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TRAIL R-1/DR4, soluble

CAT: 0209-S01-035-L250Size: 250 µgDry Ice: NoHazardous: No
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CAT#:0209-S01-035-L250Size:250 µg
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Description
TRAIL Receptor-1/DR4 and TRAIL Receptor-2/DR5 belong to the TNFR superfamily of transmembrane proteins and contain a cytoplasmic "death domain, " which can activate the cell's apoptotic machinery. These receptors are activated by binding to either membrane anchored or soluble TRAIL/Apo2L. Recombinant human soluble TRAIL Receptor-1/DR4 is a 22.7 kDa protein (215 amino acid residues) consisting of the TNFR homologous, cysteine rich portion of the extracellular domain.
Synonyms
TNFRSF10A; DR4; APO2; CD261; TRAILR1; TRAILR-1
NCBI Gene ID
8797
UniProt
O00220
Accession Number
NP_003835.3
Accession Number mRNA
NM_003844.3
Chromosomal Location
8p21
Reactivity
Human
Cross Reactivity
Human
Sequence
MSGTGAAAAT PSKVWGSSAG RIEPRGGGRG ALPTSMGQHG PSARARAGRA PGPRPAREAS PRLRVHKTFK FVVVGVLLQV VPSSAATIKL HDQSIGTQQW EHSPLGELCP PGSHRSERPG ACNRCTEGVG YTNASQQLFA CLPCTACKSD EEERSPCTTT RNTACQCKPG TFRNDNSAEM CRKCSTGCPR GMVKVKDCTP WSDIECVHKE SGNGHN
Endotoxin
< 0.1 ng/µg of protein (< 1EU/µg)
Purity
> 98% by SDS-PAGE & HPLC analyses
Bioactivity
Measured by its ability to inhibit apoptosis in LN-18 cells. The expected ED50 for this effect is 0.4 -0.5 µg/ml.
Length
215
Form
Lyophilized
Molecular Weight
22.7 kDa
Host or Source
E. coli

UniProtKB · O00220

Tumor necrosis factor receptor superfamily member 10A

TR10A_HUMAN · Homo sapiens

View on UniProt ↗
Primary accession
O00220
Review status
UniProtKB reviewed (Swiss-Prot)
Gene
TNFRSF10A
Protein existence
1: Evidence at protein level
Organism
Homo sapiens (Human)
Taxonomy ID
9606
Alternative names
—
EC number
—
Processing
Precursor
Secondary accessions
A8K5I4, Q53Y72, Q96E62
Protein keywords

Technical term

3D-structureProteomics identificationReference proteome

Biological process

Apoptosis

Cellular component

Cell membraneCytoplasmMembrane

PTM

Disulfide bondGlycoproteinMethylationPhosphoprotein

Molecular function

Receptor

Domain

RepeatSignalTransmembraneTransmembrane helix