718872). Upon engagement of ligands such as C1q or syalylated glycoproteins, two immunoreceptor tyrosine-based inhibitory motifs (ITIMs) located in CD33 cytoplasmic tail are phosphorylated by Src-like kinases such as LCK (PubMed:10887109, PubMed:28325905). These phosphorylations provide docking sites for the recruitment and activation of protein-tyrosine phosphatases PTPN6/SHP-1 and PTPN11/SHP-2 (PubMed:10206955, PubMed:10556798, PubMed:10887109). In turn, these phosphatases regulate downstream pathways through dephosphorylation of signaling molecules (PubMed:10206955, PubMed:10887109). One of the repressive effect of CD33 on monocyte activation requires phosphoinositide 3-kinase/PI3K (PubMed:15597323).Subellular location[Isoform CD33M]: Cell membrane ; Single-pass type I membrane protein.; [Isoform CD33m]: Peroxisome. Note=CD33m isoform does not localize to cell surfaces but instead accumulates in peroxisomes.TissuesMonocytic/myeloid lineage cells. In the brain, CD33 is mainly expressed on microglial cells.StructureHomodimer; disulfide-linked (PubMed:10887109). Interacts with PTPN6/SHP-1 and PTPN11/SHP-2 upon phosphorylation (PubMed:10206955, PubMed:10556798). Interacts with C1qA (via C-terminus); this interaction activates CD33 inhibitory motifs (PubMed:28325905).Post-translational modificationGlycosylated. Glycosylation at Asn-100 is critical for regulating ligand recognition.; Phosphorylation of Tyr-340 is involved in binding to PTPN6 and PTPN11. Phosphorylation of Tyr-358 is involved in binding to PTPN6. LCK phosphorylates Tyr-340 efficiently and Tyr-358 to a lesser extent.DomainCoTarget Relevance information above includes information from UniProt accession: P20138The UniProt Consortium|