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CD3 is a co-receptor for the T cell receptor (TCR), a cell surface receptor that recognizes antigens presented by MHC molecules and has a key role in the adaptive immune response.1,2 CD3 exists as a dimer composed of γ, δ, ε, or ζ subunits, which are type I transmembrane proteins encoded by distinct genes that enable TCR signal transduction.1,3 CD3ε is composed of an extracellular immunoglobulin (Ig) domain that mediates protein-protein interactions, a short membrane-proximal connecting peptide that is critical for TCR signaling, a transmembrane segment, and an intracellular immunoreceptor tyrosine-based activation motif (ITAM) that is phosphorylated by the tyrosine kinase Lck, resulting in T cell activation, proliferation, and survival.1,2,4 CD3ε forms heterodimers with CD3γ or CD3δ that interact with CD3ζζ homodimers to generate CD3 hexamers that noncovalently bind the TCR to form the CD3-TCR complex. Formulations containing murine anti-CD3ε IgG2a monoclonal antibodies have been used in the treatment of acute allograft rejection. Cayman's CD3ε (C-Term) Rabbit Monoclonal Antibody (Clone RM344) can be used for immunohistochemistry (IHC) and Western blot (WB) applications. The antibody recognizes the cytoplasmic domain of CD3ε from human samples.
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1. Structural basis of assembly of the human T cell receptor–CD3 complex. Nature 573(7775), 546-552 (2019).
2. Molecular architecture of the αβ T cell receptor–CD3 complex. Proc. Natl. Acad. Sci. USA 111(49), 17576-17581 (2014).
3. Assembly of the TCR/CD3 complex: CD3ɛ/δ and CD3ɛ/ɣ dimers associate indistinctly with both TCR ɑ and TCR β chains. Evidence for a double TCR heterodimer model. Eur. J. Immunol. 28(1), 12-21 (1998).
4. Ionic CD3−Lck interaction regulates the initiation of T-