DEDD Human

Death Effector Domain Containing Human Recombinant
Cat. No.
BT4203
Source
Escherichia Coli.
Synonyms
CASP8IP1, DEDD1, DEFT, FLDED1, KE05, DEDPro1, Death effector domain-containing testicular molecule.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

DEDD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 338 amino acids (1-318a.a) and having a molecular mass of 38.9kDa.
DEDD is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Death effector domain-containing protein (DEDD) is a cytoplasmic protein that plays a role in apoptosis. Its cell death activity is linked to its ability to translocate to the nucleus during CD95-mediated apoptosis. In the nucleus, DEDD localizes to nucleoli-like structures, activates caspase-6, and inhibits RNA polymerase I-dependent transcription. DEDD is widely expressed in various tissues, with the highest levels found in the testis. Overexpression of DEDD has been shown to induce weak apoptosis.
Description
Recombinant human DEDD protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 338 amino acids (residues 1-318) with a molecular weight of 38.9 kDa. The protein contains a 20-amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Physical Appearance
The product is a sterile, filtered solution that is colorless.
Formulation
The DEDD protein solution is provided at a concentration of 0.5 mg/ml in a buffer containing 20 mM Tris-HCl (pH 8.0), 0.4 M Urea, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the product should be stored at 4°C. For longer storage, it is recommended to store the product frozen at -20°C. To ensure long-term stability, the addition of a carrier protein (0.1% HSA or BSA) is recommended. Avoid repeated freeze-thaw cycles.
Purity
The purity of the DEDD protein is greater than 85.0% as determined by SDS-PAGE analysis.
Synonyms
CASP8IP1, DEDD1, DEFT, FLDED1, KE05, DEDPro1, Death effector domain-containing testicular molecule.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAGLKRRASQ VWPEEHGEQE HGLYSLHRMF DIVGTHLTHR DVRVLSFLFV DVIDDHERGL IRNGRDFLLA LERQGRCDES NFRQVLQLLR IITRHDLLPY VTLKRRRAVC PDLVDKYLEE TSIRYVTPRA LSDPEPRPPQ PSKTVPPHYP VVCCPTSGPQ MCSKRPARGR ATLGSQRKRR KSVTPDPKEK QTCDIRLRVR AEYCQHETAL QGNVFSNKQD PLERQFERFN QANTILKSRD LGSIICDIKF SELTYLDAFW RDYINGSLLE ALKGVFITDS LKQAVGHEAI KLLVNVDEED YELGRQKLLR NLMLQALP.

Product Science Overview

Introduction

The Death Effector Domain (DED) is a protein interaction domain found in various proteins involved in apoptosis, a form of programmed cell death. The DED domain is crucial for the formation of death-inducing signaling complexes (DISCs) that initiate the apoptotic cascade. This article delves into the background of DED-containing proteins, particularly focusing on human recombinant versions.

Structure and Function

DEDs are typically found in proteins such as Fas-associated death domain protein (FADD), caspase-8, and caspase-10. These domains facilitate protein-protein interactions necessary for the apoptotic signaling pathways. The DED domain is characterized by a conserved sequence that allows it to bind to other DED-containing proteins, forming complexes that activate downstream apoptotic signals .

Key DED-Containing Proteins
  1. FADD (Fas-Associated Death Domain Protein): FADD is an adaptor protein that plays a pivotal role in the extrinsic pathway of apoptosis. It recruits procaspase-8 and procaspase-10 to the DISC, leading to their activation and subsequent initiation of the apoptotic cascade .
  2. DEDD (Death Effector Domain-Containing DNA-Binding Protein): DEDD is another DED-containing protein that translocates to the nucleus upon apoptotic signaling. It interacts with FADD and caspase-8, contributing to the apoptotic process .
Mechanism of Action

The primary function of DED-containing proteins is to mediate the formation of DISCs. Upon activation by death receptors such as Fas, FADD is recruited to the receptor complex. FADD then binds to procaspase-8 and procaspase-10 through its DED, facilitating their activation. Once activated, these caspases cleave various substrates, leading to the execution phase of apoptosis .

Clinical Implications

The dysregulation of DED-containing proteins has been implicated in various diseases, including cancer. For instance, overexpression of FADD has been associated with increased cancer cell proliferation and resistance to apoptosis. Understanding the role of DED-containing proteins in apoptosis can provide insights into potential therapeutic targets for cancer treatment .

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