Activity has not been tested. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first.

TRAIL R2/DR5/TNFRSF10B Protein, Human, Recombinant (Avi & His), Biotinylated is expressed in HEK293 mammalian cells with C-Avi-6xHis tag. The predicted molecular weight is 18-25 KDa and the accession number is O14763.

Human

HEK293 Cells

ZTNFR9,Tumor Necrosis Factor Receptor Superfamily Member 10B,TRICK2,TRAIL-R2,TRAILR2,TRAIL Receptor 2,TNFRSF10B,TNF-Related Apoptosis-Inducing Ligand Receptor 2,KILLER,DR5,Death Receptor 5,CD262

Ile56-Glu182

Ile56-Glu182

Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Reconstitute the lyophilized protein in distilled water. The product concentration should not be less than 100 μg/ml. Before opening, centrifuge the tube to collect powder at the bottom. After adding the reconstitution buffer, avoid vortexing or pipetting for mixing.

Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.

TNFRSF10B is a member of the TNF-receptor superfamily, and contains an intracellular death domain. This receptor can be activated by tumor necrosis factor-related apoptosis inducing ligand (TNFSF10/TRAIL/APO-2L), and transduces apoptosis signal. The adapter molecule FADD recruits caspase-8 to the activated receptor and is required for the apoptosis mediated by TNFRSF10B. TNFRSF10B is expressed in a number of cell types, and to particularly high levels in lymphocytes and spleen. This single-pass transmembrane protein contains two cysteine-rich repeat units in its extracellular region, followed by a transmembrane segment and a cytoplasmic tail containing a typical “death domain”. TNFRSF10B expression is regulated by the tumor suppressor p53. It is also indicated that the activation of NF-kappa-B can be promoted by TNFRSF10B.