Recombinant TIMD4 protein (His tag)

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Recombinant Human TIMD-4 Fragment (aa 25-136) is a high-purity protein designed for studying the Ig-like V-type domain's role in immune regulation. This fragment enables targeted investigation of TIMD-4's functions in phosphatidylserine recognition, T-cell activation modulation, and apoptotic cell clearance.

T-cell immunoglobulin and mucin domain-containing protein 4 (TIMD-4) is a membrane-bound phosphatidylserine receptor with dual roles in immune response regulation. It modulates T-cell activation by suppressing naive T-cells while enhancing activated T-cell proliferation through AKT1 and ERK1/2 signaling pathways. TIMD-4 facilitates efferocytosis by binding phosphatidylserine on apoptotic cells, working cooperatively with engulfment receptors like MERTK. Additionally, it promotes autophagy by suppressing NLRP3 inflammasome activity via the LKB1/PRKAA1 pathway. The protein localizes to the cell membrane as a single-pass type I membrane protein and is also found in secreted exosomes, where it participates in exosome-mediated HIV-1 trafficking. This recombinant fragment specifically contains the functional Ig-like V-type domain critical for these interactions.