Description: A polyclonal antibody raised in Rabbit that recognizes and binds to Human TIM-1 . This antibody is tested and proven to work in the following applications:

Description: A polyclonal antibody raised in Rabbit that recognizes and binds to Human TIM-1 . This antibody is tested and proven to work in the following applications:

Description: A Rabbit Polyclonal antibody against TIM-1 from Human. This antibody is tested and validated for WB, ELISA, WB, ELISA

Description: A Rabbit Polyclonal antibody against TIM-1 from Human. This antibody is tested and validated for WB, ELISA, WB, ELISA

Description: TIM-1 Antibody: The human form of TIM-1 was initially discovered as a membrane glycoprotein through which the hepatitis A virus can gain entry into a cell. It was also identified as kidney injury molecule 1 (Kim-1), a predicted adhesion molecule that is upregulated on the surfaces of kidney epithelia. It is also expressed on T helper 2 (Th2) cells of the immune system, and following the binding of its natural ligand TIM-4, stimulates T cell expansion and cytokine production in response to viral challenge. It has been suggested that hyperactivation of TIM-1 leads to an increased level of Th2 responsiveness and asthma susceptibility, and antibodies to TIM-1 may therefore be a novel approach to treating asthma.

Description: TIM-1 Antibody: The human form of TIM-1 was initially discovered as a membrane glycoprotein through which the hepatitis A virus can gain entry into a cell. It was also identified as kidney injury molecule 1 (Kim-1), a predicted adhesion molecule that is upregulated on the surfaces of kidney epithelia. It is also expressed on T helper 2 (Th2) cells of the immune system, and following the binding of its natural ligand TIM-4, stimulates T cell expansion and cytokine production in response to viral challenge. It has been suggested that hyperactivation of TIM-1 leads to an increased level of Th2 responsiveness and asthma susceptibility, and antibodies to TIM-1 may therefore be a novel approach to treating asthma.

Description: TIM-1 Antibody: The human form of TIM-1 was initially discovered as a membrane glycoprotein through which the hepatitis A virus can gain entry into a cell. It was also identified as kidney injury molecule 1 (Kim-1), a predicted adhesion molecule that is upregulated on the surfaces of kidney epithelia. It is also expressed on T helper 2 (Th2) cells of the immune system, and following the binding of its natural ligand TIM-4, stimulates T cell expansion and cytokine production in response to viral challenge. It has been suggested that hyperactivation of TIM-1 leads to an increased level of Th2 responsiveness and asthma susceptibility, and antibodies to TIM-1 may therefore be a novel approach to treating asthma.

Description: TIM-1 Antibody: The human form of TIM-1 was initially discovered as a membrane glycoprotein through which the hepatitis A virus can gain entry into a cell. It was also identified as kidney injury molecule 1 (Kim-1), a predicted adhesion molecule that is upregulated on the surfaces of kidney epithelia. It is also expressed on T helper 2 (Th2) cells of the immune system, and following the binding of its natural ligand TIM-4, stimulates T cell expansion and cytokine production in response to viral challenge. It has been suggested that hyperactivation of TIM-1 leads to an increased level of Th2 responsiveness and asthma susceptibility, and antibodies to TIM-1 may therefore be a novel approach to treating asthma.

Description: A polyclonal antibody for detection of Oncogene TIM from Human, Mouse, Rat. This Oncogene TIM antibody is for WB, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the Internal region of human Oncogene TIM at AA range: 160-240

Description: A polyclonal antibody for detection of Oncogene TIM from Human, Mouse, Rat. This Oncogene TIM antibody is for WB, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the Internal region of human Oncogene TIM at AA range: 160-240

Description: A polyclonal antibody for detection of Oncogene TIM from Human, Mouse, Rat. This Oncogene TIM antibody is for WB, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the Internal region of human Oncogene TIM at AA range: 160-240

Description: A polyclonal antibody raised in Rabbit that recognizes and binds to Human Tim-3 . This antibody is tested and proven to work in the following applications:

Description: A polyclonal antibody raised in Rabbit that recognizes and binds to Human TIM-4 . This antibody is tested and proven to work in the following applications:

Description: A polyclonal antibody raised in Rabbit that recognizes and binds to Human TIM-4 . This antibody is tested and proven to work in the following applications:

Description: A Rabbit Polyclonal antibody against Oncogene TIM from Human/Mouse/Rat. This antibody is tested and validated for WB, ELISA, WB, ELISA

Description: A Rabbit Polyclonal antibody against Oncogene TIM from Human/Mouse/Rat. This antibody is tested and validated for WB, ELISA, WB, ELISA

Description: Rabbit polyclonal to TIM-1.

Description: Mouse monoclonal TIM antibody

Description: Mouse monoclonal TIM antibody

Description: (IN) TIM-1 peptide

Description: (NT) TIM-1 peptide

Description: Mouse polyclonal to TIM 1

Description: Rabbit polyclonal to TIM 1

Description: Mouse polyclonal to TIM 1

Description: A polyclonal antibody raised in Goat that recognizes and binds to Human Goat Anti-TIM-1 (internal region). This antibody is tested and proven to work in the following applications:

Description: TIM-4 Antibody: The T cell immunoglobulin and mucin domain containing protein (TIM) family encodes cell surface receptors that are involved in the regulation of T helper (Th) -1 and -2 cell-mediated immunity. TIM-4, which is preferentially expressed on macrophages and dendritic cells, is the natural ligand of TIM-1, and this binding leads to T-cell expansion and cytokine production. Unlike other members of the TIM family, TIM-4 lacks a putative tyrosine phosphorylation signal sequence in its intracellular domain. The TIM-4 gene maps to a locus associated with predisposition to asthma in both mice and humans and with its connection to TIM-1-triggered Th2 responsiveness, may be considered as a candidate disease/predisposition gene for asthma.

Description: TIM-4 Antibody: The T cell immunoglobulin and mucin domain containing protein (TIM) family encodes cell surface receptors that are involved in the regulation of T helper (Th) -1 and -2 cell-mediated immunity. TIM-4, which is preferentially expressed on macrophages and dendritic cells, is the natural ligand of TIM-1, and this binding leads to T-cell expansion and cytokine production. Unlike other members of the TIM family, TIM-4 lacks a putative tyrosine phosphorylation signal sequence in its intracellular domain. The TIM-4 gene maps to a locus associated with predisposition to asthma in both mice and humans and with its connection to TIM-1-triggered Th2 responsiveness, may be considered as a candidate disease/predisposition gene for asthma.

Description: TIM-4 Antibody: The T cell immunoglobulin and mucin domain containing protein (TIM) family encodes cell surface receptors that are involved in the regulation of T helper (Th) -1 and -2 cell-mediated immunity. TIM-4, which is preferentially expressed on macrophages and dendritic cells, is the natural ligand of TIM-1, and this binding leads to T-cell expansion and cytokine production. Unlike other members of the TIM family, TIM-4 lacks a putative tyrosine phosphorylation signal sequence in its intracellular domain. The TIM-4 gene maps to a locus associated with predisposition to asthma in both mice and humans and with its connection to TIM-1-triggered Th2 responsiveness, may be considered as a candidate disease/predisposition gene for asthma.

Description: TIM-4 Antibody: The T cell immunoglobulin and mucin domain containing protein (TIM) family encodes cell surface receptors that are involved in the regulation of T helper (Th) -1 and -2 cell-mediated immunity. TIM-4, which is preferentially expressed on macrophages and dendritic cells, is the natural ligand of TIM-1, and this binding leads to T-cell expansion and cytokine production. Unlike other members of the TIM family, TIM-4 lacks a putative tyrosine phosphorylation signal sequence in its intracellular domain. The TIM-4 gene maps to a locus associated with predisposition to asthma in both mice and humans and with its connection to TIM-1-triggered Th2 responsiveness, may be considered as a candidate disease/predisposition gene for asthma.

Description: The immune checkpoint protein TIM-3 is a member of the immunoglobulin superfamily and TIM family of proteins that was initially identified as a specific marker of fully differentiated IFN-γ producing CD4 T helper 1 (Th1) and CD8 cytotoxic cells. It is a Th1-specific cell surface protein that regulates macrophage activation and negatively regulates Th1-mediated auto- and alloimmune responses, and is also highly expressed on regulatory T cells, monocytes, macrophages, and dendritic cells (1). TIM-3 and PD-1 are co-expressed on most CD4 and CD8 T cells infiltrating solid tumors or in hematologic malignancy in mice; blocking TIM-3 in conjugation with a PD-1 blockade increases the functionality of exhausted T cells and synergizes with to inhibit tumor growth (2,3).

Description: The immune checkpoint protein TIM-3 is a member of the immunoglobulin superfamily and TIM family of proteins that was initially identified as a specific marker of fully differentiated IFN-γ producing CD4 T helper 1 (Th1) and CD8 cytotoxic cells. It is a Th1-specific cell surface protein that regulates macrophage activation and negatively regulates Th1-mediated auto- and alloimmune responses, and is also highly expressed on regulatory T cells, monocytes, macrophages, and dendritic cells (1). TIM-3 and PD-1 are co-expressed on most CD4 and CD8 T cells infiltrating solid tumors or in hematologic malignancy in mice; blocking TIM-3 in conjugation with a PD-1 blockade increases the functionality of exhausted T cells and synergizes with to inhibit tumor growth (2,3).

Description: The TIM (T cell/transmembrane, immunoglobulin and mucin) family plays a critical role in regulating immune responses, including allergy, asthma, transplant tolerance, autoimmunity and the response to viral infections. The unique structure of TIM immunoglobulin variable region domains allows highly specific recognition of phosphatidylserine (PtdSer), exposed on the surface of apoptotic cells. TIM-1 (T cell-immunoglobulinmucin; also KIM-1 and HAVcr-1) is a 100 kDa, type I transmembrane glycoprotein member of the TIM family of immunoglobulin superfamily molecules. There are two cytoplasmic alternate splice forms of TIM1. One is a long (359 aa) kidney form termed TIM-1b, and one is a short (334 aa) liver form termed TIM-1a. TIM-1, important for asthma and allergy, is preferentially expressed on T-helper 2 (Th2) cells and functions as a potent costimulatory molecule for T cell activation.

Description: The TIM (T cell/transmembrane, immunoglobulin and mucin) family plays a critical role in regulating immune responses, including allergy, asthma, transplant tolerance, autoimmunity and the response to viral infections. The unique structure of TIM immunoglobulin variable region domains allows highly specific recognition of phosphatidylserine (PtdSer), exposed on the surface of apoptotic cells. Tim-1 (KIM-1; HAVcr-1) is a 100 kDa, type I transmembrane glycoprotein member of the TIM family of immunoglobulin superfamily molecules. There are two cytoplasmic alternate splice forms of Tim-1. One is a long (359 aa) kidney form termed Tim-1b, and one is a short (334 aa) liver form termed Tim-1a. Tim-1, important for asthma and allergy, is preferentially expressed on T-helper 2 (Th2) cells and functions as a potent costimulatory molecule for T cell activation.

Description: Mouse monoclonal to TIM 1

Description: Mouse monoclonal to TIM 1

Description: Mouse monoclonal to TIM 1

Description: A polyclonal antibody raised in Rabbit that recognizes and binds to Human TIMD4 / TIM4 / TIM-4 (Internal). This antibody is tested and proven to work in the following applications:

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: Rabbit polyclonal to Oncogene TIM.

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 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.