TRAIL R2/TNFRSF10B Protein, Human (Biotinylated, HEK293, His)

TRAIL R2/TNFRSF10B protein is the receptor of TNFSF10/TRAIL and recruits caspase-8 through FADD to initiate cell apoptosis. It forms the death-inducing signaling complex (DISC), activates caspases and mediates apoptosis. TRAIL R2/TNFRSF10B Protein, Human (Biotinylated, HEK293, His) is the recombinant human-derived TRAIL R2/TNFRSF10B protein, expressed by HEK293 , with C-His labeled tag. The total length of TRAIL R2/TNFRSF10B Protein, Human (Biotinylated, HEK293, His) is 127 a.a., with molecular weight of ~15.8 kDa.

The TRAIL R2/TNFRSF10B Protein functions as a receptor for the cytotoxic ligand TNFSF10/TRAIL. Upon ligand binding, the adapter molecule FADD recruits caspase-8 to the activated receptor, forming the death-inducing signaling complex (DISC), which triggers caspase-8 proteolytic activation and initiates the subsequent cascade of caspases, mediating apoptosis. Additionally, TRAIL R2/TNFRSF10B promotes the activation of NF-kappa-B and is essential for endoplasmic reticulum (ER) stress-induced apoptosis. In its monomeric state, it can interact with TRADD and RIPK1, and in the absence of stimulation, it interacts with BIRC2, DDX3X, and GSK3B. Stimulation of the receptor enhances interactions with BIRC2 and DDX3X, accompanied by their cleavage. Notably, TRAIL R2/TNFRSF10B can also interact with the HCMV protein UL141, preventing cell surface expression, where two TNFRSF10B monomers interact with a UL141 homodimer, and three TNFRSF10B molecules interact with TNFSF10 homotrimer. These intricate interactions underline the multifaceted role of TRAIL R2/TNFRSF10B in apoptotic and signaling pathways.

Human

HEK293

C-His

O14763 (I56-E182)

8795  [NCBI]

Approximately 15.8 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.