Human CD137 / 4-1BB (His Tag) recombinant protein
CD137 (also known as 4-1BB) is a surface co-stimulatory glycoprotein originally described as present on activated T lymphocytes, which belongs to the tumor necrosis factor (TNF) receptor superfamily. It is expressed mainly on activated CD4+ and CD8+ T cells, and binds to a high-affinity ligand (4-1BBL) expressed on several antigen-presenting cells such as macrophages and activated B cells. Upon ligand binding, 4-1BB is associated with the tumor necrosis factor receptor–associated factors (TRAFs), the adaptor protein which mediates downstream signaling events including the activation of NF-kappaB and cytokine production. 4-1BB signaling either by binding to 4-1BBL or by antibody ligation delivers signals for T-cell activation and growth, as well as monocyte proliferation and B-cell survival, and plays an important role in the amplification of T cell-mediated immune responses. In addition, CD137 and CD137L are expressed in different human primary tumor tissues, suggesting that they may influence the progression of tumors. Crosslinking of CD137 on activated T cells has shown promise in enhancing anti-tumor immune responses in murine models, and agonistic anti-CD137 antibodies are currently being tested in phase I clinical trials.
Tumor necrosis factor receptor superfamily member 9
Protein short names
LY63; TNFRSF9; ILA; A930040I11RIK; MGC2172; AI325004; RP23-272N19.6; CD137; CDW137; AA408498; 4-1BB
TNFRSF9; CD137; ILA
A DNA sequence encoding the human 4-1BB extracellular domain (NP_001552.2) (Met 1-Gln 186) was fused with a polyhistidine tag at the C-terminus.
The recombinant human 4-1BB consists of 174 amino acids and has a calculated molecular mass of 18.8 kDa. By SDS-PAGE under reducing conditions, the apparent molecular mass of rh4-1BB is approximately 33-36 kDa due to glycosylation.
> 85 % as determined by SDS-PAGE
Human CD137 / 4-1BB / TNFRSF9 Protein (His Tag) SDS-PAGE
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