Dimeric T Cell Receptor and Co-Receptors
Native-like Structure. Bioactive Performance. Reliable Results.
Conigen’s recombinant T-cell receptors (TCRs) and co-receptors, including CD3ε/δ (CD3 epsilon/delta) and CD4 mimic native structures to support studies of antigen recognition, receptor activation, and immunotherapy targeting.
TCRs are heterodimeric membrane proteins that initiate T-cell signaling through interaction with the CD3 complex (CD3ε, CD3δ, CD3γ, and CD3ζ dimers). These dimers are essential for stabilizing receptor structure and facilitating ITAM phosphorylation, which drives downstream immune signaling. Co-receptors such as CD4 enhance MHC binding and T-cell activation. Disrupting these dimer interfaces can weaken T-cell responses, while preserving them supports robust immune function and therapeutic modulation in oncology and autoimmune disease.
Spotlight: CD4
Bioactive Performance
CD4 is a co-receptor for the TCR and the primary receptor for HIV-1 entry. Conigen’s CD4 protein homodimer includes four Ig-like domains and mimics the native conformation, showing significantly enhanced binding to the HIV-1 envelope glycoprotein gp120 compared to monomeric forms.
Human CD4 protein homodimer, His-Tag (CSP-24004) potently binding to HIV-1 envelope glycoprotein gp120-JR-FL as measured by ELISA. The CD4 dimer (0.2 μg/ml) was coated on 96-well microtiter plates and detected by serial dilutions of gp120 protein.
This recombinant protein supports studies in HIV pathogenesis, immunology, and receptor-ligand interactions.