Human CD3e/CD3 epsilon (His & Fc Tag) recombinant protein

Human CD3e/CD3 epsilon (His & Fc Tag) recombinant protein

• DataSheet
• Material Safety Data Sheets (MSDS)

T-cell surface glycoprotein CD3 epsilon chain, also known as CD3E, is a single-pass type I membrane protein. CD3E contains 1 Ig-like (immunoglobulin-like) domain and 1 ITAM domain. CD3E, together with CD3-gamma, CD3-delta and CD3-zeta, and the T-cell receptor alpha/beta and gamma/delta heterodimers, forms the T cell receptor-CD3 complex. The CD3 epsilon subunit of the T cell receptor (TCR) complex contains two defined signaling domains, a proline-rich sequence and an immune tyrosine activation motifs (ITAMs), and this complex undergoes a conformational change upon ligand binding that is thought to be important for the activation of T cells. In the CD3 epsilon mutant mice, all stages of T cell development and activation that are TCR-dependent were impaired, but not eliminated, including activation of mature naïve T cells with the MHCII presented superantigen, staphylococcal enterotoxin B, or with a strong TCR cross-linking antibody specific for either TCR-Cbeta or CD3 epsilon. T cell receptor-CD3 complex plays an important role in coupling antigen recognition to several intracellular signal-transduction pathways. This complex is critical for T-cell development and function, and represents one of the most complex transmembrane receptors. CD3E plays an essential role in T-cell development, and defects in CD3E gene cause severe immunodeficiency. Homozygous mutations in CD3D and CD3E genes lead to a complete block in T-cell development and thus to an early-onset severe combined immunodeficiency phenotype.

CD3E; T3E; FLJ18683; TCRE; AI504783; IMD18; CD3-EPSILON; CD3; CD3EPSILON

Human Cells

A DNA sequence encoding the human CD3E (Met 1-Asp126) was fused with the C-terminal polyhistidine-tagged Fc region of human IgG1 at the C-terminus.

Human

The secreted recombinant human CD3E is a disulfide-linked homodimeric protein. The reduced monomer comprises 355 amino acids and has a predicted molecular mass of 40 kDa. As a result of glycosylation, it migrates as an approximately 44-53 and 38 kDa band in SDS-PAGE under reducing conditions.

(84.6+14.1) % as determined by SDS-PAGE