PDIA3 Mouse

Protein Disulfide Isomerase A3 Mouse Recombinant
Cat. No.
BT1098
Source
Escherichia Coli.
Synonyms

ERp57, ERp60, ERp61, GRP57, GRP58, HsT17083, P58, PI-PLC, ER60, Protein disulfide-isomerase A3, Disulfide isomerase ER-60, Endoplasmic reticulum resident protein 60, ER protein 60, 58 kDa microsomal protein, Endoplasmic reticulum resident protein 57, ER protein 57, 58 kDa glucose-regulated protein, PDIA3.

Appearance
Sterile filtered colourless solution.
Purity

Greater than 95.0% 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

PDIA3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 505 amino acids (25-505 a.a) and having a molecular mass of 56.8kDa.

PDIA3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques. 

Product Specs

Introduction
Protein disulfide-isomerase A3 (PDIA3), also known as ERp57 or GRP58, is an enzyme primarily located in the endoplasmic reticulum (ER). It plays a crucial role in protein folding and quality control by catalyzing the formation, breakage, and rearrangement of disulfide bonds in newly synthesized glycoproteins. PDIA3 interacts with chaperones like calreticulin and calnexin to facilitate proper protein folding. It is involved in various cellular processes, including immune response through MHC class I peptide loading, response to cellular stress like glucose deprivation, and has been linked to neurological processes like response to nerve injury.
Description
This product consists of the recombinant mouse PDIA3 protein, specifically amino acids 25 to 505, with an N-terminal His-tag of 23 amino acids. It is produced in E. coli, resulting in a single, non-glycosylated polypeptide chain with a molecular weight of approximately 56.8 kDa. The protein is purified using proprietary chromatographic methods to ensure high purity.
Physical Appearance
Clear, colorless liquid that has been sterilized by filtration.
Formulation
The PDIA3 protein is provided at a concentration of 1 mg/ml in a buffer consisting of 20 mM Tris-HCl (pH 8.0), 1 mM DTT, 0.1 M NaCl, and 10% glycerol.
Stability
For short-term storage (up to 4 weeks), keep refrigerated at 4°C. For extended storage, freeze at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is recommended for long-term storage. Avoid repeated freezing and thawing to maintain protein integrity.
Purity
The purity of the PDIA3 protein is greater than 95%, as determined by SDS-PAGE analysis.
Biological Activity
The protein exhibits a specific activity exceeding 15 A650/cm/min/mg. This activity is determined by measuring the increase in absorbance at 650 nm, reflecting the rate of insulin precipitation due to insulin reduction catalyzed by the enzyme.
Synonyms

ERp57, ERp60, ERp61, GRP57, GRP58, HsT17083, P58, PI-PLC, ER60, Protein disulfide-isomerase A3, Disulfide isomerase ER-60, Endoplasmic reticulum resident protein 60, ER protein 60, 58 kDa microsomal protein, Endoplasmic reticulum resident protein 57, ER protein 57, 58 kDa glucose-regulated protein, PDIA3.

Source
Escherichia Coli.
Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MGSMSDVLEL TDENFESRVS DTGSAGLMLV EFFAPWCGHC KRLAPEYEAA ATRLKGIVPL AKVDCTANTN TCNKYGVSGY PTLKIFRDGE EAGAYDGPRT ADGIVSHLKK QAGPASVPLR TEEEFKKFIS DKDASVVGFF RDLFSDGHSE FLKAASNLRD NYRFAHTNIE SLVKEYDDNG EGITIFRPLH LANKFEDKTV AYTEKKMTSG KIKKFIQDSI FGLCPHMTED NKDLIQGKDL LTAYYDVDYE KNAKGSNYWR NRVMMVAKKF LDAGHKLNFA VASRKTFSHE LSDFGLESTT GEVPVVAIRT AKGEKFVMQE EFSRDGKALE QFLQEYFDGN LKRYLKSEPI PESNEGPVKV VVAENFDDIV NEEDKDVLIE FYAPWCGHCK NLEPKYKELG EKLSKDPNIV IAKMDATAND VPSPYEVKGF PTIYFSPANK KLTPKKYEGG RELNDFISYL QREATNPPII QEEKPKKKKK AQEDL.

Product Science Overview

Introduction

Protein Disulfide Isomerase A3 (PDIA3), also known as ERp57, is a member of the protein disulfide isomerase (PDI) family. This enzyme plays a crucial role in the formation, isomerization, and reduction or oxidation of disulfide bonds in client proteins, functioning as a protein folding chaperone .

Structure and Function

PDIA3 is primarily localized in the endoplasmic reticulum (ER) due to its N-terminal signal peptide. However, it is ubiquitous within the cell, likely due to a noncanonical ER retention motif (QEDL) at the C-terminal, the presence of a nuclear localization sequence, and its capability to interact with a wide range of proteins . The enzyme catalyzes the rearrangement of -S-S- bonds in proteins, which is essential for proper protein folding and stability .

Role in Cellular Processes

PDIA3 is a core component of the major histocompatibility complex class I (MHC I) peptide loading complex, where it functions as an essential folding chaperone for TAPBP. Through TAPBP, PDIA3 assists in the dynamic assembly of the MHC I complex with high-affinity antigens in the ER. This process is crucial for the presentation of antigens to cytotoxic T cells in adaptive immunity .

Involvement in Disease

PDIA3 has been implicated in various physiopathological processes, including cancer initiation, progression, and chemosensitivity. For instance, studies have shown that the inhibition or silencing of PDIA3 in glioblastoma cell lines can reduce cell spreading and increase chemosensitivity to the drug temozolomide . Additionally, PDIA3 is required for the oxidative folding of influenza A virus hemagglutinin, indicating its role in viral propagation .

Therapeutic Potential

Given its involvement in critical cellular processes and disease mechanisms, PDIA3 is considered a potential therapeutic target. Inhibiting PDIA3 functions could lead to cytotoxic effects in cancer cells and enhance the efficacy of existing treatments . Further research is needed to explore its therapeutic potential fully.

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