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TIGIT encodes a member of the PVR (poliovirus receptor) family of immunoglobin proteins. Additionally we are shipping TIGIT Antibodies (51) and TIGIT Proteins (47) and many more products for this protein.
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Our data provide important structural and biochemical determinants responsible for the recognition of nectin-2 (show PVRL2 ELISA Kits) by TIGIT.
TIGIT is a powerful negative regulator of CD4 (show CD4 ELISA Kits)(+) T cells in systemic lupus erythematosus.
TIGIT signaling in NK cells after MDSC coculture led to a decrease in the phosphorylation of ZAP70 (show ZAP70 ELISA Kits)/Syk (show SYK ELISA Kits) and ERK1/2 (show MAPK1/3 ELISA Kits).
energetic basis for the TIGIT/nectin-2 (show PVRL2 ELISA Kits) interaction and revealed that an "aromatic key" of nectin-2 (show PVRL2 ELISA Kits) is critical for this interaction, whereas variations in the lock were tolerated.
TIGIT-positive circulating follicular helper T cells display robust B-cell help functions: potential role in sickle cell alloimmunization.
implying that TIGIT exerts immunosuppressive effects by competing with DNAM-1 (show CD226 ELISA Kits) for the same ligand, CD155 (show PVR ELISA Kits)
These findings identify TIGIT as a novel marker of dysfunctional HIV-specific T cells
This study shows that HBZ (show HBZ ELISA Kits)-induced TIGIT plays a pivotal role in attenuating host immune responses and shaping a microenvironment favorable to human T-cell leukemia virus type 1.
a novel mechanism that links TIGIT expression with NK-cell functional heterogeneity, and this mechanism might partially explain why individuals have different susceptibilities to infection, autoimmune disease, and cancer.
Human regulatory T cells expressing the receptors TIGIT and CD226 (show CD226 ELISA Kits) display widely divergent phenotypes in regard to expansion and activation.
study provides evidence that TIGIT expression by Th cells and its interaction with CD155 (show PVR ELISA Kits) enhances Th2 responses, and blockade of TIGIT is therapeutic for experimental allergic airway inflammation
TIGIT negatively regulates inflammation by altering macrophage phenotype.
TIGIT signaling in Tregs directs their phenotype. It suppresses antitumor immunity via Tregs and not CD8 (show CD8A ELISA Kits)+ T cells. TIGIT+ Tregs upregulated TIM-3 (show HAVCR2 ELISA Kits) expression in tumor tissue. TIM-3 (show HAVCR2 ELISA Kits) and TIGIT synergized to suppress antitumor immune responses.
TIGIT is a safeguard molecule to improve liver regeneration through negatively regulating NK-hepatocyte crosstalk.
Findings suggest that TIGIT is a key checkpoint inhibitor of chronic antiviral and antitumor responses through impairing CD226 (show CD226 ELISA Kits) function when disrupting its homodimerization.
TIGIT/PVR (show PVRL2 ELISA Kits) ligation signaling mediates suppression of IFN-gamma (show IFNG ELISA Kits) production via the NF-kappaB (show NFKB1 ELISA Kits) pathway.
expressed on a Treg cell subset that selectively suppresses Th1 (show HAND1 ELISA Kits) and Th17 cells but not Th2 cells
found that TIGIT was up-regulated selectively on NK cells and protected against liver injury in an acute adenovirus infection model in both an NK cell- and Kupffer cell-dependent manner
findings show that TIGIT is expressed by NK cells, that it interacts specifically with PVR (show PVRL2 ELISA Kits) and possibly with an additional unknown ligand found on PBMCs and that these interactions lead to the inhibition of NK-cell activities
This gene encodes a member of the PVR (poliovirus receptor) family of immunoglobin proteins. The product of this gene is expressed on several classes of T cells including follicular B helper T cells (TFH). The protein has been shown to bind PVR with high affinity\; this binding is thought to assist interactions between TFH and dendritic cells to regulate T cell dependent B cell responses.
T-cell immunoreceptor with Ig and ITIM domains
, V-set and immunoglobulin domain containing 9
, V-set and immunoglobulin domain-containing protein 9
, V-set and transmembrane domain containing 3
, V-set and transmembrane domain-containing protein 3
, Washington University cell adhesion molecule