PDIA6 Human

Protein Disulfide Isomerase A6 Human Recombinant
Cat. No.
BT1417
Source
Escherichia Coli.
Synonyms
Protein disulfide-isomerase A6, Endoplasmic reticulum protein 5, ER protein 5, ERp5, Protein disulfide isomerase P5, Thioredoxin domain-containing protein 7, PDIA6, ERP5, P5, TXNDC7.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90.0% 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.
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Description

PDIA6 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 442 amino acids (20-440 a.a.) and having a molecular mass of 48.5kDa. The PDIA6 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
PDIA6, a member of the protein disulfide isomerase (PDI) family, is found in the endoplasmic reticulum of eukaryotes and the periplasmic space of prokaryotes. This enzyme plays a crucial role in protein folding by catalyzing the formation and breakage of disulfide bonds between cysteine residues. Acting as a chaperone, PDIA6 prevents the aggregation of misfolded proteins. Additionally, it contributes to platelet aggregation and activation triggered by agonists such as convulxin, collagen, and thrombin.
Description
Recombinant human PDIA6, expressed in E. coli, is a non-glycosylated polypeptide chain with a His tag (21 amino acids) at its N-terminus. This single-chain protein consists of 442 amino acids (20-440 a.a.), resulting in a molecular weight of 48.5 kDa. Purification of PDIA6 is achieved using proprietary chromatographic methods.
Physical Appearance
A sterile, colorless solution.
Formulation
The PDIA6 solution is provided at a concentration of 1 mg/ml in a buffer consisting of 20 mM Tris-HCl (pH 8.0), 10% glycerol, 2 mM DTT, and 50 mM NaCl.
Stability
For short-term storage (2-4 weeks), the PDIA6 solution should be kept at 4°C. Long-term storage requires freezing at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for extended storage. Repeated freezing and thawing should be avoided.
Purity
SDS-PAGE analysis indicates a purity greater than 90.0%.
Synonyms
Protein disulfide-isomerase A6, Endoplasmic reticulum protein 5, ER protein 5, ERp5, Protein disulfide isomerase P5, Thioredoxin domain-containing protein 7, PDIA6, ERP5, P5, TXNDC7.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MLYSSSDDVI ELTPSNFNRE VIQSDSLWLV EFYAPWCGHC QRLTPEWKKA ATALKDVVKV GAVDADKHHS LGGQYGVQGF PTIKIFGSNK NRPEDYQGGR TGEAIVDAAL SALRQLVKDR LGGRSGGYSS GKQGRSDSSS KKDVIELTDD SFDKNVLDSE DVWMVEFYAP WCGHCKNLEP EWAAAASEVK EQTKGKVKLA AVDATVNQVL ASRYGIRGFP TIKIFQKGES PVDYDGGRTR SDIVSRALDL FSDNAPPPEL LEIINEDIAK RTCEEHQLCV VAVLPHILDT GAAGRNSYLE VLLKLADKYK KKMWGWLWTE AGAQSELETA LGIGGFGYPA MAAINARKMK FALLKGSFSE QGINEFLREL SFGRGSTAPV GGGAFPTIVE REPWDGRDGE LPVEDDIDLS DVELDDLGKD EL.

Product Science Overview

Structure and Function

PDIA6 is a multi-domain enzyme that belongs to the thioredoxin superfamily. It consists of 440 amino acids and has a molecular weight of approximately 48 kDa . The enzyme contains active sites that catalyze the rearrangement of disulfide bonds in substrate proteins, ensuring their correct folding and preventing aggregation .

Biological Role

PDIA6 functions as a chaperone that inhibits the aggregation of misfolded proteins. It plays a significant role in the endoplasmic reticulum (ER) by regulating the unfolded protein response (UPR), a cellular stress response related to the ER . PDIA6 binds to UPR sensors such as ERN1, inactivating their signaling and thereby negatively regulating the UPR . This regulation is crucial for maintaining cellular homeostasis and preventing ER stress-induced apoptosis.

Additionally, PDIA6 is involved in platelet aggregation and activation by agonists such as convulxin, collagen, and thrombin . This highlights its importance in various physiological processes beyond protein folding.

Clinical Significance

PDIA6 has been implicated in several diseases and conditions due to its role in protein folding and ER stress response. Dysregulation of PDIA6 activity can lead to the accumulation of misfolded proteins, contributing to the pathogenesis of diseases such as neurodegenerative disorders and cancer . Understanding the function and regulation of PDIA6 is therefore critical for developing therapeutic strategies targeting these conditions.

Recombinant PDIA6

Recombinant PDIA6 is produced using recombinant DNA technology, which involves inserting the gene encoding PDIA6 into an expression system, such as bacteria or yeast, to produce the protein in large quantities. This recombinant form is used in various research applications to study the enzyme’s structure, function, and role in disease.

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