Description: TIMs are type I transmembrane glycoproteins with one Ig-like V-type domain and a Ser/Thr-rich mucin stalk. TIM-3 is expressed on the surface of effector T cel tonsil, lymph node or spleen. ls (CD4+Th1 and CD8+Tc1) but not on helper T cells (CD4+Th2 and CD8+Tc2). In chronic inflammation, autoimmune disorders, and some cancers, TIM-3 is upregulated on several other hematopoietic cell types. The Ig domain of TIM-3 interacts with a ligand on resting but not activated Th1 and Th2 cells. The glycosylated Ig domain of TIM-3 binds cell-associated galectin-9. This induces TIM-3 Tyr phosphorylation and pro-apoptotic signaling. TIM-3 functions as a negative regulator of Th1 cell activity. Its blockade results in increased IFN-gamma production, Th1 cell proliferation and cytotoxicity, regulatory T cell development, and increases in macrophage and neutrophil infiltration into sites of inflammation.

Description: TIMs are type I transmembrane glycoproteins with one Ig-like V-type domain and a Ser/Thr-rich mucin stalk. TIM-3 is expressed on the surface of effector T cel tonsil, lymph node or spleen. ls (CD4+Th1 and CD8+Tc1) but not on helper T cells (CD4+Th2 and CD8+Tc2). In chronic inflammation, autoimmune disorders, and some cancers, TIM-3 is upregulated on several other hematopoietic cell types. The Ig domain of TIM-3 interacts with a ligand on resting but not activated Th1 and Th2 cells. The glycosylated Ig domain of TIM-3 binds cell-associated galectin-9. This induces TIM-3 Tyr phosphorylation and pro-apoptotic signaling. TIM-3 functions as a negative regulator of Th1 cell activity. Its blockade results in increased IFN-gamma production, Th1 cell proliferation and cytotoxicity, regulatory T cell development, and increases in macrophage and neutrophil infiltration into sites of inflammation.

Description: TIMs are type I transmembrane glycoproteins with one Ig-like V-type domain and a Ser/Thr-rich mucin stalk. TIM-3 is expressed on the surface of effector T cel tonsil, lymph node or spleen. ls (CD4+Th1 and CD8+Tc1) but not on helper T cells (CD4+Th2 and CD8+Tc2). In chronic inflammation, autoimmune disorders, and some cancers, TIM-3 is upregulated on several other hematopoietic cell types. The Ig domain of TIM-3 interacts with a ligand on resting but not activated Th1 and Th2 cells. The glycosylated Ig domain of TIM-3 binds cell-associated galectin-9. This induces TIM-3 Tyr phosphorylation and pro-apoptotic signaling. TIM-3 functions as a negative regulator of Th1 cell activity. Its blockade results in increased IFN-gamma production, Th1 cell proliferation and cytotoxicity, regulatory T cell development, and increases in macrophage and neutrophil infiltration into sites of inflammation.

Description: The protein encoded by the HAVCR2 gene belongs to the immunoglobulin superfamily, and TIM family of proteins. CD4-positive T helper lymphocytes can be divided into types 1 (Th1) and 2 (Th2) on the basis of their cytokine secretion patterns. Th1 cells are involved in cell-mediated immunity to intracellular pathogens and delayed-type hypersensitivity reactions, whereas, Th2 cells are involved in the control of extracellular helminthic infections and the promotion of atopic and allergic diseases. This protein is a Th1-specific cell surface protein that regulates macrophage activation, and inhibits Th1-mediated auto- and alloimmune responses, and promotes immunological tolerance. [RefSeq]

Description: The protein encoded by the HAVCR2 gene belongs to the immunoglobulin superfamily, and TIM family of proteins. CD4-positive T helper lymphocytes can be divided into types 1 (Th1) and 2 (Th2) on the basis of their cytokine secretion patterns. Th1 cells are involved in cell-mediated immunity to intracellular pathogens and delayed-type hypersensitivity reactions, whereas, Th2 cells are involved in the control of extracellular helminthic infections and the promotion of atopic and allergic diseases. This protein is a Th1-specific cell surface protein that regulates macrophage activation, and inhibits Th1-mediated auto- and alloimmune responses, and promotes immunological tolerance. [RefSeq]

Description: The protein encoded by the HAVCR2 gene belongs to the immunoglobulin superfamily, and TIM family of proteins. CD4-positive T helper lymphocytes can be divided into types 1 (Th1) and 2 (Th2) on the basis of their cytokine secretion patterns. Th1 cells are involved in cell-mediated immunity to intracellular pathogens and delayed-type hypersensitivity reactions, whereas, Th2 cells are involved in the control of extracellular helminthic infections and the promotion of atopic and allergic diseases. This protein is a Th1-specific cell surface protein that regulates macrophage activation, and inhibits Th1-mediated auto- and alloimmune responses, and promotes immunological tolerance. [RefSeq]

Description: The protein encoded by the HAVCR2 gene belongs to the immunoglobulin superfamily, and TIM family of proteins. CD4-positive T helper lymphocytes can be divided into types 1 (Th1) and 2 (Th2) on the basis of their cytokine secretion patterns. Th1 cells are involved in cell-mediated immunity to intracellular pathogens and delayed-type hypersensitivity reactions, whereas, Th2 cells are involved in the control of extracellular helminthic infections and the promotion of atopic and allergic diseases. This protein is a Th1-specific cell surface protein that regulates macrophage activation, and inhibits Th1-mediated auto- and alloimmune responses, and promotes immunological tolerance. [RefSeq]

Description: TIMs are type I transmembrane glycoproteins with one Ig-like V-type domain and a Ser/Thr-rich mucin stalk. TIM-3 is expressed on the surface of effector T cells (CD4+Th1 and CD8+Tc1) but not on helper T cells (CD4+Th2 and CD8+Tc2). In chronic inflammation, autoimmune disorders, and some cancers, TIM-3 is upregulated on several other hematopoietic cell types. The Ig domain of TIM-3 interacts with a ligand on resting but not activated Th1 and Th2 cells. The glycosylated Ig domain of TIM-3 binds cell-associated galectin-9. This induces TIM-3 Tyr phosphorylation and pro-apoptotic signaling. TIM-3 functions as a negative regulator of Th1 cell activity. Its blockade results in increased IFN-gamma production, Th1 cell proliferation and cytotoxicity, regulatory T cell development, and increases in macrophage and neutrophil infiltration into sites of inflammation.

Description: TIMs are type I transmembrane glycoproteins with one Ig-like V-type domain and a Ser/Thr-rich mucin stalk. TIM-3 is expressed on the surface of effector T cells (CD4+Th1 and CD8+Tc1) but not on helper T cells (CD4+Th2 and CD8+Tc2). In chronic inflammation, autoimmune disorders, and some cancers, TIM-3 is upregulated on several other hematopoietic cell types. The Ig domain of TIM-3 interacts with a ligand on resting but not activated Th1 and Th2 cells. The glycosylated Ig domain of TIM-3 binds cell-associated galectin-9. This induces TIM-3 Tyr phosphorylation and pro-apoptotic signaling. TIM-3 functions as a negative regulator of Th1 cell activity. Its blockade results in increased IFN-gamma production, Th1 cell proliferation and cytotoxicity, regulatory T cell development, and increases in macrophage and neutrophil infiltration into sites of inflammation.

Description: TIMs are type I transmembrane glycoproteins with one Ig-like V-type domain and a Ser/Thr-rich mucin stalk. TIM-3 is expressed on the surface of effector T cells (CD4+Th1 and CD8+Tc1) but not on helper T cells (CD4+Th2 and CD8+Tc2). In chronic inflammation, autoimmune disorders, and some cancers, TIM-3 is upregulated on several other hematopoietic cell types. The Ig domain of TIM-3 interacts with a ligand on resting but not activated Th1 and Th2 cells. The glycosylated Ig domain of TIM-3 binds cell-associated galectin-9. This induces TIM-3 Tyr phosphorylation and pro-apoptotic signaling. TIM-3 functions as a negative regulator of Th1 cell activity. Its blockade results in increased IFN-gamma production, Th1 cell proliferation and cytotoxicity, regulatory T cell development, and increases in macrophage and neutrophil infiltration into sites of inflammation.

Description: TIMs are type I transmembrane glycoproteins with one Ig-like V-type domain and a Ser/Thr-rich mucin stalk. TIM-3 is expressed on the surface of effector T cells (CD4+Th1 and CD8+Tc1) but not on helper T cells (CD4+Th2 and CD8+Tc2). In chronic inflammation, autoimmune disorders, and some cancers, TIM-3 is upregulated on several other hematopoietic cell types. The Ig domain of TIM-3 interacts with a ligand on resting but not activated Th1 and Th2 cells. The glycosylated Ig domain of TIM-3 binds cell-associated galectin-9. This induces TIM-3 Tyr phosphorylation and pro-apoptotic signaling. TIM-3 functions as a negative regulator of Th1 cell activity. Its blockade results in increased IFN-gamma production, Th1 cell proliferation and cytotoxicity, regulatory T cell development, and increases in macrophage and neutrophil infiltration into sites of inflammation.

Description: TIMs are type I transmembrane glycoproteins with one Ig-like V-type domain and a Ser/Thr-rich mucin stalk. TIM-3 is expressed on the surface of effector T cel tonsil, lymph node or spleen. ls (CD4+Th1 and CD8+Tc1) but not on helper T cells (CD4+Th2 and CD8+Tc2). In chronic inflammation, autoimmune disorders, and some cancers, TIM-3 is upregulated on several other hematopoietic cell types. The Ig domain of TIM-3 interacts with a ligand on resting but not activated Th1 and Th2 cells. The glycosylated Ig domain of TIM-3 binds cell-associated galectin-9. This induces TIM-3 Tyr phosphorylation and pro-apoptotic signaling. TIM-3 functions as a negative regulator of Th1 cell activity. Its blockade results in increased IFN-gamma production, Th1 cell proliferation and cytotoxicity, regulatory T cell development, and increases in macrophage and neutrophil infiltration into sites of inflammation.

Description: TIMs are type I transmembrane glycoproteins with one Ig-like V-type domain and a Ser/Thr-rich mucin stalk. TIM-3 is expressed on the surface of effector T cel tonsil, lymph node or spleen. ls (CD4+Th1 and CD8+Tc1) but not on helper T cells (CD4+Th2 and CD8+Tc2). In chronic inflammation, autoimmune disorders, and some cancers, TIM-3 is upregulated on several other hematopoietic cell types. The Ig domain of TIM-3 interacts with a ligand on resting but not activated Th1 and Th2 cells. The glycosylated Ig domain of TIM-3 binds cell-associated galectin-9. This induces TIM-3 Tyr phosphorylation and pro-apoptotic signaling. TIM-3 functions as a negative regulator of Th1 cell activity. Its blockade results in increased IFN-gamma production, Th1 cell proliferation and cytotoxicity, regulatory T cell development, and increases in macrophage and neutrophil infiltration into sites of inflammation.

Description: TIMs are type I transmembrane glycoproteins with one Ig-like V-type domain and a Ser/Thr-rich mucin stalk. TIM-3 is expressed on the surface of effector T cel tonsil, lymph node or spleen. ls (CD4+Th1 and CD8+Tc1) but not on helper T cells (CD4+Th2 and CD8+Tc2). In chronic inflammation, autoimmune disorders, and some cancers, TIM-3 is upregulated on several other hematopoietic cell types. The Ig domain of TIM-3 interacts with a ligand on resting but not activated Th1 and Th2 cells. The glycosylated Ig domain of TIM-3 binds cell-associated galectin-9. This induces TIM-3 Tyr phosphorylation and pro-apoptotic signaling. TIM-3 functions as a negative regulator of Th1 cell activity. Its blockade results in increased IFN-gamma production, Th1 cell proliferation and cytotoxicity, regulatory T cell development, and increases in macrophage and neutrophil infiltration into sites of inflammation.

Description: TIMs are type I transmembrane glycoproteins with one Ig-like V-type domain and a Ser/Thr-rich mucin stalk. TIM-3 is expressed on the surface of effector T cel tonsil, lymph node or spleen. ls (CD4+Th1 and CD8+Tc1) but not on helper T cells (CD4+Th2 and CD8+Tc2). In chronic inflammation, autoimmune disorders, and some cancers, TIM-3 is upregulated on several other hematopoietic cell types. The Ig domain of TIM-3 interacts with a ligand on resting but not activated Th1 and Th2 cells. The glycosylated Ig domain of TIM-3 binds cell-associated galectin-9. This induces TIM-3 Tyr phosphorylation and pro-apoptotic signaling. TIM-3 functions as a negative regulator of Th1 cell activity. Its blockade results in increased IFN-gamma production, Th1 cell proliferation and cytotoxicity, regulatory T cell development, and increases in macrophage and neutrophil infiltration into sites of inflammation.

Description: TIMs are type I transmembrane glycoproteins with one Ig-like V-type domain and a Ser/Thr-rich mucin stalk. TIM-3 is expressed on the surface of effector T cel tonsil, lymph node or spleen. ls (CD4+Th1 and CD8+Tc1) but not on helper T cells (CD4+Th2 and CD8+Tc2). In chronic inflammation, autoimmune disorders, and some cancers, TIM-3 is upregulated on several other hematopoietic cell types. The Ig domain of TIM-3 interacts with a ligand on resting but not activated Th1 and Th2 cells. The glycosylated Ig domain of TIM-3 binds cell-associated galectin-9. This induces TIM-3 Tyr phosphorylation and pro-apoptotic signaling. TIM-3 functions as a negative regulator of Th1 cell activity. Its blockade results in increased IFN-gamma production, Th1 cell proliferation and cytotoxicity, regulatory T cell development, and increases in macrophage and neutrophil infiltration into sites of inflammation.

Description: TIMs are type I transmembrane glycoproteins with one Ig-like V-type domain and a Ser/Thr-rich mucin stalk. TIM-3 is expressed on the surface of effector T cel tonsil, lymph node or spleen. ls (CD4+Th1 and CD8+Tc1) but not on helper T cells (CD4+Th2 and CD8+Tc2). In chronic inflammation, autoimmune disorders, and some cancers, TIM-3 is upregulated on several other hematopoietic cell types. The Ig domain of TIM-3 interacts with a ligand on resting but not activated Th1 and Th2 cells. The glycosylated Ig domain of TIM-3 binds cell-associated galectin-9. This induces TIM-3 Tyr phosphorylation and pro-apoptotic signaling. TIM-3 functions as a negative regulator of Th1 cell activity. Its blockade results in increased IFN-gamma production, Th1 cell proliferation and cytotoxicity, regulatory T cell development, and increases in macrophage and neutrophil infiltration into sites of inflammation.

Description: TIMs are type I transmembrane glycoproteins with one Ig-like V-type domain and a Ser/Thr-rich mucin stalk. TIM-3 is expressed on the surface of effector T cel tonsil, lymph node or spleen. ls (CD4+Th1 and CD8+Tc1) but not on helper T cells (CD4+Th2 and CD8+Tc2). In chronic inflammation, autoimmune disorders, and some cancers, TIM-3 is upregulated on several other hematopoietic cell types. The Ig domain of TIM-3 interacts with a ligand on resting but not activated Th1 and Th2 cells. The glycosylated Ig domain of TIM-3 binds cell-associated galectin-9. This induces TIM-3 Tyr phosphorylation and pro-apoptotic signaling. TIM-3 functions as a negative regulator of Th1 cell activity. Its blockade results in increased IFN-gamma production, Th1 cell proliferation and cytotoxicity, regulatory T cell development, and increases in macrophage and neutrophil infiltration into sites of inflammation.

Description: TIMs are type I transmembrane glycoproteins with one Ig-like V-type domain and a Ser/Thr-rich mucin stalk. TIM-3 is expressed on the surface of effector T cel tonsil, lymph node or spleen. ls (CD4+Th1 and CD8+Tc1) but not on helper T cells (CD4+Th2 and CD8+Tc2). In chronic inflammation, autoimmune disorders, and some cancers, TIM-3 is upregulated on several other hematopoietic cell types. The Ig domain of TIM-3 interacts with a ligand on resting but not activated Th1 and Th2 cells. The glycosylated Ig domain of TIM-3 binds cell-associated galectin-9. This induces TIM-3 Tyr phosphorylation and pro-apoptotic signaling. TIM-3 functions as a negative regulator of Th1 cell activity. Its blockade results in increased IFN-gamma production, Th1 cell proliferation and cytotoxicity, regulatory T cell development, and increases in macrophage and neutrophil infiltration into sites of inflammation.

Description: TIMs are type I transmembrane glycoproteins with one Ig-like V-type domain and a Ser/Thr-rich mucin stalk. TIM-3 is expressed on the surface of effector T cel tonsil, lymph node or spleen. ls (CD4+Th1 and CD8+Tc1) but not on helper T cells (CD4+Th2 and CD8+Tc2). In chronic inflammation, autoimmune disorders, and some cancers, TIM-3 is upregulated on several other hematopoietic cell types. The Ig domain of TIM-3 interacts with a ligand on resting but not activated Th1 and Th2 cells. The glycosylated Ig domain of TIM-3 binds cell-associated galectin-9. This induces TIM-3 Tyr phosphorylation and pro-apoptotic signaling. TIM-3 functions as a negative regulator of Th1 cell activity. Its blockade results in increased IFN-gamma production, Th1 cell proliferation and cytotoxicity, regulatory T cell development, and increases in macrophage and neutrophil infiltration into sites of inflammation.

Description: TIMs are type I transmembrane glycoproteins with one Ig-like V-type domain and a Ser/Thr-rich mucin stalk. TIM-3 is expressed on the surface of effector T cel tonsil, lymph node or spleen. ls (CD4+Th1 and CD8+Tc1) but not on helper T cells (CD4+Th2 and CD8+Tc2). In chronic inflammation, autoimmune disorders, and some cancers, TIM-3 is upregulated on several other hematopoietic cell types. The Ig domain of TIM-3 interacts with a ligand on resting but not activated Th1 and Th2 cells. The glycosylated Ig domain of TIM-3 binds cell-associated galectin-9. This induces TIM-3 Tyr phosphorylation and pro-apoptotic signaling. TIM-3 functions as a negative regulator of Th1 cell activity. Its blockade results in increased IFN-gamma production, Th1 cell proliferation and cytotoxicity, regulatory T cell development, and increases in macrophage and neutrophil infiltration into sites of inflammation.

Description: TIMs are type I transmembrane glycoproteins with one Ig-like V-type domain and a Ser/Thr-rich mucin stalk. TIM-3 is expressed on the surface of effector T cel tonsil, lymph node or spleen. ls (CD4+Th1 and CD8+Tc1) but not on helper T cells (CD4+Th2 and CD8+Tc2). In chronic inflammation, autoimmune disorders, and some cancers, TIM-3 is upregulated on several other hematopoietic cell types. The Ig domain of TIM-3 interacts with a ligand on resting but not activated Th1 and Th2 cells. The glycosylated Ig domain of TIM-3 binds cell-associated galectin-9. This induces TIM-3 Tyr phosphorylation and pro-apoptotic signaling. TIM-3 functions as a negative regulator of Th1 cell activity. Its blockade results in increased IFN-gamma production, Th1 cell proliferation and cytotoxicity, regulatory T cell development, and increases in macrophage and neutrophil infiltration into sites of inflammation.

Description: TIMs are type I transmembrane glycoproteins with one Ig-like V-type domain and a Ser/Thr-rich mucin stalk. TIM-3 is expressed on the surface of effector T cel tonsil, lymph node or spleen. ls (CD4+Th1 and CD8+Tc1) but not on helper T cells (CD4+Th2 and CD8+Tc2). In chronic inflammation, autoimmune disorders, and some cancers, TIM-3 is upregulated on several other hematopoietic cell types. The Ig domain of TIM-3 interacts with a ligand on resting but not activated Th1 and Th2 cells. The glycosylated Ig domain of TIM-3 binds cell-associated galectin-9. This induces TIM-3 Tyr phosphorylation and pro-apoptotic signaling. TIM-3 functions as a negative regulator of Th1 cell activity. Its blockade results in increased IFN-gamma production, Th1 cell proliferation and cytotoxicity, regulatory T cell development, and increases in macrophage and neutrophil infiltration into sites of inflammation.

Description: TIMs are type I transmembrane glycoproteins with one Ig-like V-type domain and a Ser/Thr-rich mucin stalk. TIM-3 is expressed on the surface of effector T cells (CD4+ Th1 and CD8+Tc1) but not on helper T cells (CD4+Th2 and CD8+Tc2). In chronic inflammation, autoimmune disorders, and some cancers, TIM-3 is upregulated on several other hematopoietic cell types. The Ig domain of TIM-3 interacts with a ligand on resting but not activated Th1 and Th2 cells. The glycosylated Ig domain of TIM-3 binds cell-associated galectin-9. This induces TIM-3 Tyr phosphorylation and pro-apoptotic signaling. TIM-3 functions as a negative regulator of Th1 cell activity. Its blockade results in increased IFN-gamma production, Th1 cell proliferation and cytotoxicity, regulatory T cell development, and increases in macrophage and neutrophil infiltration into sites of inflammation.

Description: TIMs are type I transmembrane glycoproteins with one Ig-like V-type domain and a Ser/Thr-rich mucin stalk. TIM-3 is expressed on the surface of effector T cells (CD4+ Th1 and CD8+Tc1) but not on helper T cells (CD4+Th2 and CD8+Tc2). In chronic inflammation, autoimmune disorders, and some cancers, TIM-3 is upregulated on several other hematopoietic cell types. The Ig domain of TIM-3 interacts with a ligand on resting but not activated Th1 and Th2 cells. The glycosylated Ig domain of TIM-3 binds cell-associated galectin-9. This induces TIM-3 Tyr phosphorylation and pro-apoptotic signaling. TIM-3 functions as a negative regulator of Th1 cell activity. Its blockade results in increased IFN-gamma production, Th1 cell proliferation and cytotoxicity, regulatory T cell development, and increases in macrophage and neutrophil infiltration into sites of inflammation.

Description: TIMs are type I transmembrane glycoproteins with one Ig-like V-type domain and a Ser/Thr-rich mucin stalk. TIM-3 is expressed on the surface of effector T cells (CD4+ Th1 and CD8+Tc1) but not on helper T cells (CD4+Th2 and CD8+Tc2). In chronic inflammation, autoimmune disorders, and some cancers, TIM-3 is upregulated on several other hematopoietic cell types. The Ig domain of TIM-3 interacts with a ligand on resting but not activated Th1 and Th2 cells. The glycosylated Ig domain of TIM-3 binds cell-associated galectin-9. This induces TIM-3 Tyr phosphorylation and pro-apoptotic signaling. TIM-3 functions as a negative regulator of Th1 cell activity. Its blockade results in increased IFN-gamma production, Th1 cell proliferation and cytotoxicity, regulatory T cell development, and increases in macrophage and neutrophil infiltration into sites of inflammation.

Description: TIMs are type I transmembrane glycoproteins with one Ig-like V-type domain and a Ser/Thr-rich mucin stalk. TIM-3 is expressed on the surface of effector T cell tonsil, lymph node or spleen. ls (CD4+Th1 and CD8+Tc1) but not on helper T cells (CD4+Th2 and CD8+Tc2). In chronic inflammation, autoimmune disorders, and some cancers, TIM-3 is upregulated on several other hematopoietic cell types. The Ig domain of TIM-3 interacts with a ligand on resting but not activated Th1 and Th2 cells. The glycosylated Ig domain of TIM-3 binds cell-associated galectin-9. This induces TIM-3 Tyr phosphorylation and pro-apoptotic signaling. TIM-3 functions as a negative regulator of Th1 cell activity. Its blockade results in increased IFN-gamma production, Th1 cell proliferation and cytotoxicity, regulatory T cell development, and increases in macrophage and neutrophil infiltration into sites of inflammation.

Description: TIMs are type I transmembrane glycoproteins with one Ig-like V-type domain and a Ser/Thr-rich mucin stalk. TIM-3 is expressed on the surface of effector T cell tonsil, lymph node or spleen. ls (CD4+Th1 and CD8+Tc1) but not on helper T cells (CD4+Th2 and CD8+Tc2). In chronic inflammation, autoimmune disorders, and some cancers, TIM-3 is upregulated on several other hematopoietic cell types. The Ig domain of TIM-3 interacts with a ligand on resting but not activated Th1 and Th2 cells. The glycosylated Ig domain of TIM-3 binds cell-associated galectin-9. This induces TIM-3 Tyr phosphorylation and pro-apoptotic signaling. TIM-3 functions as a negative regulator of Th1 cell activity. Its blockade results in increased IFN-gamma production, Th1 cell proliferation and cytotoxicity, regulatory T cell development, and increases in macrophage and neutrophil infiltration into sites of inflammation.

Description: TIMs are type I transmembrane glycoproteins with one Ig-like V-type domain and a Ser/Thr-rich mucin stalk. TIM-3 is expressed on the surface of effector T cell tonsil, lymph node or spleen. ls (CD4+Th1 and CD8+Tc1) but not on helper T cells (CD4+Th2 and CD8+Tc2). In chronic inflammation, autoimmune disorders, and some cancers, TIM-3 is upregulated on several other hematopoietic cell types. The Ig domain of TIM-3 interacts with a ligand on resting but not activated Th1 and Th2 cells. The glycosylated Ig domain of TIM-3 binds cell-associated galectin-9. This induces TIM-3 Tyr phosphorylation and pro-apoptotic signaling. TIM-3 functions as a negative regulator of Th1 cell activity. Its blockade results in increased IFN-gamma production, Th1 cell proliferation and cytotoxicity, regulatory T cell development, and increases in macrophage and neutrophil infiltration into sites of inflammation.

Description: Hepatitis A virus cellular receptor 2 is also known as HAVCR2, FLJ14428, KIM3, TIM3, TIMD3, is a member of the TIM family of immune regulating molecules with one Ig-like V-type domain and a Ser/Thr-rich mucin stalk. CD4-positive T helper lymphocytes can be divided into types 1 (Th1) and 2 (Th2) on the basis of their cytokine secretion patterns. Th1 cells and their associated cytokines are involved in cell-mediated immunity to intracellular pathogens and delayed-type hypersensitivity reactions, whereas Th2 cells are involved in the control of extracellular helminthic infections and the promotion of atopic and allergic diseases. The 2 types of cells also cross-regulate the functions of the other. HAVCR2 is a Th1-specific cell surface protein that regulates macrophage activation and enhances the severity of experimental autoimmune encephalomyelitis in mice. HAVCR2 regulates macrophage activation. Inhibits T-helper type 1 lymphocyte (Th1)-mediated auto- and alloimmune responses and promotes immunological tolerance. May be also involved in T-cell homing. Dysregulation of the HAVCR2-galectin-9 pathway could underlie chronic autoimmune disease states in human, such as multiple sclerosis.

Description: Hepatitis A virus cellular receptor 2 is also known as HAVCR2, FLJ14428, KIM3, TIM3, TIMD3, is a member of the TIM family of immune regulating molecules with one Ig-like V-type domain and a Ser/Thr-rich mucin stalk. CD4-positive T helper lymphocytes can be divided into types 1 (Th1) and 2 (Th2) on the basis of their cytokine secretion patterns. Th1 cells and their associated cytokines are involved in cell-mediated immunity to intracellular pathogens and delayed-type hypersensitivity reactions, whereas Th2 cells are involved in the control of extracellular helminthic infections and the promotion of atopic and allergic diseases. The 2 types of cells also cross-regulate the functions of the other. HAVCR2 is a Th1-specific cell surface protein that regulates macrophage activation and enhances the severity of experimental autoimmune encephalomyelitis in mice. HAVCR2 regulates macrophage activation. Inhibits T-helper type 1 lymphocyte (Th1)-mediated auto- and alloimmune responses and promotes immunological tolerance. May be also involved in T-cell homing. Dysregulation of the HAVCR2-galectin-9 pathway could underlie chronic autoimmune disease states in human, such as multiple sclerosis.

Description: Lyophilized from a 0.2 μm filtered solution of PBS, pH7.4.

Description: Lyophilized from a 0.2 μm filtered solution of PBS, pH7.4.

Description: Lyophilized from a 0.2 μm filtered solution of PBS, pH7.4.

Description: Lyophilized from a 0.2 μm filtered solution of PBS, pH7.4.

Description: Lyophilized from a 0.2 μm filtered solution of PBS, pH7.4.

Description: Lyophilized from a 0.2 μm filtered solution of PBS, pH7.4.

Description: Lyophilized from a 0.2 μm filtered solution of PBS, pH7.4.

Description: Lyophilized from a 0.2 μm filtered solution of PBS, pH7.4.

Description: A polyclonal antibody raised in Rabbit that recognizes and binds to Human HAVCR2 / TIM-3 (aa176-194). This antibody is tested and proven to work in the following applications:

Description: A sandwich quantitative ELISA assay kit for detection of Human Hepatitis A Virus Cellular Receptor 2 (HAVCR2) in samples from tissue homogenates, cell lysates or other biological fluids.

Description: A sandwich quantitative ELISA assay kit for detection of Human Hepatitis A Virus Cellular Receptor 2 (HAVCR2) in samples from tissue homogenates, cell lysates or other biological fluids.

Description: Description of target: Hepatitis A virus cellular receptor 2 (HAVCR2), also known as T-cell immunoglobulin and mucin-domain containing-3 (TIM-3), is a protein that in humans is encoded by the HAVCR2 gene. The protein encoded by this gene belongs to the immunoglobulin superfamily, and TIM family of proteins. CD4-positive T helper lymphocytes can be divided into types 1 (Th1) and 2 (Th2) on the basis of their cytokine secretion patterns. Th1 cells are involved in cell-mediated immunity to intracellular pathogens and delayed-type hypersensitivity reactions, whereas, Th2 cells are involved in the control of extracellular helminthic infections and the promotion of atopic and allergic diseases. This protein is a Th1-specific cell surface protein that regulates macrophage activation, and inhibits Th1-mediated auto- and alloimmune responses, and promotes immunological tolerance.;Species reactivity: Human;Application: ELISA;Assay info: ;Sensitivity: <10pg/ml

Description: Description of target: Hepatitis A virus cellular receptor 2 (HAVCR2), also known as T-cell immunoglobulin and mucin-domain containing-3 (TIM-3), is a protein that in humans is encoded by the HAVCR2 gene. The protein encoded by this gene belongs to the immunoglobulin superfamily, and TIM family of proteins. CD4-positive T helper lymphocytes can be divided into types 1 (Th1) and 2 (Th2) on the basis of their cytokine secretion patterns. Th1 cells are involved in cell-mediated immunity to intracellular pathogens and delayed-type hypersensitivity reactions, whereas, Th2 cells are involved in the control of extracellular helminthic infections and the promotion of atopic and allergic diseases. This protein is a Th1-specific cell surface protein that regulates macrophage activation, and inhibits Th1-mediated auto- and alloimmune responses, and promotes immunological tolerance.;Species reactivity: Human;Application: ELISA;Assay info: ;Sensitivity: <10pg/ml

Description: Description of target: Cell surface receptor implicated in modulating innate and adaptive immune responses. Generally accepted to have an inhibiting function. Reports on stimulating functions suggest that the activity may be influenced by the cellular context and/or the respective ligand (PubMed:24825777). Regulates macrophage activation (PubMed:11823861). Inhibits T-helper type 1 lymphocyte (Th1)-mediated auto- and alloimmune responses and promotes immunological tolerance (PubMed:14556005). In CD8+ cells attenuates TCR-induced signaling, specifically by blocking NF-kappaB and NFAT promoter activities resulting in the loss of IL-2 secretion. The function may implicate its association with LCK proposed to impair phosphorylation of TCR subunits, and/or LGALS9-dependent recruitment of PTPRC to the immunological synapse (PubMed:24337741, PubMed:26492563). In contrast, shown to activate TCR-induced signaling in T-cells probably implicating ZAP70, LCP2, LCK and FYN (By similarity). Expressed on Treg cells can inhibit Th17 cell responses (PubMed:24838857). Receptor for LGALS9 (PubMed:16286920, PubMed:24337741). Binding to LGALS9 is believed to result in suppression of T-cell responses; the resulting apoptosis of antigen-specific cells may implicate HAVCR2 phosphorylation and disruption of its association with BAG6. Binding to LGALS9 is proposed to be involved in innate immune response to intracellular pathogens. Expressed on Th1 cells interacts with LGALS9 expressed on Mycobacterium tuberculosis-infected macrophages to stimulate antibactericidal activity including IL-1 beta secretion and to restrict intracellular bacterial growth (By similarity). However, the function as receptor for LGALS9 has been challenged (PubMed:23555261). Also reported to enhance CD8+ T-cell responses to an acute infection such as by Listeria monocytogenes (By similarity). Receptor for phosphatidylserine (PtSer); PtSer-binding is calcium-dependent. May recognize PtSer on apoptotic cells leading to their phagocytosis. Mediates the engulfment of apoptotic cells by dendritic cells. Expressed on T-cells, promotes conjugation but not engulfment of apoptotic cells. Expressed on dendritic cells (DCs) positively regulates innate immune response and in synergy with Toll-like receptors promotes secretion of TNF-alpha. In tumor-imfiltrating DCs suppresses nucleic acid-mediated innate immune repsonse by interaction with HMGB1 and interfering with nucleic acid-sensing and trafficking of nucleid acids to endosomes (By similarity). Expressed on natural killer (NK) cells acts as a coreceptor to enhance IFN-gamma production in response to LGALS9 (PubMed:22323453). In contrast, shown to suppress NK cell-mediated cytotoxicity (PubMed:22383801). Negatively regulates NK cell function in LPS-induced endotoxic shock (By similarity).By similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toiUniProtKB:Q8VIM0 (HAVR2_MOUSE)1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More…</a></p> Manual assertion inferred by curator fromiRef.20"Regulation of T cell responses by the receptor molecule Tim-3."_x005F_x005F_x000D_Gorman J.V., Colgan J.D._x005F_x005F_x000D_Immunol. Res. 59:56-65(2014) [PubMed] [Europe PMC] [Abstract]Cited for: REVIEW ON FUNCTION IN REGULATING T-CELL RESPONSES.7 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment iniRef.1"Th1-specific cell surface protein Tim-3 regulates macrophage activation and severity of an autoimmune disease."_x005F_x005F_x000D_Monney L., Sabatos C.A., Gaglia J.L., Ryu A., Waldner H., Chernova T., Manning S., Greenfield E.A., Coyle A.J., Sobel R.A., Freeman G.J., Kuchroo V.K._x005F_x005F_x000D_Nature 415:536-541(2002) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, VARIANT LEU-140, TISSUE SPECIFICITY.Ref.8"Tim-3 inhibits T helper type 1-mediated auto- and alloimmune responses and promotes immunological tolerance."_x005F_x005F_x000D_Sanchez-Fueyo A., Tian J., Picarella D., Domenig C., Zheng X.X., Sabatos C.A., Manlongat N., Bender O., Kamradt T., Kuchroo V.K., Gutierrez-Ramos J.-C., Coyle A.J., Strom T.B._x005F_x005F_x000D_Nat. Immunol. 4:1093-1101(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION.Ref.9"The Tim-3 ligand galectin-9 negatively regulates T helper type 1 immunity."_x005F_x005F_x000D_Zhu C., Anderson A.C., Schubart A., Xiong H., Imitola J., Khoury S.J., Zheng X.X., Strom T.B., Kuchroo V.K._x005F_x005F_x000D_Nat. Immunol. 6:1245-1252(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A RECEPTOR FOR LGALS9.Ref.16"Tim-3 is an inducible human natural killer cell receptor that enhances interferon gamma production in response to galectin-9."_x005F_x005F_x000D_Gleason M.K., Lenvik T.R., McCullar V., Felices M., O'Brien M.S., Cooley S.A., Verneris M.R., Cichocki F., Holman C.J., Panoskaltsis-Mortari A., Niki T., Hirashima M., Blazar B.R., Miller J.S._x005F_x005F_x000D_Blood 119:3064-3072(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, TISSUE SPECIFICITY.Ref.18"TIM-3 does not act as a receptor for galectin-9."_x005F_x005F_x000D_Leitner J., Rieger A., Pickl W.F., Zlabinger G., Grabmeier-Pfistershammer K., Steinberger P._x005F_x005F_x000D_PLoS Pathog. 9:E1003253-E1003253(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A RECEPTOR FOR LGALS9.Ref.19"Enhanced suppressor function of TIM-3+ FoxP3+ regulatory T cells."_x005F_x005F_x000D_Gautron A.S., Dominguez-Villar M., de Marcken M., Hafler D.A._x005F_x005F_x000D_Eur. J. Immunol. 44:2703-2711(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, TISSUE SPECIFICITY.Ref.22"TIM-3 Suppresses Anti-CD3/CD28-Induced TCR Activation and IL-2 Expression through the NFAT Signaling Pathway."_x005F_x005F_x000D_Tomkowicz B., Walsh E., Cotty A., Verona R., Sabins N., Kaplan F., Santulli-Marotto S., Chin C.N., Mooney J., Lingham R.B., Naso M., McCabe T._x005F_x005F_x000D_PLoS ONE 10:E0140694-E0140694(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH VAV1; AKT; LCP2; ZAP70; SYK; PIK3R1; FYN; SH3BP2 AND SH2D2A, MUTAGENESIS OF TYR-265 AND TYR-272. ;Species reactivity: Human;Application: ELISA;Assay info: Assay Methodology: Quantitative Sandwich Immunoassay;Sensitivity: < 33 pg/mL

Description: For quantitative detection of human IGFBP-3 in cell culture supernates, cell lysates, serum and plasma (heparin, EDTA).

Description: For quantitative detection of human IL-3 in cell culture supernates, serum and plasma( heparin, EDTA, citrate).

Description: For quantitative detection of human MMP-3 in cell culture supernates, serum and plasma (heparin).

Description: For quantitative detection of human Neurotrophin-3 in cell culture supernates and serum.

Description: For quantitative detection of human TIMP-3 in cell culture supernates, serum, plasma(heparin , EDTA) and saliva.

Description: For quantitative detection of Human Kallikrein 3 in cell culture supernates, cell lysates, serum and plasma (heparin, EDTA).

Description: For quantitative detection of human ICAM-3 in cell culture supernates, cell lysates, serum and plasma (heparin, EDTA).

Description: For quantitative detection of human Ficolin-3 in cell culture supernates, serum and plasma(heparin).

Description: For quantitative detection of human DKK-3 in cell culture supernates, cell lysates, serum and plasma (heparin, EDTA).

Description: For quantitative detection of human Relaxin 3 in cell culture supernates, serum and plasma( heparin).