TRAIL R2/TNFRSF10B 蛋白, Human

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 is the recombinant human-derived TRAIL R2/TNFRSF10B protein, expressed by E. coli , with tag free. The total length of TRAIL R2/TNFRSF10B Protein, Human is 132 a.a., with molecular weight of ~14.8 kDa.

TRAIL R2/TNFRSF10B 蛋白作为细胞毒性配体 TNFSF10/TRAIL 的受体发挥作用。配体结合后，接头分子 FADD 将 caspase-8 募集到激活的受体上，形成死亡诱导信号复合物 (DISC)，从而触发 caspase-8 蛋白水解激活并启动随后的 caspase 级联，介导细胞凋亡。此外，TRAIL R2/TNFRSF10B 促进 NF-kappa-B 的激活，对于内质网 (ER) 应激诱导的细胞凋亡至关重要。在单体状态下，它可以与 TRADD 和 RIPK1 相互作用，在没有刺激的情况下，它可以与 BIRC2、DDX3X 和 GSK3B 相互作用。受体的刺激增强了与 BIRC2 和 DDX3X 的相互作用，并伴随着它们的裂解。值得注意的是，TRAIL R2/TNFRSF10B 还可以与 HCMV 蛋白 UL141 相互作用，防止细胞表面表达，其中两个 TNFRSF10B 单体与 UL141 同二聚体相互作用，三个 TNFRSF10B 分子与 TNFSF10 同三聚体相互作用。这些复杂的相互作用强调了 TRAIL R2/TNFRSF10B 在细胞凋亡和信号传导途径中的多方面作用。

Measured by its ability to inhibit TRAIL-mediated cytotoxicity using L‑929 mouse fibroblast cells treated with TRAIL. The ED₅₀ for this effect is 5.9 ng/mL , corresponding to a specific activity is 1.69×10⁵ units/mg.

Human

E. coli

Tag Free

O14763 (E52-S183)

8795  [NCBI]

ESALITQQDLAPQQRAAPQQKRSSPSEGLCPPGHHISEDGRDCISCKYGQDYSTHWNDLLFCLRCTRCDSGEVELSPCTTTRNTVCQCEEGTFREEDSPEMCRKCRTGCPRGMVKVGDCTPWSDIECVHKES

Approximately 14.8 kDa

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

无菌粉末.

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.

<1 EU/μg; determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.