PRDX2 Mouse
PRDX2, Peroxiredoxin-2 (EC:1.11.1.15), TSA, Thioredoxin peroxidase 1, Thioredoxin-dependent peroxide reductase 1, Thiol-specific antioxidant protein, Prdx2, Tdpx1, Tpx.
Greater than 90.0% as determined by SDS-PAGE.
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.
Description
PRDX2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids (1-198 a.a) and having a molecular mass of 24.3kDa. PRDX2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
PRDX2, a member of the peroxiredoxin family, functions as an antioxidant enzyme by reducing hydrogen peroxide and alkyl hydroperoxides. This enzyme plays a crucial role in cellular protection against oxidative stress and contributes to the antiviral response of CD8(+) T-cells. Additionally, PRDX2 has been implicated in cancer development and progression due to its proliferative effects. Insufficient PRDX2 protection against peroxidases can lead to DNA damage, potentially resulting in neurological disorders like Alzheimer's disease or promoting cancer development.
Recombinantly produced in E. coli, PRDX2 Mouse Recombinant is a non-glycosylated polypeptide chain with a single chain. It consists of 222 amino acids (1-198 a.a), with a molecular weight of 24.3 kDa. A 24 amino acid His-tag is fused to the N-terminus of PRDX2. Purification is achieved through proprietary chromatographic techniques.
The PRDX2 protein solution has a concentration of 1 mg/ml. It is prepared in a buffer containing 20mM Tris-HCl (pH 8.0), 10% glycerol, and 1mM DTT.
SDS-PAGE analysis has determined the purity to be greater than 90.0%.
The enzyme exhibits a specific activity greater than 700 pmol/min/ug. Specific activity is defined as the amount of hydroperoxide reduced by 1ug of enzyme per minute at a temperature of 25°C.
PRDX2, Peroxiredoxin-2 (EC:1.11.1.15), TSA, Thioredoxin peroxidase 1, Thioredoxin-dependent peroxide reductase 1, Thiol-specific antioxidant protein, Prdx2, Tdpx1, Tpx.
MGSSHHHHHH SSGLVPRGSH MGSHMASGNA QIGKSAPDFT ATAVVDGAFK EIKLSDYRGK YVVLFFYPLD FTFVCPTEII AFSDHAEDFR KLGCEVLGVS VDSQFTHLAW INTPRKEGGL GPLNIPLLAD VTKSLSQNYG VLKNDEGIAY RGLFIIDAKG VLRQITVNDL PVGRSVDEAL RLVQAFQYTD EHGEVCPAGW KPGSDTIKPN VDDSKEYFSK HN
Product Science Overview
eIF4E is a member of the eukaryotic initiation factor 4 (eIF4) family. It recognizes and binds to the 5’ cap structure of eukaryotic mRNAs, which is a 7-methylguanosine triphosphate (m7GpppN) cap . This binding is essential for the recruitment of the ribosome to the mRNA, facilitating the initiation of translation . eIF4E functions in synergy with other proteins such as the helicase eIF4A and the scaffolding protein eIF4G to form the eIF4F complex . This complex unwinds secondary structures in the mRNA 5’ untranslated regions (UTRs) to allow ribosome binding and translation initiation .
The activity of eIF4E is tightly regulated in cells under normal physiological conditions. It can be controlled by post-translational modifications, such as phosphorylation, and by the binding of inhibitory proteins, including eIF4E binding proteins (4E-BPs) and CYFIP1 . These regulatory mechanisms ensure that protein synthesis is appropriately modulated in response to cellular conditions and external stimuli .
eIF4E is also involved in the cellular response to stress. It localizes to processing bodies (PBs) and stress granules (SGs) under different stress conditions . For instance, during heat shock, eIF4E can be redirected to stress granules, indicating its role in the cellular stress response . This localization is crucial for the regulation of mRNA stability and translation during stress .
Recombinant mouse eIF4E is a form of the protein that has been produced using recombinant DNA technology. This involves inserting the gene encoding eIF4E into a suitable expression system, such as bacteria or yeast, to produce the protein in large quantities. Recombinant proteins are often used in research to study the function and regulation of the protein in a controlled environment .
Recombinant eIF4E is widely used in biochemical and structural studies to understand its role in translation initiation and its interactions with other proteins. It is also used in studies investigating the regulation of protein synthesis and the cellular response to stress . By using recombinant eIF4E, researchers can gain insights into the molecular mechanisms underlying translation initiation and its regulation in eukaryotic cells .
