Recombinant human TIM 3 protein (Active) is a Human Fragment protein, in the 22 to 200 aa range, expressed in HEK 293, with >90% purity, < 1 EU/µg endotoxin level and suitable for ELISA, SDS-PAGE, FuncS.
S E V E Y R A E V G Q N A Y L P C F Y T P A A P G N L V P V C W G K G A C P V F E C G N V V L R T D E R D V N Y W T S R Y W L N G D F R K G D V S L T I E N V T L A D S G I Y C C R I Q I P G I M N D E K F N L K L V I K P A K V T P A P T R Q R D F T A A F P R M L T T R G H G P A E T Q T L G S L P D I N L T Q I S T L A N E L R D S R L A N D L R D S G A T I R
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application ELISA | Reactivity Reacts | Dilution info - | Notes - |
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes DTT-reduced Protein migrates as 40-48 kDa due to glycosylation. |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
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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).
CD366, TIM3, TIMD3, HAVCR2, Hepatitis A virus cellular receptor 2, HAVcr-2, T-cell immunoglobulin and mucin domain-containing protein 3, T-cell immunoglobulin mucin receptor 3, T-cell membrane protein 3, TIMD-3, TIM-3
Recombinant human TIM 3 protein (Active) is a Human Fragment protein, in the 22 to 200 aa range, expressed in HEK 293, with >90% purity, < 1 EU/µg endotoxin level and suitable for ELISA, SDS-PAGE, FuncS.
Measured by its binding ability in a functional ELISA. Anti-Human TIM-3 MAb (human IgG4) captured on CM5 chip via Anti-Human IgG Fc antibodies surface, can bind ab182714 with an affinity constant of 9.7 nM as determined.
pH: 7.4
Constituents: 95% PBS, 5% Trehalose
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).
Belongs to the immunoglobulin superfamily. TIM family.
O-glycosylated with core 1 or possibly core 8 glycans.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
This product is stable after storage at:
TIM-3 also known as T cell immunoglobulin and mucin-domain containing-3 or HAVCR2 is a protein involved in immune regulation. It possesses an approximate mass of 35 kDa. TIM-3 is expressed on various immune cells including T cells NK cells and dendritic cells especially after activation. The expression level often changes in response to inflammatory conditions suggesting its role in modulating immune responses.
TIM-3 functions as a checkpoint inhibitor impacting immune cell activity. It is not part of a larger physical complex but it modulates immune responses by interacting with its ligands such as Galectin-9 phosphatidylserine and CEACAM1. TIM-3 involvement in downregulating Th1 cell responses shows its necessary role in maintaining immune homeostasis. The protein also acts in regulating tolerance mechanisms and preventing autoimmunity.
TIM-3 participation is seen in the immune checkpoint and T cell exhaustion pathways. TIM-3 signaling results in T cell inhibition affecting the PD-1 pathway as well. It shares a relationship with proteins like LAG-3 and PD-1 which are key to immune inhibitory signaling. These interactions depict TIM-3's role in immune tolerance during chronic infections and malignancies.
TIM-3 association with cancer and chronic infections provides insight into therapeutic implications. In cancer TIM-3 contributes to immune evasion often co-expressed with PD-1 leading to T cell exhaustion. In autoimmune diseases TIM-3 modulation may affect disease progression by influencing immune tolerance. Understanding TIM-3's role in these contexts aids in developing targeted therapies such as anti-TIM-3 antibodies to enhance immune responses in cancer while promoting tolerance in autoimmunity.
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Immobilized ab182714 at 0.2 μg/mL (100 μL/well) can bind Anti-TIM3 MAb, Human IgG4 with a linear range of 0.2-6 ng/mL.
Anti-Human TIM-3 MAb (human IgG4) captured on CM5 chip via Anti-Human IgG Fc antibodies surface, can bind ab182714 with an affinity constant of 9.7 nM as determined in a SPR assay.
DTT-reduced (+) SDS-PAGE analysis of ab182714, stained overnight with Coomassie Blue. The protein migrates as 45-50 kDa due to glycosylation.
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