Skip to Content
MilliporeSigma
All Photos(1)

Key Documents

View All Documentation

T9701

Sigma-Aldrich

TRAIL human

recombinant, expressed in E. coli, ≥98% (SDS-PAGE and HPLC), lyophilized powder

Synonym(s):

Apo2 Ligand, Apo2L, TL2, TNF-related apoptosis-inducing ligand

Sign Into View Organizational & Contract Pricing
All Photos(1)

About This Item

CAS Number:
2244730-93-4
MDL number:
MFCD01867158
UNSPSC Code:
12352200
NACRES:
NA.32

biological source

human

Quality Level

200

recombinant

expressed in E. coli

description

extracellular domain

assay

≥98% (SDS-PAGE and HPLC)

form

lyophilized powder

mol wt

19.6 kDa
predicted mol wt ~21 kDa

technique(s)

immunofluorescence: suitable

impurities

endotoxin, tested

UniProt accession no.

P50591

storage temp.

−20°C

Gene Information

human ... TNFSF10(8743)

Looking for similar products? Visit Product Comparison Guide

Application

Human TRAIL can be used as a selection agent for treating human cells for phenotypic enrichments. The product can also be used in chemical transfection for identifying Small RNA Modulators of TRAIL-Induced Apoptosis Pathway by utilizing libraries of synthetic small interfering RNA (siRNA) and microRNAs (miRNA).
TRAIL human has been used in immunofluorescence analyses, to study the delocalization of melanoma antigen-D2 in the nucleoplasm after a cellular stress.

Biochem/physiol Actions

TNF-related apoptosis-inducing ligand (TRAIL) is a type II transmembrane protein that belongs to TNF family. The product present in both soluble as well as membrane-bound form, can induce rapid apoptosis of various transformed cell lines but not the normal cells. Additionally, the product can also induce apoptotic cell death in TRAIL-sensitive U343MG cells.
TRAIL is a cytokine with anti-inflammatory, and antitumor activity. It is expressed in various cells including immune cells, vascular cells and adipocytes. TRAIL is associated with vascular endothelial cell protection.
Type II transmembrane protein of the TNF superfamily. Ligand for apoptosis-inducing death receptors DR4 and DR5, decoy receptors DcR1 and DcR2, and osteoprotegerin. Approximately 28% amino acid sequence identity to FAS ligand. Human and mouse TRAIL share 65% sequence identity.

Physical form

Lyophilized from phosphate buffered saline

Analysis Note

The biological activity is determined by its ability to induce apoptotic cell death in TRAIL-sensitive LN-18 cells.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Customers Also Viewed

Slide 1 of 2

1 of 2

Tumor Necrosis Factor-α human TNF-α, recombinant, expressed in E. coli, powder, suitable for cell culture

Sigma-Aldrich

T6674

Tumor Necrosis Factor-α human

2-Deoxy-D-glucose ≥98% (GC), crystalline

Sigma-Aldrich

D8375

2-Deoxy-D-glucose

Fatih Birtekocak et al.
Iranian journal of pharmaceutical research : IJPR, 20(2), 45-56 (2021-09-28)
Colon cancer is one of the most prominent causes of cancer-related morbidity and mortality and curable if detected in the early stages. TNF-related apoptosis-inducing ligand (TRAIL) is a therapeutic protein and has a potential anti-cancer activity that is widely used
Lower maternal serum tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) levels in early preeclampsia. A retrospective study
Morano D, et al.
Pregnancy hypertension, 12, 1-5 (2018)
Synergistic effect of TRAIL and irradiation in elimination of glioblastoma stem-like cells
Liu J, et al.
Clinical and Experimental Medicine, 1-13 (2018)
Melanoma antigen-D2: a nucleolar protein undergoing delocalization during cell cycle and after cellular stress
Pirlot C, et al.
Biochimica et Biophysica Acta - Molecular Cell Research, 1863(4), 581-595 (2016)
Jan E Carette et al.
Nature biotechnology, 29(6), 542-546 (2011-05-31)
Insertional mutagenesis in a haploid background can disrupt gene function. We extend our earlier work by using a retroviral gene-trap vector to generate insertions in >98% of the genes expressed in a human cancer cell line that is haploid for
View All Related Papers

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service