Human TLT-1/TREML1 Protein 3169

Additional Information:
accession XP_016866312|express systemHEK293|product tagC-hFc|purity> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC|backgroundTriggering receptor expressed on myeloid cells (TREM)-like transcript-1 (TLT-1) is an immunoreceptor tyrosine-based inhibitory motif (ITIM)-baring TREM family protein. Triggering receptor expressed on myeloid cells (TREM) like transcript-1 (TLT-1) is a membrane protein receptor found in alpha-granules of platelets and megakaryocytes.|molecular weightThe protein has a predicted MW of 42.60 kDa. Due to glycosylation, the protein migrates to 50-60 kDa based on Tris-Bis PAGE result.|available size100 g, 500 g|endotoxinLess than 1EU per g by the LAL method.|Human TLT-1/TREML1 Protein 3169proteinSize 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 relevanceTriggering receptor expressed on myeloid cells (TREM)-like transcript-1 (TLT-1) is an immunoreceptor tyrosine-based inhibitory motif (ITIM)-baring TREM family protein. Triggering receptor expressed on myeloid cells (TREM) like transcript-1 (TLT-1) is a membrane protein receptor found in alpha-granules of platelets and megakaryocytes.Protein namesTrem-like transcript 1 protein (TLT-1) (Triggering receptor expressed on myeloid cells-like protein 1)Mass32679DaFunctionCell surface receptor that may play a role in the innate and adaptive immune response. ECO:0000269.Subellular locationCell membrane ECO:0000269; Single-pass type I membrane protein PubMed:15100151. Cytoplasm ECO:0000269. Note=Sequestered in cytoplasmic vesicles in resting platelets (PubMed:15100151). Transported to the cell surface after stimulation by thrombin (PubMed:15100151). Soluble fragments can be released into the serum by proteolysis (PubMed:16505478).TissuesDetected in platelets, monocytic leukemia and in T-cell leukemia. PubMed:15128762, ECO:0000269.StructureWhen phosphorylated, interacts with PTPN6 (By similarity). When phosphorylated, interacts with PTPN11. PubMed:15128762.Post-translational modificationPhosphorylated on tyrosine residues. ECO:0000269.Target Relevance information above includes information from UniProt accession: Q86YW5The UniProt Consortium|