TNFRSF10A Human
TNFRSF10A, TNF Receptor Superfamily Member 10a, Tumor Necrosis Factor Receptor Superfamily, Member 10a, TNF-Related Apoptosis-Inducing Ligand Receptor 1, Death Receptor 4, TRAIL Receptor 1, TRAIL-R1, TRAILR1, APO2, DR4, Tumor Necrosis Factor Receptor Superfamily Member 10a Variant 2, Tumor Necrosis Factor Receptor Superfamily Member 10A, Cytotoxic TRAIL Receptor, CD261 Antigen, TRAILR-1, CD261.
Greater than 90.0% as determined by SDS-PAGE.
Description
TNFRSF10A produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 224 amino acids (24-239a.a.) and having a molecular mass of 23.9kDa. TNFRSF10A is expressed with an 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Product Specs
TNFRSF10A, TNF Receptor Superfamily Member 10a, Tumor Necrosis Factor Receptor Superfamily, Member 10a, TNF-Related Apoptosis-Inducing Ligand Receptor 1, Death Receptor 4, TRAIL Receptor 1, TRAIL-R1, TRAILR1, APO2, DR4, Tumor Necrosis Factor Receptor Superfamily Member 10a Variant 2, Tumor Necrosis Factor Receptor Superfamily Member 10A, Cytotoxic TRAIL Receptor, CD261 Antigen, TRAILR-1, CD261.
ASGTEAAAAT PSKVWGSSAG RIEPRGGGRG ALPTSMGQHG PSARARAGRA PGPRPAREAS PRLRVHKTFK FVVVGVLLQV VPSSAATIKL HDQSIGTQQW EHSPLGELCP PGSHRSEHPG ACNRCTEGVG YTNASNNLFA CLPCTACKSD EEERSPCTTT RNTACQCKPG TFRNDNSAEM CRKCSRGCPR GMVKVKDCTP WSDIECVHKE SGNGHNLEHH HHHH
Product Science Overview
TRAIL-R1, also known as Death Receptor 4 (DR4), is a transmembrane receptor that plays a crucial role in mediating the apoptotic signals initiated by TRAIL. Upon binding with TRAIL, TRAIL-R1 undergoes a conformational change that allows it to recruit and activate downstream signaling molecules, leading to the activation of caspases and subsequent cell death .
The apoptotic signaling pathway initiated by TRAIL-R1 involves several key steps:
- Ligand Binding: TRAIL binds to TRAIL-R1 on the cell surface.
- Receptor Trimerization: The binding induces trimerization of TRAIL-R1, which is essential for signal transduction.
- DISC Formation: The trimerized receptor recruits adaptor proteins such as FADD (Fas-associated death domain) and procaspase-8 to form the death-inducing signaling complex (DISC).
- Caspase Activation: Within the DISC, procaspase-8 is cleaved to its active form, caspase-8, which then activates downstream effector caspases like caspase-3, leading to apoptosis .
Recombinant TRAIL-R1 is a laboratory-engineered version of the natural receptor, designed to study its function and potential therapeutic applications. By using recombinant technology, scientists can produce large quantities of TRAIL-R1 for research purposes, including structural analysis, drug screening, and therapeutic development .
The ability of TRAIL-R1 to selectively induce apoptosis in cancer cells while sparing normal cells makes it a promising target for cancer therapy. Recombinant TRAIL and TRAIL receptor agonists have been extensively studied for their potential to treat various cancers. Clinical trials have explored the use of recombinant TRAIL in combination with other chemotherapeutic agents to enhance its efficacy and overcome resistance mechanisms .
Despite its potential, the clinical application of TRAIL-R1-based therapies faces several challenges:
- Resistance: Some cancer cells develop resistance to TRAIL-induced apoptosis, necessitating the development of combination therapies or novel agonists.
- Immunomodulatory Effects: Recent studies have shown that recombinant TRAIL can also modulate the tumor immune microenvironment, influencing the efficacy of cancer immunotherapy .
- Optimization: Ongoing research aims to optimize the dosing and delivery of recombinant TRAIL to maximize its therapeutic benefits while minimizing side effects .
