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Biotinylated Human TRAIL R2/DR5/TNFRSF10B Protein 4748

$525.00$1,750.00

Summary

  • Expression: HEK293
  • Functional: Yes (ELISA)
  • Amino Acid Range: Ile56-Glu182
Weight1 lbs
Dimensions9 × 5 × 2 in
product tag

C-His-Avi, also biotinylated

Biotinylated Human TRAIL R2/DR5/TNFRSF10B Protein 4748

protein
Size and concentration
100, 500µg and lyophilized
Form
Lyophilized
Storage Instructions
Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer
Shipped at ambient temperature.
Purity
> 95% as determined by Tris-Bis PAGE
target relevance
DR5, also called TRAIL R2, TRICK 2, TNFRSF10B, and MK is a type 1 TNF R superfamily, membrane protein which is a receptor for TRAIL (APO2 ligand). DR5 is a receptor for the cytotoxic ligand TNFSF10/TRAIL. 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.
Protein names
Tumor necrosis factor receptor superfamily member 10B (Death receptor 5) (TNF-related apoptosis-inducing ligand receptor 2) (TRAIL receptor 2) (TRAIL-R2) (CD antigen CD262)
Gene names
TNFRSF10B,TNFRSF10B DR5 KILLER TRAILR2 TRICK2 ZTNFR9 UNQ160/PRO186
Mass
47878Da
Function
FUNCTION: Receptor for the cytotoxic ligand TNFSF10/TRAIL (PubMed:10549288). The adapter molecule FADD 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. Promotes the activation of NF-kappa-B. Essential for ER stress-induced apoptosis. {ECO:0000269|PubMed:10542098, ECO:0000269|PubMed:10549288, ECO:0000269|PubMed:15322075}.
Subellular location
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
Tissues
TISSUE SPECIFICITY: Widely expressed in adult and fetal tissues; very highly expressed in tumor cell lines such as HeLaS3, K-562, HL-60, SW480, A-549 and G-361; highly expressed in heart, peripheral blood lymphocytes, liver, pancreas, spleen, thymus, prostate, ovary, uterus, placenta, testis, esophagus, stomach and throughout the intestinal tract; not detectable in brain.
Structure
SUBUNIT: Monomer (PubMed:10549288). Can interact with TRADD and RIPK1. Interacts with HCMV protein UL141; this interaction prevents TNFRSF10B cell surface expression. Two TNFRSF10B monomers interact with a UL141 homodimer. Three TNFRSF10B molecules interact with TNFSF10 homotrimer (PubMed:10549288). In the absence of stimulation, interacts with BIRC2, DDX3X and GSK3B. The interaction with BIRC2 and DDX3X is further enhanced upon receptor stimulation and accompanied by DDX3X and BIRC2 cleavage (PubMed:18846110). {ECO:0000269|PubMed:10549288, ECO:0000269|PubMed:18846110, ECO:0000269|PubMed:23498957, ECO:0000269|PubMed:23555243}.
Post-translational modification
PTM: (Microbial infection) Glycosylated on Arg residue by S.typhimurium protein Ssek3. {ECO:0000269|PubMed:30902834}.
Domain
TOPO_DOM 5
Target Relevance information above includes information from UniProt accession : O14763
The UniProt Consortium

Data

ELISA with Biotinylated Human TRAIL R2/DR5/TNFRSF10B Protein
Immobilized Biotinylated Human TRAIL R2, His Tag at 0.5µg/ml (100µl/Well) on the streptavidin precoated plate (5µg/ml). Dose response curve for Anti-TRAIL R2 Antibody, hFc Tag with the EC50 of 5.8ng/ml determined by ELISA.
HPLC of Biotinylated Human TRAIL R2/DR5/TNFRSF10B Protein
The purity of Biotinylated Human TRAIL R2 is greater than 95% as determined by SEC-HPLC.
SDS-PAGE gel of Biotinylated Human TRAIL R2/DR5/TNFRSF10B Protein
Biotinylated Human TRAIL R2 on Tris-Bis PAGE under reduced conditions. The purity is greater than 95%.

Publications

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.




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