CD96
CD96 (TACTILE, T-cell activation increased late expression) is an immunoglobulin superfamily receptor that emerged as an inhibitory checkpoint controlling NK-cell function. CD96 is a type I transmembrane glycoprotein with three extracellular Ig-like domains expressed on T cells (transiently on activated CD8+ T cells) and constitutively on NK cells and NKT cells. Its principal ligand is CD155 (PVR/necl-5), shared competitively with the activating receptor DNAM-1 (CD226) and the inhibitory receptor TIGIT; a second ligand is CD111 (nectin-1). Through its ITIM-like cytoplasmic motif, CD96 attenuates NK-cell and CD8+ T-cell cytotoxicity and interferon-γ production, restricting immunopathology during viral infection, while the DNAM-1-CD96-TIGIT balance dictates NK-cell education. CD96 blockade in preclinical cancer models enhances NK-cell-mediated tumor control, particularly in combination with TIGIT or PD-1 inhibition, positioning CD96 as an emerging immuno-oncology target. CD96 also participates in NK-cell adhesion to endothelial cells via interaction with CD155 during diapedesis.
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CD96 Protéines Recombinantes (7)
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Recombinant Protein Expression Service
- Codon Optimization
- Gene Synthesis
- Construction of Expression Vector
- Strain Screening
- Protein Expression
- Purification & QC
- Protein Delivery
- Formule: Human
- Masse moléculaire: Sf9 insect cells
The EpCAM/TROP1 protein serves as an important homogeneous interacting molecule that promotes direct contact between intestinal epithelial cells (IEC) and intraepithelial lymphocytes (IEL) in the mucosal epithelium. This feature helps establish an immune barrier against mucosal infections. EpCAM/TROP1 Protein, Human (His-SUMO) is the recombinant human-derived EpCAM/TROP1 protein, expressed by E. coli , with N-6*His, N-SUMO labeled tag.
