FADD peptide

Name: FADD peptide
SKU: DAG-P1571
Rating: 5 (1 reviews)

Regulatory status: For research use only, not for use in diagnostic procedures.

COA

SDS

Datasheet

Summary

Nature

Synthetic

Tag/Conjugate

Unconjugated

Purity

> 95 % by SDS-PAGE.

Format

Lyophilized

Preservative

0.02% Thimerosal

Storage

Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles. Preservative: 0.02% Thimerosal (merthiolate) Constituents: 0.1% BSA, PBS, pH 7.2

Reconstitution

FADD peptide is supplied as 1mg of dried peptide. When the peptide is reconstituted in 1 mL strile water, the concentration will be 1 mg/mL.

Introduction

The protein encoded by this gene is an adaptor molecule that interacts with various cell surface receptors and mediates cell apoptotic signals. Through its C-terminal death domain, this protein can be recruited by TNFRSF6/Fas-receptor, tumor necrosis factor receptor, TNFRSF25, and TNFSF10/TRAIL-receptor, and thus it participates in the death signaling initiated by these receptors. Interaction of this protein with the receptors unmasks the N-terminal effector domain of this protein, which allows it to recruit caspase-8, and thereby activate the cysteine protease cascade. Knockout studies in mice also suggest the importance of this protein in early T cell development. [provided by RefSeq, Jul 2008]

Entrez Gene ID

8772

Synonyms

FADD; Fas (TNFRSF6)-associated via death domain; GIG3; MORT1; FAS-associated death domain protein; growth-inhibiting gene 3 protein; mediator of receptor induced toxicity; mediator of receptor-induced toxicity; Fas-associating protein with death domain; Fas-associating death domain-containing protein;

Citations

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Documents

pdf COA

pdf SDS

pdf Datasheet

QA & Reviews

Customer Reviews

References

Novel engineered TRAIL-based chimeric protein strongly inhibits tumor growth and bypasses TRAIL resistance

INTERNATIONAL JOURNAL OF CANCER

Authors: Rozga, Piotr; Kloska, Damian; Pawlak, Sebastian; Teska-Kaminska, Malgorzata; Galazka, Marlena; Bukato, Katarzyna; Pieczykolan, Anna; Jaworski, Albert; Molga-Kaczmarska, Anna; Kopacz, Aleksandra; Badyra, Bogna; Kachamakova-Trojanowska, Neli; Zolnierkiewicz, Olga; Targosz-Korecka, Marta; Poleszak, Katarzyna; Szymanik, Michal; Zerek, Bartlomiej; Pieczykolan, Jerzy; Jozkowicz, Alicja; Grochot-Przeczek, Anna

Abstract

Targeting of the TRAIL-DR4/5 pathway was proposed as a promising approach for specific induction of apoptosis in cancer cells. Clinical trials, however, showed inadequate efficiency of TRAIL as a monotherapy. It is a widely held view that the application of multifunctional molecules or combination therapy may lead to substantial improvement. Here, we demonstrate the effectiveness and safety of a novel chimeric protein, AD-O51.4, which is a TRAIL equipped with positively charged VEGFA-derived effector peptides. The study was performed in multiple cancer cell line- and patient-derived xenografts. A pharmacokinetic profile was established in monkeys. AD-O51.4 strongly inhibits tumor growth, even leading to complete long-term tumor remission. Neither mice nor monkeys treated with AD-O51.4 demonstrate symptoms of drug toxicity. AD-O51.4 exhibits a satisfactory half-life in plasma and accumulates preferentially in tumors. The cellular mechanism of AD-O51.4 activity involves both cytotoxic effects in tumor cells and antiangiogenic effects on the endothelium. The presence of DRs in cancer cells is crucial for AD-O51.4-driven apoptosis execution. The TRAIL component of the fusion molecule serves as an apoptosis inducer and a cellular anchor for the effector peptides in TRAIL-sensitive and TRAIL-resistant cancer cells, respectively. The FADD-dependent pathway, however, seems to be not indispensable in death signal transduction; thus, AD-O51.4 is capable of bypassing the refractoriness of TRAIL. AD-O51.4-driven cell death, which exceeds TRAIL activity, is achieved due to the N-terminally fused polypeptide, containing VEGFA-derived effector peptides. The high anticancer efficiency of AD-O51.4 combined with its safety has led to the entry of AD-O51.4 into toxicological studies.

Controlling Cell Death through Post-translational Modifications of DED Proteins

TRENDS IN CELL BIOLOGY

Authors: Seyrek, Kamil; Ivanisenko, Nikita, V; Richter, Max; Hillert, Laura K.; Koenig, Corinna; Lavrik, Inna N.

Abstract

Apoptosis is a form of programmed cell death, deregulation of which occurs in multiple disorders, including neurodegenerative and autoimmune diseases as well as cancer. The formation of a death-inducing signaling complex (DISC) and death effector domain (DED) filaments are critical for initiation of the extrinsic apoptotic pathway. Post-translational modifications (PTMs) of DED-containing DISC components such as FADD, procaspase-8, and c-FLIP comprise an additional level of apoptosis regulation, which is necessary to overcome the threshold for apoptosis induction. In this review we discuss the influence of PTMs of FADD, procaspase-8, and c-FLIP on DED filament assembly and cell death induction, with a focus on the 3D organization of the DED filament.