Recombinant Mouse DR5 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-1658

Recombinant Mouse DR5 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-1658
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Product Overview

Tag His
Host Species Mouse
Accession NP_064671.2
Background Tumor necrosis factor receptor superfamily, member 1b, official symbol TNFRSF1B, also known as Death receptor 5, CD262, TNF-related apoptosis-inducing ligand receptor 2 (TRAIL R2), 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 (TNFSF1/TRAIL/APO-2L), and transduces an apoptosis signal. Studies with FADD-deficient mice suggested that FADD, a death domain containing adaptor protein, is required for the apoptosis mediated by this protein. TRAIL R2/CD262/TNFRSF1B was purified independently as the only receptor for TRAIL detectable on the surface of two different human cell lines that undergo apoptosis upon stimulation with TRAIL. TRAIL R2/CD262/TNFRSF1B contains two extracellular cysteine-rich repeats, typical for TNF receptor (TNFR) family members, and a cytoplasmic death domain. TRAIL R2/CD262/TNFRSF1B mediates apoptosis via the intracellular adaptor molecule FADD/MORT1. TRAIL receptors can signal both death and gene transcription, functions reminiscent of those of TNFR1 and TRAMP, two other members of the death receptor family. Defects in TRAIL R2/CD262/TNFRSF1B may be a cause of head and neck squamous cell carcinomas (HNSCC) also known as squamous cell carcinoma of the head and neck.Immune CheckpointImmunotherapyCancer ImmunotherapyTargeted Therapy
Description A DNA sequence encoding the extracellular domain of mouse TNFRSF10B (NP_064671.2) (Met 1-Ser 177) was expressed, with a C-terminal His tag.
Source HEK293
Predicted N Terminal Asn 53
AA Sequence Met 1-Ser 177
Molecular Weight The secreted recombinant mouse TNFRSF10B consists of 136 a.a. and has a calculated molecular mass of 15 kDa. As a result of glycosylation, the apparent molecular mass of the recombinant protein is approximately 25-35 kDa in SDS-PAGE under reducing conditions.
Purity >95% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity 1. Immobilized mouse TNFRSF10B-His at 10 ug/ml (100 ul/well) can bind biotinylated human TNFSF10, The EC50 of biotinylated human TNFSF10 is 0.16-0.38 ug/ml.2. Measured by its ability to inhibit TRAIL-mediated cytotoxicity using L-929 mouse fibroblast cells treated with TRAIL. The ED50 for this effect is typically 0.5-2 ug/mL in the presence of 20 ng/ml Recombinant Human TRAIL/TNFSF10.
Formulation Lyophilized from sterile PBS, pH 7.4.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Receptor for the cytotoxic ligand TNFSF10/TRAIL. 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.
Subcellular Location Membrane; Single-pass type I membrane protein.
Database References
Tissue Specificity Highly expressed in heart, lung and kidney.

Gene Functions References

  1. Death receptor5 pathway and mitochondrial pathway, which are likely mediated by HIF-1alpha, contribute to hypoxia-induced spermatocyte apoptosis. PMID: 28444885
  2. downregulation of cIAPs in PSC cholangiocytes may contribute to the development of the disease. Our results also indicate that inhibition of TRAIL signaling pathways may be beneficial in the treatment of PSC PMID: 28055006
  3. Authors demonstrate, for the first time, expression of TNF-related apoptosis-inducing ligand (TRAIL) and its signaling death receptor 5 (DR5) in the murine inner ear. PMID: 26791792
  4. Malignant transformation in the endometrium is related to reduction of membrane DR4 and DR5 expression. PMID: 23815209
  5. TRAIL expression by osteoclast-like cells is increased in the presence of RANKL and after scraping; DcR2 expression peaks at 24 hours, and and decreases at 5 days; DR5 expression peaks at 5 days PMID: 23430714
  6. Induction of death receptor 5 expression in tumor vasculature by perifosine restores the vascular disruption activity of TRAIL-expressing CD34(+) cells. PMID: 23605004
  7. TRAIL-DR5 interaction promoted malignant behaviors of B16F10 cells. PMID: 23347256
  8. results suggest that the transmembrane domains together with their adjacent stalk regions can play a major role in control of death receptor activation thereby contributing to cell type specific differences in TRAILR1 and TRAILR2 signaling PMID: 22916132
  9. DR5 is selectively expressed by neuroprogenitor cells and newborn neurons. PMID: 21938487
  10. Results suggest that excessive iodine could induce TRAIL and DR5 abnormal expression in thyroid. TRAIL band with DR5 to promote follicular cells apoptosis thus mediate thyroid destruction in EAT. PMID: 21225479
  11. NK cells inhibit dendritic cell cross-priming, but not direct priming, in a TRAIL/DR5-dependent manner. PMID: 21832159
  12. Antibody-based therapy targeting DR5 is an efficient strategy not only to eliminate TRAIL-sensitive tumor cells. PMID: 14769851
  13. presence and function of TRAIL and MK, a death-inducing ligand and its receptor, in mammalian preimplantation embryos. PMID: 15128592
  14. binding of Fas-associated death domain (FADD) to the tumor necrosis factor-related apoptosis-inducing ligand receptor DR5 is regulated by the death effector domain of FADD PMID: 15173180
  15. Inactivation of the TRAIL-R gene did not affect tumorigenesis in the thymus and intestines of p53 knock-out mice and mice mutated in the Adenomatous Polyposis Coli gene, respectively. PMID: 15514675
  16. DR5 has a limited role during embryogenesis and early stages of development but plays an organ-specific role in the response to DNA-damaging stimuli. PMID: 15713653
  17. ceramide acts as a common mediator of caspase-independent programmed cell death caused by death receptors such as mTRAIL-R2 and TNF-R55 PMID: 17026999
  18. These data demonstrate an important role for the TRAIL/DR5/FADD/caspase 8 pathway in the apoptosis associated with skeletal myoblast differentiation. PMID: 17041756
  19. These data represent the first indication that testicular germ cells, specifically spermatocytes, can undergo TRAIL-mediated apoptosis. PMID: 17051329
  20. Thus, sDR5 represents a potential novel therapeutic drug for patients with fulminant hepatitis. PMID: 17126290
  21. cathepsin E plays a substantial role in host defense against tumor cells through TRAIL-dependent apoptosis and/or tumor-associated macrophage-mediated cytotoxicity PMID: 18006832
  22. Thus TRAIL-R may function as an inflammation and tumor suppressor in multiple tissues in vivo. PMID: 18079962
  23. adherent TRAIL-R-expressing skin carcinoma cells were TRAIL resistant in vitro but were sensitized to TRAIL upon detachment by inactivation of the ERK signaling pathway PMID: 18079967
  24. Death receptor 5 mediated-apoptosis contributes to cholestatic liver disease. PMID: 18667695
  25. Apoptosis in experimental non-alcoholic steatohepatitis is associated with p53 activation and TRAIL receptor expression. PMID: 19226377
  26. Data demonstrate that cytokine induced upregulation of TRAIL, DR4 and DR5 in tubules from patients with proliferative lupus nephritis may play a protective role by enhancing survival while also exerting a proinflammatory effect. PMID: 19349211


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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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