TIGIT Antibody (Rabbit mAb) [J11M4]

Application: Reactivity: Human

Usage Information

Dilution
WB1:2000 IHC1:200 - 1:800 IF1:800 - 1:3200

Application
WB, IHC, IF

Reactivity
Human

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
26 kDa 18 kDa, 30-40 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
TIGIT Antibody (Rabbit mAb) [J11M4] detects endogenous levels of total TIGIT protein.

Clone
J11M4

Synonym(s)
FLJ39873; TIGIT; VSIG9; VSIG9, VSTM3; VSTM3; Washington University cell adhesion molecule; WUCAM

Background
T-cell immunoreceptor with Ig and ITIM domains (TIGIT) is an inhibitory immune checkpoint receptor of the poliovirus receptor (PVR) family that carries an extracellular immunoglobulin variable domain and a cytoplasmic tail containing an ITIM and an ITT‑like tyrosine motif, and it modulates T‑cell and NK‑cell responses through high‑affinity binding to CD155/PVR and lower‑affinity interactions with CD112 and CD113 on antigen‑presenting and tumor cells. TIGIT is expressed at low levels on resting CD4 and CD8 T cells and NK cells and is upregulated upon activation and chronic antigen exposure, where it marks exhausted or dysfunctional tumor‑infiltrating lymphocytes and contributes to the inhibitory receptor landscape that limits effector function in the tumor microenvironment and during chronic infections such as HIV. Ligand engagement by CD155 or CD112 triggers phosphorylation of the ITIM and ITT‑like motifs in the TIGIT cytoplasmic tail and recruits phosphatases and adaptor molecules that attenuate TCR and NK‑cell receptor signaling, reduce production of pro‑inflammatory cytokines including IFN‑γ and TNF‑α, and diminish cytotoxic granule release, leading to suppression of T‑cell activation and NK‑cell–mediated killing. TIGIT also exerts indirect regulatory effects by competing with the activating receptor CD226 for shared ligands such as CD155; higher TIGIT affinity and expression skew ligand binding toward inhibitory signaling and modify co‑stimulatory balance at the immunological synapse, thereby further dampening antitumor and antiviral responses. In cancer, TIGIT is consistently upregulated on CD8 tumor‑infiltrating lymphocytes, CD4 helper and regulatory T cells, and intratumoral NK cells, and TIGIT^high populations associate with poor survival across multiple tumor entities; functional studies show that blocking TIGIT restores proliferation, cytokine production and cytotoxicity of these lymphocytes and enhances recognition of tumor cells expressing CD155 and CD112. Preclinical models demonstrate that dual TIGIT and PD‑1 blockade produces synergistic effects, markedly increasing tumor antigen–specific CD8 T‑cell expansion and function and promoting rejection of established tumors more effectively than either monotherapy, supporting the rationale for clinical trials combining anti‑TIGIT with PD‑1/PD‑L1 inhibitors in solid and hematologic malignancies. TIGIT also contributes to immune regulation beyond cancer; its expression on regulatory T cells strengthens their suppressive activity, and TIGIT deficiency in autoimmune models leads to exaggerated inflammatory responses, highlighting a physiological role in maintaining immune homeostasis that must be considered when targeting this pathway.

Background

T-cell immunoreceptor with Ig and ITIM domains (TIGIT) is an inhibitory immune checkpoint receptor of the poliovirus receptor (PVR) family that carries an extracellular immunoglobulin variable domain and a cytoplasmic tail containing an ITIM and an ITT‑like tyrosine motif, and it modulates T‑cell and NK‑cell responses through high‑affinity binding to CD155/PVR and lower‑affinity interactions with CD112 and CD113 on antigen‑presenting and tumor cells. TIGIT is expressed at low levels on resting CD4 and CD8 T cells and NK cells and is upregulated upon activation and chronic antigen exposure, where it marks exhausted or dysfunctional tumor‑infiltrating lymphocytes and contributes to the inhibitory receptor landscape that limits effector function in the tumor microenvironment and during chronic infections such as HIV. Ligand engagement by CD155 or CD112 triggers phosphorylation of the ITIM and ITT‑like motifs in the TIGIT cytoplasmic tail and recruits phosphatases and adaptor molecules that attenuate TCR and NK‑cell receptor signaling, reduce production of pro‑inflammatory cytokines including IFN‑γ and TNF‑α, and diminish cytotoxic granule release, leading to suppression of T‑cell activation and NK‑cell–mediated killing. TIGIT also exerts indirect regulatory effects by competing with the activating receptor CD226 for shared ligands such as CD155; higher TIGIT affinity and expression skew ligand binding toward inhibitory signaling and modify co‑stimulatory balance at the immunological synapse, thereby further dampening antitumor and antiviral responses. In cancer, TIGIT is consistently upregulated on CD8 tumor‑infiltrating lymphocytes, CD4 helper and regulatory T cells, and intratumoral NK cells, and TIGIT^high populations associate with poor survival across multiple tumor entities; functional studies show that blocking TIGIT restores proliferation, cytokine production and cytotoxicity of these lymphocytes and enhances recognition of tumor cells expressing CD155 and CD112. Preclinical models demonstrate that dual TIGIT and PD‑1 blockade produces synergistic effects, markedly increasing tumor antigen–specific CD8 T‑cell expansion and function and promoting rejection of established tumors more effectively than either monotherapy, supporting the rationale for clinical trials combining anti‑TIGIT with PD‑1/PD‑L1 inhibitors in solid and hematologic malignancies. TIGIT also contributes to immune regulation beyond cancer; its expression on regulatory T cells strengthens their suppressive activity, and TIGIT deficiency in autoimmune models leads to exaggerated inflammatory responses, highlighting a physiological role in maintaining immune homeostasis that must be considered when targeting this pathway.

References
https://pubmed.ncbi.nlm.nih.gov/31828774/ https://pubmed.ncbi.nlm.nih.gov/35058314/

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%