Recombinant Human TIM 3 protein (Tagged) (Biotin)
Be the first to review this product! Submit a review
|
(0 Publication)
Recombinant Human TIM 3 protein (Tagged) (Biotin) is a Human Fragment protein, in the 22 to 200 aa range, expressed in HEK 293 cells, with >90%, suitable for SDS-PAGE.
View Alternative Names
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
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human TIM 3 protein (Tagged) (Biotin) (AB271766)
SDS-PAGE analysis of 3 μg ab271766.
This protein runs at a higher MW by SDS-PAGE due to glycosylation.
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
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.
Pathways
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.
Specifications
Form
Liquid
General info
Function
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).
Sequence similarities
Belongs to the immunoglobulin superfamily. TIM family.
Post-translational modifications
O-glycosylated with core 1 or possibly core 8 glycans.. Phosphorylated on tyrosine residues; modestly increased after TCR/CD28 stimulation. Can be phosphorylated in the cytoplasmic domain by FYN (By similarity). Phosphorylation at Tyr-265 is increased by stimulation with ligand LGALS9.
Target data
Product promise
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com