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 >  Protein>TRAIL R3 >TR3-H52H3

Human TRAIL R3 protein, His Tag (MALS verified)

分子别名(Synonym)

CD263, DCR1, DCR1-TNFR, LIT, TRAIL-R3, TRAILR3, TRID

表达区间及表达系统(Source)

Human TRAIL R3 protein, His Tag (TR3-H52H3) is expressed from human 293 cells (HEK293). It contains AA Ala 26 - Pro 235 (Accession # O14798).

Predicted N-terminus: Ala 26

Request for sequence

蛋白结构(Molecular Characterization)

TRAIL R3 Structure

This protein carries a polyhistidine tag at the C-terminus.

The protein has a calculated MW of 24 kDa. The protein migrates as 43-55 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE) due to glycosylation.

内毒素(Endotoxin)

Less than 1.0 EU per μg by the LAL method.

纯度(Purity)

>95% as determined by SDS-PAGE.

>90% as determined by SEC-MALS.

制剂(Formulation)

Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.

Contact us for customized product form or formulation.

重构方法(Reconstitution)

Please see Certificate of Analysis for specific instructions.

For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

存储(Storage)

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:

  1. -20°C to -70°C for 12 months in lyophilized state;
  2. -70°C for 3 months under sterile conditions after reconstitution.

质量管理控制体系(QMS)

  1. 质量管理体系(ISO, GMP)
  2. 质量优势
  3. 质控流程
 

电泳(SDS-PAGE)

TRAIL R3 SDS-PAGE

Human TRAIL R3 protein, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 95% (With Star Ribbon Pre-stained Protein Marker).

SEC-MALS

TRAIL R3 SEC-MALS

The purity of Human TRAIL R3 protein, His Tag (Cat. No. TR3-H52H3) is more than 90% and the molecular weight of this protein is around 35-50 kDa verified by SEC-MALS.

Report

 

活性(Bioactivity)-ELISA

TRAIL R3 ELISA

Immobilized Human TRAIL R3 protein, His Tag (Cat. No. TR3-H52H3) at 5 μg/mL (100 μL/well) can bind Human TRAIL, Mouse IgG2a Fc Tag (Cat. No. TRL-H5259) with a linear range of 0.008-0.5 μg/mL (QC tested).

Protocol

 
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背景(Background)

Tumor necrosis factor receptor superfamily member 10C (TNFRSF10C) is also known as Decoy receptor 1 (DcR1), TNF-related apoptosis-inducing ligand receptor 3 (TRAIL receptor 3 or TRAIL-R3), CD263. TNFRSF10C is a decoy receptor for TRAIL (tumor necrosis factor-related apoptosis-inducing ligand), a member of the tumor necrosis factor (TNF) ligand family. This receptor is not capable of inducing apoptosis (lacks a cytoplasmic death domain), and is thought to function as an antagonistic receptor that protects cells from TRAIL-induced apoptosis.

 

前沿进展

Synthesis of (S)-4-Methylgeranyl Esters, the Pheromone Components of the Ponerine Ant, Holcoponera striatula, and their (R)-Isomers
Tashiro, Watanabe
Biosci Biotechnol Biochem (2025)
Abstract: (2E,4S)-3,4,7-Trimethylocta-2,6-dien-1-yl octanoate [(S)-1], decanoate [(S)-2], and dodecanoate [(S)-3] are the main trail pheromone components of the Dufour's gland secretion of the ponerine ant, Holcoponera striatula. We synthesized these pheromone components from an optically active alcohol, (R)-5, by using Johnson-Claisen rearrangement reaction as the key step for constructing a methyl-branched alkyl chain. The alcohol (R)-5 was prepared by using the enzymatic resolution of its racemate. To investigate the biological activity of the enantiomers of these pheromone components, we synthesized the antipodes (R)-1, (R)-2, and (R)-3.© The Author(s) 2025. Published by Oxford University Press on behalf of Japan Society for Bioscience, Biotechnology, and Agrochemistry.
Apoptotic Receptors and CD107a Expression by NK Cells in an Interaction Model with Trophoblast Cells
Mikhailova, Sokolov, Grebenkina et al
Curr Issues Mol Biol (2024) 46 (8), 8945-8957
Abstract: Natural killer cells (NK cells) exert cytotoxicity towards target cells in several ways, including the expression of apoptosis-mediating ligands (TRAIL, FasL). In addition, NK cells themselves may be susceptible to apoptosis due to the expression of TRAIL receptors. These receptors include TRAIL-R1 (DR4), TRAIL-R2 (DR5), capable of inducing apoptosis, and TRAIL-R3 (DcR1), TRAIL-R4 (DcR2), the so-called "decoy receptors", which lack an intracellular domain initiating activation of caspases. Of particular interest is the interaction of uterine NK cells with cells of fetal origin, trophoblasts, which are potential targets for natural killer cells to carry out cytotoxicity. The aim of this work was to evaluate the expression of proapoptotic receptors and their ligands as well as CD107a expression by NK cells in a model of interaction with trophoblast cells. To evaluate NK cells, we used cells of the NK-92 line; cells of the JEG-3 line were used as target cells. The cytokines IL-1β, IL-15, IL-18, TNFα, IL-10, TGFβ and conditioned media (CM) of the first and third trimester chorionic villi explants were used as inducers. We established that cytokines changed the expression of apoptotic receptors by NK cells: in the presence of TNFα, the amount and intensity of Fas expression increased, while in the presence of TGFβ, the amount and intensity of expression of the DR5 receptor decreased. Soluble chorionic villi factors alter the expression of TRAIL and FasL by NK-92 cells, which can reflect the suppression of the TRAIL-dependent mechanism of apoptosis in the first trimester and stimulating the Fas-dependent mechanism in the third trimester. In the presence of trophoblast cells, the expression of TRAIL and DcR1 by NK cells was reduced compared to intact cells, indicating an inhibitory effect of trophoblast cells on NK cell cytotoxicity. In the presence of chorionic villi CM and trophoblast cells, a reduced number of NK-92 cells expressing DR4 and DR5 was found. Therefore, soluble factors secreted by chorionic villi cells regulate the resistance of NK cells to death by binding TRAIL, likely maintaining their activity at a certain level in case of contact with trophoblast cells.
Efficacy and safety of tetrandrine in treatment of rheumatoid arthritis: a meta-analysis
Xu, Li, Ye et al
Zhejiang Da Xue Xue Bao Yi Xue Ban (2024) 53 (4), 519-526
Abstract: To explore the efficacy and safety of tetrandrine in the treatment of rheumatoid arthritis.Randomized controlled studies of tetrandrine in the treatment of rheumatoid arthritis were searched in CNKI, VIP, Wanfang database, SinoMed, PubMed, Springer, Web of Science and Cochrane Central Register of Controlled Trails databases. A meta-analysis was conducted using R 3.5.3 software to evaluate the clinical outcomes, including the total effective rate, erythrocyte sedimentation rate (ESR), C-reactive protein (CRP), rheumatoid factor (RF), visual analogue scale (VAS), disease activity score (DAS), tender joint count (TJC), swollen joint count (SJC), and morning stiffness duration, as well as adverse events of rheumatoid arthritis patients.A total of 10 articles were included in the study. The meta-analysis indicated that tetrandrine significantly improved the total effective rate (OR=3.27, 95%CI: 2.01-5.37, P<0.01), ESR (SMD=1.12, 95%CI: 0.06-2.19, P<0.05), CRP (SMD=0.75, 95%CI: 0.28-1.22, P<0.01), VAS (SMD=0.64, 95%CI: 0.29-1.00, P<0.01), TJC (SMD=1.16, 95%CI: 0.58-1.74, P<0.01), SJC (SMD=0.85, 95%CI: 0.40-1.31, P<0.01), and morning stiffness (SMD=1.09, 95%CI: 0.68-1.50, P<0.01). However, no statistical significance was found in RF (SMD=1.70, 95%CI: -1.10-4.51, P>0.05) and DAS (SMD=0.26, 95%CI: -0.59-1.11, P>0.05). The overall incidence of adverse events associated with tetrandrine treatment for rheumatoid arthritis was 20% (95%CI: 12%-27%, I2=60%, P<0.05), with mild severity and favorable outcomes.Tetrandrine is effective in the treatment of RA patients with a mild degree of adverse events.
Mapping trends and hotspots regarding the use of telenursing for elderly individuals with chronic diseases: A bibliometric analysis
Yuan, Wang, Tao et al
Medicine (Baltimore) (2024) 103 (9), e37313
Abstract: Telenursing is receiving extensive attention from scholars and medical staff. However, there are few studies on the knowledge structure of telenursing for elderly individuals with chronic diseases. This study aims to demonstrate current research status and development trend of telenursing for elderly individuals with chronic diseases through a visual analysis of CiteSpace, so as to provide a more comprehensive perspective for future researches.Literature about telenursing for elderly patients with chronic diseases from 2002 to 2022 was retrieved from the Web of Science Core Collection using CiteSpace 6.1.R3.A total of 375 records were obtained. Annual publication and citation frequency gradually increased over the investigated period, reaching a peak in 2022. Journal of Telemedicine and Telecare was the most prolific and the most cited journal. The United States was the most productive country, the University of Melbourne was the most productive institution, and the author CHEN C ranked the highest in the number of publications. The most popular keywords were "care," "telemedicine," "management," "older adult," "chronic disease," "health," and "heart failure," which had a high frequency and centrality. The keywords "telehealth," "randomized controlled trail," "chronic obstructive pulmonary disease," "implementation" and "time" showed the strongest citation burst. The keywords were clustered to form 10 labels. The article published in 2010 by Chaudhry SI was cited the most. The top 3 cited journals were all special journal of telemedicine.This study revealed current research status and development trend of telenursing for elderly individuals with chronic diseases. The bibliometric analysis of telenursing expands the knowledge field of telemedicine and provides new insights into the management of elderly patients with chronic diseases.Copyright © 2024 the Author(s). Published by Wolters Kluwer Health, Inc.
Showing 1-4 of 170 papers.
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