PDIA6 Human, Active
Protein Disulfide Isomerase A6 Human Recombinant, Active
Cat. No.
BT1472
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, resides within 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. Beyond its isomerase activity, PDIA6 acts as a chaperone, effectively preventing the aggregation of misfolded proteins. Furthermore, PDIA6 participates in platelet aggregation and activation induced by agonists like convulxin, collagen, and thrombin.
Description
Recombinant human PDIA6, expressed in E. coli, is a purified, non-glycosylated polypeptide chain with a His tag (21 amino acids) attached to its N-terminus. This single-chain protein consists of 442 amino acids (residues 20-440) and exhibits a molecular weight of 48.5 kDa. The purification process involves proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution, sterile-filtered.
Formulation
The provided PDIA6 solution (concentration: 1 mg/ml) is formulated in a buffer consisting of 20mM Tris-HCl (pH 8.0), 10% glycerol, 2mM DTT, and 50mM NaCl.
Stability
For optimal storage, maintain the PDIA6 solution at 4°C if it will be completely utilized within 2-4 weeks. For extended storage periods, freezing at -20°C is recommended. To enhance long-term stability during storage, consider adding a carrier protein like HSA or BSA (0.1%). Minimize repeated freeze-thaw cycles to preserve protein integrity.
Purity
The purity of PDIA6 exceeds 90.0%, as determined by SDS-PAGE analysis.
Biological Activity
The specific activity of PDIA6 is greater than 10 A650/cm/min/mg, determined by measuring its ability to inhibit the aggregation of insulin (INS) in the presence of DTT. This assay confirms the protein's enzymatic activity.
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 characterized by its thioredoxin (TRX) domains, which are essential for its enzymatic activity. The protein has an N-terminal ER-signal sequence, two catalytically active TRX domains, a TRX-like domain, and a C-terminal ER-retention sequence . These domains enable PDIA6 to catalyze the formation and rearrangement of disulfide bonds in substrate proteins, facilitating their proper folding .
Role in Cellular Processes
PDIA6 is involved in several critical cellular processes:
- Protein Folding: PDIA6 assists in the proper folding of newly synthesized proteins by catalyzing thiol-disulfide interchange reactions .
- Unfolded Protein Response (UPR): PDIA6 negatively regulates the UPR by binding to UPR sensors such as ERN1, thereby inactivating ERN1 signaling . This regulation is crucial for maintaining ER homeostasis and preventing cellular stress.
- Chaperone Activity: PDIA6 functions as a chaperone, inhibiting the aggregation of misfolded proteins .
- Platelet Aggregation: PDIA6 plays a role in platelet aggregation and activation by agonists such as convulxin, collagen, and thrombin .
Clinical Significance
Recombinant PDIA6
Recombinant PDIA6 is produced using recombinant DNA technology, which allows for the expression of the human PDIA6 gene in a host organism, typically bacteria or yeast. This recombinant form retains the enzymatic activity and functional properties of the native protein, making it valuable for research and therapeutic applications.
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