Cynomolgus HVEM/TNFRSF14 (Fc Tag) recombinant protein

Cynomolgus HVEM/TNFRSF14 (Fc Tag) recombinant protein

• DataSheet
• Material Safety Data Sheets (MSDS)

Herpesvirus entry mediator (HVEM), also referred to as TNFRSF14, TR2 (TNF receptor-like molecule) and ATAR (another TRAF-associated receptor), is a member of type I transmembrane protein belonging to the TNF-receptor superfamily. It is expressed on many immune cells, including T and B cells, NK cells, monocytes, and neutrophils. Two TNF superfamily ligands lymphotoxin α (TNF-β) and LIGHT (TNFSF14) are identified as cellular ligands for HVEM and initiate the positive signaling. However, recent studies have revealed that HVEM is also involved in the unique inhibitory signaling pathway for T cells through activating tyrosine phosphorylation of the immunoreceptor tyrosine-based inhibitory motif (ITIM) in B and T lymphocyte attenuator (BTLA). HVEM provides a stimulatory signal following engagement with LIGHT (TNFSF14) on T cells. In contrast, it can also provide an inhibitory signal to T cells when it binds the B and T lymphocyte attenuator (BTLA), a ligand member of the Immunoglobulin (Ig) superfamily. Thus, HVEM may be viewed as a molecular switch, capable of facilitating both stimulatory and inhibitory cosignaling in T cells. Substantial evidence from both human disease and from experimental mouse models has indicated that dysregulation of the LIGHT-HVEM-BTLA cosignaling pathway can cause inflammation in the lung and in mucosal tissues.

RP3-395M20.6; RP24-89N4.1; TNFRS14; HVEM; MGC123499; TR2; HVEA; CD270; MGC123498; ATAR; TNFRSF14; LIGHTR

Human Cells

A DNA sequence encoding the cynomolgus TNFRSF14 (Met1-Arg201) was expressed with the Fc region of human IgG1 at the C-terminus.

Cynomolgus

The recombinant cynomolgus TNFRSF14 is a disulfide-linked homodimer. The reduced monomer comprises 404 amino acids and has a calculated molecular mass of 44.2 KDa. The apparent molecular mass of the protein is approximately 57 and 36 KDa respectively in SDS-PAGE.

(93.7+5.3) % as determined by SDS-PAGE