Rhesus CD3e/CD3 epsilon (His Tag) recombinant protein

Rhesus CD3e/CD3 epsilon (His 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; FLJ18683; T3E; TCRE; CD3-EPSILON; IMD18; AI504783; CD3EPSILON; CD3

G7NCB9

Human Cells

A DNA sequence encoding the rhesus CD3E (XP_001097204.1) CD3E extracellular domain (Met 1-Asp 117) was fused with a polyhistidine tag at the C-terminus.

Rhesus

The recombinant rhesus CD3E consists of 107 amino acids and has a calculated molecular mass of 12.3 kDa.

> 96 % as determined by SDS-PAGE