Recombinant Human TIM-4 (C-6His)

Recombinant Human T-cell Immunoglobulin And Mucin Domain-containing Protein 4 is produced by our Mammalian expression system and the target gene encoding Glu25-Leu315 is expressed with a 6His tag at the C-terminus. T-cell Immunoglobulin and Mucin Domain-containing Protein 4(TIM-4) belongs to the immunoglobulin superfamily, is a member of the TIM family of immune regulating proteins. TIMs are type I transmembrane proteins with one Ig-like V domain and one Ser/Thr-rich mucin domain. Structurally, TIM-4 is distinguished from other TIMs by the presence of an RGD motif in its Ig domain and the lack of a site for tyrosine phosphorylation in its cytoplasmic tail. The mucin domain in TIM-4 is larger than in TIM-1 or TIM-3. TIM-4 is expressed by macrophages and mature dendritic cells but not by lymphocytes. it is Involved in regulating T-cell proliferation and lymphotoxin signaling.The interaction of TIM-4 with TIM-1 induces costimulatory and hyperproliferative signals in T cells. TIM-4 binds specifically to TIM-1 which is also the cellular receptor for the hepatitis A virus, and has been implicated in the development of asthma. Protein Function: Phosphatidylserine receptor that plays different role in immune response including phagocytosis of apoptotic cells and T-cell regulation. Controls T-cell activation in a bimodal fashion, decreasing the activation of naive T-cells by inducing cell cycle arrest, while increasing proliferation of activated T-cells by activating AKT1 and ERK1/2 phosphorylations and subsequent signaling pathways (By similarity). Also plays a role in efferocytosis which is the process by which apoptotic cells are removed by phagocytic cells (PubMed:32703939, PubMed:34067457). Mechanistically, promotes the engulfment of apoptotic cells or exogenous particles by securing them to phagocytes through direct binding to phosphatidylserine present on apoptotic cells, while other engulfment receptors such as MERTK efficiently recognize apoptotic cells and mediate their ingestion (PubMed:32640697). Additionally, promotes autophagy process by suppressing NLRP3 inflammasome activity via activation of LKB1/PRKAA1 pathway in a phosphatidylserine-dependent mechanism (By similarity) , (Microbial infection) Plays a positive role in exosome-mediated trafficking of HIV-1 virus and its entry into immune cells [The Uniprot Consortium]