This protein carries an Avi tag (Avitag™) at the C-terminus, followed by a polyhistidine tag.
The protein has a calculated MW of 16.9 kDa. The protein migrates as 22 kDa and 24 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
Biotinylation of this product is performed using Avitag™ technology. Briefly, the single lysine residue in the Avitag is enzymatically labeled with biotin.
The biotin to protein ratio is 0.5-1 as determined by the HABA assay.
Less than 1.0 EU per μg by the LAL method.
>90% as determined by SDS-PAGE.
Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally trehalose is added as protectant before lyophilization.
Contact us for customized product form or formulation.
Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:
-20°C to -70°C for 12 months in lyophilized state;
-70°C for 3 months under sterile conditions after reconstitution.
Biotinylated Human TRAIL R2, Avitag,His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 90%.
Immobilized Human TRAIL, Mouse IgG2a Fc Tag (Cat. No. TRL-H5259) at 10 μg/mL (100 μL/well) can bind Biotinylated Human TRAIL R2, Avitag,His Tag (Cat. No. TR2-H82E6) with a linear range of 2-78 ng/mL (QC tested).
Tumor necrosis factor receptor superfamily member 10B (TNFRSF10B) is also known as TNF-related apoptosis-inducing ligand receptor 2 (TRAILR2), Death receptor 5 (DR5), CD262, KILLER, is a member of the TNF-receptor superfamily, and contains an intracellular death domain. TNFRSF10B / DR-5 is widely expressed in adult and fetal tissues; very highly expressed in tumor cell lines. TRAILR2 / CD262 / DR5 is the receptor for the cytotoxic ligand TNFSF10/TRAIL. The adapter molecule FADD (a death domain containing adaptor protein) of TRAIL-R2 / TNFRSF10B recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. CD262 / DR5 Promotes the activation of NF-kappa-B. DR5 is essential for ER stress-induced apoptosis and is regulated by p53/TP53.