Recombinant Human TIM‑1/KIM‑1/HAVCR Fc Chimera (Catalog #9319-TM) inhibits anti-CD3-induced proliferation of PHA-activated human Tcells. The ED50 for this effect is 0.6-3.6 μg/mL.
T cell immunoglobulin and mucin domain 1 (TIM-1), also known as KIM-1 and HAVcr1, is a member of the TIM family which is involved in the regulation of innate and adaptive immune responses (1). TIM-1 is a type I transmembrane protein that contains an N-terminal immunoglobulin-like domain, a mucin domain with O- and N-linked carbohydrates, a transmembrane segment, and a cytoplasmic signaling domain (2). Multiple TIM-1 variants can be produced due to polymorphisms or alternative splicing resulting in deletions in the mucin domain. Within the extracellular domain, human TIM-1 shares 41% aa sequence identity with mouse and rat TIM-1. TIM-1 is expressed on splenic B cells, IL-10+ regulatory B cells, CD4+ T cells, mast cells, invariant NKT (iNKT) cells, dendritic cells, kidney epithelium and a broad range of mucosal epithelium (1, 3-5). It is upregulated on activated Th2 cells, after dendritic cell maturation, and on kidney tubular epithelial cells after injury (6-9). Metalloproteinase-mediated cleavage of TIM-1 at the membrane-proximal region results in the release of a soluble form of TIM-1 which is detectable in the urine and in circulation (10). TIM-1 serves as a receptor for phosphatidylserine, LMIR5/CD300b, TIM-1 (homophilic), TIM-4, IgA, and the glycoproteins of a number of enveloped viruses (2, 11-16). Its interaction with phosphatidylserine enables TIM-1 to mediate the phagocytosis of apoptotic cells (12, 13) and iNKT cell activation (17). TIM-1 binding induces the activation of LMIR5-expressing myeloid cells, contributing to tissue homeostasis as well as damage following kidney injury (14). TIM-1 ligation co-stimulates T cell activation and enhances Th2 cytokine production (7, 15). In humans, TIM-1 serves as a cellular entry receptor for various viruses, including hepatitis A virus, Ebolavirus and Marburgvirus (2, 11).
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