Human TRAIL/TNFRSF10 Protein 4072

$315.00 – $1,050.00

Summary

Expression: E.coli
Functional: Yes (ELISA)
Amino Acid Range: Val114-Gly281

SKU: 4072parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	NP_003801
express system	E.coli
product tag	No Tag
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by SEC-HPLC
background	Tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) is a member of the TNF superfamily that can initiate the apoptosis pathway by binding to its associated death receptors DR4 and DR5. The activation of the TRAIL pathway in inducing tumor-selective apoptosis leads to the development of TRAIL-based cancer therapies, which include recombinant forms of TRAIL, TRAIL receptor agonists, and other therapeutic agents.
molecular weight	The protein has a predicted MW of 19.6 kDa same as Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Human TRAIL/TNFRSF10 Protein 4072

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
Tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) is a member of the TNF superfamily that can initiate the apoptosis pathway by binding to its associated death receptors DR4 and DR5. The activation of the TRAIL pathway in inducing tumor-selective apoptosis leads to the development of TRAIL-based cancer therapies, which include recombinant forms of TRAIL, TRAIL receptor agonists, and other therapeutic agents.
Protein names Tumor necrosis factor ligand superfamily member 10 (Apo-2 ligand) (Apo-2L) (TNF-related apoptosis-inducing ligand) (Protein TRAIL) (CD antigen CD253)
Protein family Tumor necrosis factor family
Mass 32509Da
Function Cytokine that binds to TNFRSF10A/TRAILR1, TNFRSF10B/TRAILR2, TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4 and possibly also to TNFRSF11B/OPG (PubMed:10549288, PubMed:26457518). Induces apoptosis. Its activity may be modulated by binding to the decoy receptors TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4 and TNFRSF11B/OPG that cannot induce apoptosis. {ECO:0000269\|PubMed:10549288, ECO:0000269\|PubMed:26457518}.
Subellular location Cell membrane {ECO:0000269\|PubMed:14609566}; Single-pass type II membrane protein {ECO:0000305}. Secreted {ECO:0000269\|PubMed:14609566}. Note=Exists both as membrane-bound and soluble form. {ECO:0000269\|PubMed:14609566}.
Tissues Widespread; most predominant in spleen, lung and prostate.
Structure Homotrimer (PubMed:26457518). One TNFSF10 homotrimer interacts with three TNFSF10A mononers (PubMed:26457518). One TNFSF10 homotrimer interacts with three TNFSF10B mononers (PubMed:10549288). {ECO:0000269\|PubMed:10549288, ECO:0000269\|PubMed:26457518}.
Post-translational modification Tyrosine phosphorylated by PKDCC/VLK. {ECO:0000269\|PubMed:25171405}.
Target Relevance information above includes information from UniProt accession: P50591
The UniProt Consortium

Data

Human DcR1, His Tag immobilized on CM5 Chip can bind Human TRAIL, No Tag with an affinity constant of 0.57 nM as determined in SPR assay (Biacore T200).

Immobilized Human TRAIL at 2µg/ml (100µl/Well) on the plate. Dose response curve for Human TRAIL R1, hFc Tag with the EC50 of 25.4ng/ml determined by ELISA (QC Test).

The purity of Human TRAIL is greater than 95% as determined by SEC-HPLC.

SDS-PAGE gel of Human TRAIL/TNFRSF10 Protein

Human TRAIL on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

pmid	title	authors	citation
We haven't added any publications to our database yet.

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.