Recombinant Mouse Hepatitis A Virus Cellular Receptor 2 Homolog (HAVCR2) Protein (hFc), Active

Name: Recombinant Mouse Hepatitis A Virus Cellular Receptor 2 Homolog (HAVCR2) Protein (hFc), Active
Brand: Beta LifeScience
SKU: BLC-05619P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Mouse Hepatitis A Virus Cellular Receptor 2 Homolog (HAVCR2) Protein (hFc), Active is produced by our Mammalian cell expression system. This is a extracellular protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Endotoxin	Less than 1.0 EU/μg as determined by LAL method.
Activity	The ED50 as determined by its ability to bind Human Galectin 9 in functional ELISA is less than 20 ug/ml.
Uniprotkb	Q8VIM0
Target Symbol	HAVCR2
Synonyms	Havcr2; Tim3; Timd3; Hepatitis A virus cellular receptor 2 homolog; HAVcr-2; T-cell immunoglobulin and mucin domain-containing protein 3; TIMD-3; T-cell immunoglobulin mucin receptor 3; TIM-3; T-cell membrane protein 3; CD antigen CD366
Species	Mus musculus (Mouse)
Expression System	Mammalian cell
Tag	C-hFc
Complete Sequence	RSLENAYVFEVGKNAYLPCSYTLSTPGALVPMCWGKGFCPWSQCTNELLRTDERNVTYQKSSRYQLKGDLNKGDVSLIIKNVTLDDHGTYCCRIQFPGLMNDKKLELKLDIKAAKVTPAQTAHGDSTTASPRTLTTERNGSETQTLVTLHNNNGTKISTWADEIKDSGETIR
Expression Range	20-191aa
Protein Length	Extracellular Domain
Mol. Weight	46.3 kDa
Research Area	Immunology
Form	Lyophilized powder
Buffer	Lyophilized from a 0.2 μm filtered 1xPBS, pH 7.4
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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. Regulates macrophage activation. Inhibits T-helper type 1 lymphocyte (Th1)-mediated auto- and alloimmune responses and promotes immunological tolerance. 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. In contrast, shown to activate TCR-induced signaling in T-cells probably implicating ZAP70, LCP2, LCK and FYN. Expressed on Treg cells can inhibit Th17 cell responses. Receptor for LGALS9. 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. However, the function as receptor for LGALS9 has been challenged. Also reported to enhance CD8+ T-cell responses to an acute infection such as by Listeria monocytogenes. 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. Can enhance mast cell production of Th2 cytokines Il-4, IL-6 and IL-13. Expressed on natural killer (NK) cells acts as a coreceptor to enhance IFN-gamma production in response to LGALS9. In contrast, shown to suppress NK cell-mediated cytotoxicity. Negatively regulates NK cell function in LPS-induced endotoxic shock.
Subcellular Location	[Isoform 1]: Membrane; Single-pass type I membrane protein. Cell junction.; [Isoform 2]: Secreted.
Protein Families	Immunoglobulin superfamily, TIM family
Database References	KEGG: mmu:171285 STRING: 10090.ENSMUSP00000020668 UniGene: PMID: 29316433 Here, the authors demonstrate that Tim-3 inhibits macrophage phagocytosis of Listeria monocytogenes by inhibiting the nuclear erythroid 2-related factor 2 (Nrf2) signaling pathway and increases bacterial burden. PMID: 28205579 Studied role of Tim-3 role's in T cell activation using a chronic disease model. Results showed a major function of Tim-3 is to enhance T cell activation during either acute or chronic viral infection, and that Tim-3 is not required for the development of T cell exhaustion. PMID: 29463725 the data suggested that Tim-3 played a crucial role in the macrophage polarization and brain inflammation following intracerebral hemorrhage PMID: 29107214 Tim-3 might contribute to successful pregnancy by restraining Th1 bias PMID: 29083087 synergism in cell death by Caspase-1- and RipK3 resulted in restriction of PD-1 and TIM3 expression on primed CD8(+) T cells, which promoted the survival of activated CD8(+) T cells. PMID: 28686578 these findings reveal a critical role for Tim-3-Gal-9 signaling-mediated immunoregulation by pNK cells in maternal-fetal immune tolerance and suggest that Tim-3 abundance on pNK cells is a potential biomarker for recurrent miscarriage diagnosis. PMID: 28951537 Tim-3 and PD-1 pathways play critical roles in regulating CD8(+) T cell function and maintaining normal pregnancy. PMID: 28331165 CB2R may have a crucial neuroprotective role following HI insult through the modulation of the inflammatory-related HIF-1alpha/TIM-3 signalling pathway in microglia PMID: 28253997 Our results show that Tim-3 is a critical negative regulator of NLRP3 inflammasome and provides a potential target for intervention of diseases with uncontrolled inflammasome activation. PMID: 28799242 demonstrated that both IL-10 and TGF-beta upregulated TIM-3 surface expression on dendritic cells via a common signaling pathway that involved sequential activation of c-Src and Bruton's tyrosine kinase PMID: 27439518 Methylation level of the TIM-3 promoter gradually decreased after each round of T-cell polarization, and this decrease was inversely correlated with TIM-3 expression. PMID: 26890332 in mice, TIM-3 is not essential for development of HDM-induced acute or chronic allergic airway inflammation, although it appears to be involved in reduced lymphocyte recruitment during HDM-induced chronic allergic airway inflammation. PMID: 27209052 Authors found that a CD8(+) T-cell population with age-associated exhaustion was distinguishable by its expression of Tim-3. PMID: 26750587 TIM4 binds TIM3 on the surface of polarized Th1 cells to induce Th1 cell apoptosis, which may contribute to the development of Th2-dominant immune disorders. PMID: 26403707 decreases immunological rejection during composite tissue allotransplantation PMID: 26561949 The Gal-9/Tim-3 signal is important for the regulation of decidua NK cells function, which is beneficial for the maintenance of a normal pregnancy. PMID: 25578313 TIM-3 expression by NK cells and gamma/delta T cells is similar in the peripheral and decidual immune cells from pregnant mice. PMID: 26278059 Tim-3 acts at a receptor-proximal point to enhance Lyn kinase-dependent signaling pathways that modulate both immediate-phase degranulation and late-phase cytokine production downstream of FcepsilonRI ligation. PMID: 26598760 Our data indicate that Tim-3 expression on NK cells is regulated by T-bet, and that Tim-3 levels correlate with advanced stages of gastric cancer PMID: 26214042 TIM-3 plays a role in regulating the uterine natural killer cells and contributes to the maintenance of tolerance at the feto-maternal interface. PMID: 25897749 TIM-3 is highly expressed in hypoxic brain regions of a mouse cerebral hypoxia-ischaemia (H/I) model. TIM-3 is distinctively upregulated in activated microglia and astrocytes in a HIF-1-dependent manner. PMID: 25790768 These data identify an IL-27/NFIL3 signalling axis as a key regulator of effector T-cell responses via induction of Tim-3, IL-10 and T-cell dysfunction. PMID: 25614966 CD4+ T cell-dependent "negative" TIM-3 costimulation is essential for hepatic homeostasis and resistance against IR stress in OLTs PMID: 25676534 In DSS colitis, Tim-3 inhibited the polarization of pathogenic pro-inflammatory M1 macrophages, while Tim-3 downregulation or blockade resulted in an increased M1 response. Tim-3 effect on macrophage response may be TLR4 dependent. PMID: 26208474 These data suggest that Tim-3 and IFN-gamma may play a regulatory role in T. gondii-infected pregnant mouse model. PMID: 25270237 Gal-9, a natural TIM-3 ligand, was produced primarily by and released from ischemia-reperfusion-stressed hepatocytes, both in vivo and in vitro. PMID: 25450716 HCC conditioned medium or transforming growth factor-beta fostered Tim-3 expression and the alternative activation of macrophages. PMID: 25608525 Tim-3 induces Th2-biased immunity and macrophage activation during Schistosoma japonicum infection. PMID: 25987707 The Tim-3 pathway plays an inhibitory role in natural killer cell function. PMID: 25337993 Specific antigen-presenting cell subsets and the inhibitory receptor Tim-3 may contribute to CD8+ T cell impairment in metapneumovirus pathogenesis. PMID: 25653440 Tim-3 modulates microglia activity and regulates the interaction of microglia-neural cells. PMID: 25557503 The TIM-3 pathway ameliorates Theiler's murine encephalomyelitis virus-induced demyelinating disease. PMID: 24486565 CEACAM1 serves as a heterophilic ligand for TIM-3 that is required for its ability to mediate T-cell inhibition, and this interaction has a crucial role in regulating autoimmunity and anti-tumour immunity PMID: 25363763 Tim-3 is widely involved in the physiopathology of sepsis by regulating innate and adaptive immune responses. Blockade of the Tim-3 pathway or decreased Tim-3 expression may exacerbate sepsis by increasing immune deviation and immunosuppression in vivo. PMID: 24945079 Tim-3 signaling pathway acts as a novel negative mediator in LPS-induced endotoxic shock and could be a potential therapeutic target for the treatment of sepsis. PMID: 24561184 These results demonstrate an essential role for Btk-c-Src signaling in TIM-3-induced DC suppression. PMID: 25172495 The increased expression of IL-17 and Tim-3 in BALF. PMID: 23904364 Tim-3/galectin-9 pathway plays a critical role in the homeostasis of hepatic Tregs through the elimination induction in Teffs and the inhibition of IFN-gamma release. PMID: 24333756 Our findings demonstrate that Tim-3 plays an important role in brain inflammation after intracerebral hemorrhage PMID: 24289479 Data indicate that the absence of T cell Ig and mucin domain (Tim) 3 (Tim-3) expression impairs CD8 T cell responses to Listeria monocytogenes infection. monocytogenes PMID: 24567532 results indicate that the Tim-3 pathway is highly involved in the regulation of asthma; targeting Tim-3 by siRNA may hold therapeutic potential in preventing the development of allergic asthma PMID: 23232962 These data indicate that Tim-3 may be involved in the process of toxoplasmic encephalitis in mice infected with the Toxoplasma gondii Pru strain. PMID: 23595213 Anti-Tim-3 treatment augments atherosclerosis lesion development, accompanied by an increase in the number of monocytes/macrophages and CD4(+) T cells and by decreased regulatory T cells and regulatory B cells. PMID: 23990206 These results indicate that the therapeutic efficacy of targeting Tim-3 in experimental autoimmune encephalomyelitis is dependent on the nature of the effector T cells contributing to the disease. PMID: 23562810 Up-regulated expression of Tim-3 on T cells after burn injury plays an important role in the development and maintenance of burn-induced T cell immune suppression. PMID: 22038354 In the liver Tim-3+ natural killer {NK)T cells are in an activated state, and Gal-9 directly induces Tim-3+ NKT cell apoptosis and contributes to the depletion of NKT cells in diet-induced steatosis. PMID: 23296703 T-cell Ig mucin-3 (Tim-3) and its ligand, galectin 9 (Gal-9), were significantly decreased in dextran sodium sulfate-induced colitis PMID: 23117395 Deletion of the terminal cytoplasmic domain of Tim3 potentiates its ability to downregulate cytotoxic lymphocytes (Tc1) inflammation; this enhanced Tim3 activity is associated with decreased phosphorylation of the T cell receptor-CD3zeta-chain. PMID: 22875804 TIM-3 circumvents the stimulatory effects of nucleic acids in tumor immunity by interactding with HMGB1 to interfere with the recruitment of nucleic acids into dendritic cell endosomes PMID: 22842346

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

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Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

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