TREML1 is located in a gene cluster on chromosome 6 with the single Ig variable (IgV) domain activating receptors TREM1 and TREM2, but it has distinct structural and functional properties. TREML1 enhances calcium signaling in an SHP2 (PTPN11)-dependent manner. TLT1 has a calculated molecular mass of 33 kD. Unlike other TREM proteins, the IgV domain of TLT1 has no potential N-glycosylation sites. The transmembrane domain of TLT1 lacks charged residues, and the 127-amino acid cytoplasmic region has 2 tyr residues (Y245 and Y281), each in an ITIM.truncation results in a membrane-bound form of TLT1 lacking the ITIMs. RT-PCR analysis detected weak expression of TLT1 in monocyte, B-cell, and T-cell lines. TLT1 expression could be upregulated by mitogen stimulation.
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