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T5819

Sigma-Aldrich

TRAIL Receptor 2/Fc Chimera from mouse

>95% (SDS-PAGE), recombinant, expressed in baculovirus infected Sf21 cells, lyophilized powder

Synonym(s):

DR5, MK, TRICK2

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About This Item

MDL number:
UNSPSC Code:
12352200

recombinant

expressed in baculovirus infected Sf21 cells

assay

>95% (SDS-PAGE)

form

lyophilized powder

mol wt

~49 kDa by SDS-PAGE (reducing)
calculated mol wt ~40 kDa

impurities

endotoxin, tested

UniProt accession no.

storage temp.

−20°C

Gene Information

Application

TRAIL Receptor 2/Fc Chimera from mouse was used to study apoptosis induced by acetyl-keto-beta-boswellic acid isolated from Boswellia carterri and Boswellia serrata in prostate cancer cells via death receptor 5-mediated pathway.[1]

Biochem/physiol Actions

Member of the TNFR superfamily that binds TRAIL and induces apoptosis in a variety of cell types.
Member of the TNFR superfamily that binds TRAIL and induces apoptosis in a variety of cell types. The degree of homology between the death domains of mouse TRAIL R2 and either human TRAIL R1 or TRAIL R2 is 76% and 79%, respectively.
TRAIL Receptor 2 also refers as DR5 or TRICK2 belongs to TNF receptor family and can induce apoptosis via FADD and caspase-8. It also promotes NF-κ-B activation.[2]

Other Notes

Extracellular domain of mouse TRAIL R2 (a.a. 1-177) fused to the C-terminal Fc region of human IgG1.

Physical form

Lyophilized from a 0.2 μm filtered solution in phosphate buffered saline.

Analysis Note

Inhibits apoptosis of mouse L929 cells treated with 20 ng/ml recombinant human TRAIL or 12 ng/ml cross-linked recombinant human TRAIL.

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Min Lu et al.
Cancer research, 68(4), 1180-1186 (2008-02-19)
Acetyl-keto-beta-boswellic acid (AKBA), a triterpenoid isolated from Boswellia carterri Birdw and Boswellia serrata, has been found to inhibit tumor cell growth and to induce apoptosis. The apoptotic effects and the mechanisms of action of AKBA were studied in LNCaP and
P Schneider et al.
Immunity, 7(6), 831-836 (1998-01-16)
TRAIL induces apoptosis through two closely related receptors, TRAIL-R1 (DR4) and TRAIL-R2 (DR5). Here we show that TRAIL-R1 can associate with TRAIL-R2, suggesting that TRAIL may signal through heteroreceptor signaling complexes. Both TRAIL receptors bind the adaptor molecules FADD and

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