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Disulfide Isomerase Active Protein | PDI active protein

Recombinant Human Protein Disulfide Isomerase

Gene Names
P4HB; DSI; GIT; PDI; PHDB; PDIA1; PO4DB; PO4HB; PROHB; ERBA2L; P4Hbeta
Purity
Greater than 95.0% as determined by a) Analysis by RP-HPLC. b) Analysis by SDS-PAGE.
Synonyms
Disulfide Isomerase; Recombinant Human Protein Disulfide Isomerase; PDI Human; Protein Disulfide Isomerase Human Recombinant; Protein Disulfide Isomerase; PDI; EC 5.3.4.1; Prolyl 4-hydroxylase subunit beta; Cellular thyroid hormone-binding protein; p55; P4HB; ERBA2L; PDIA1; PO4DB; DSI; GIT; PHDB; PO4HB; PROHB; P4Hbeta; PDI active protein
Ordering
For Research Use Only!
Host
E Coli
Purity/Purification
Greater than 95.0% as determined by a) Analysis by RP-HPLC. b) Analysis by SDS-PAGE.
Form/Format
The PDI protein (1mg/ml)solution was lyophilized from PBS pH-7.
Sterile Filtered White lyophilized (freeze-dried) powder.
Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Leu-Arg-Arg-Ala
Sequence Length
508
Isomerase Activity
0.5 umol active RNase A min-1 umol PDI-1. According to the re-activation of reduced and denatured RNase A (Lyles, M. M. and Gilbert, H. F. (1991) Biochemistry 30, 613-619).
Reductase Activity
1.0 x 10-3 Delta 650nm/ min-2. By measuring the turbidity increase at 650 nm due to insulin reduction (Holmgren, A. (1979) J. Biol. Chem. 254, 96279632). The activity is expressed as the ratio of the slope of a linear part of the turbidity curve to the lag time (MartŽ ´nez-Galisteo, E., Padilla, C. A., Garcia-Alfonso, C., Lo ´pez-Barea, J., and Barcena, J. A. (1993) Biochimie (Paris) 75, 803809).
Solubility
It is recommended to reconstitute the lyophilized PDI in sterile 18M Omega -cm H2O not less than 100 ug/ml, which can then be further diluted to other aqueous solutions.
Preparation and Storage
Lyophilized Protein Disulfide Isomerase although stable at room temperature for 3 weeks, should be stored desiccated below -18 degree C.
Upon reconstitution Human PDI should be stored at 4 degree C between 2-7 days and for future use below -18 degree C.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please avoid freeze-thaw cycles.
Related Product Information for PDI active protein
PDI Human Recombinant produced in E Coli is a single, non-glycosylated, polypeptide chain containing 503 amino acids and having a molecular mass of 62.4 kDa. The PDI is fused to a 12 amino acid His tag (515 a.a. total) at N-terminal and purified by proprietary chromatographic techniques.
Product Categories/Family for PDI active protein

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Accession #
NCBI Official Full Name
protein disulfide-isomerase
NCBI Official Synonym Full Names
prolyl 4-hydroxylase, beta polypeptide
NCBI Official Symbol
P4HB
NCBI Official Synonym Symbols
DSI; GIT; PDI; PHDB; PDIA1; PO4DB; PO4HB; PROHB; ERBA2L; P4Hbeta
NCBI Protein Information
protein disulfide-isomerase; cellular thyroid hormone-binding protein; collagen prolyl 4-hydroxylase beta; glutathione-insulin transhydrogenase; p55; procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), beta polypeptide; prolyl 4-hydroxylase subunit beta; protein disulfide isomerase family A, member 1; protein disulfide isomerase-associated 1; protein disulfide isomerase/oxidoreductase; protocollagen hydroxylase; thyroid hormone-binding protein p55
UniProt Protein Name
Protein disulfide-isomerase
UniProt Gene Name
P4HB
UniProt Synonym Gene Names
ERBA2L; PDI; PDIA1; PO4DB; PDI
UniProt Entry Name
PDIA1_HUMAN

NCBI Description

This gene encodes the beta subunit of prolyl 4-hydroxylase, a highly abundant multifunctional enzyme that belongs to the protein disulfide isomerase family. When present as a tetramer consisting of two alpha and two beta subunits, this enzyme is involved in hydroxylation of prolyl residues in preprocollagen. This enzyme is also a disulfide isomerase containing two thioredoxin domains that catalyze the formation, breakage and rearrangement of disulfide bonds. Other known functions include its ability to act as a chaperone that inhibits aggregation of misfolded proteins in a concentration-dependent manner, its ability to bind thyroid hormone, its role in both the influx and efflux of S-nitrosothiol-bound nitric oxide, and its function as a subunit of the microsomal triglyceride transfer protein complex. [provided by RefSeq, Jul 2008]

Uniprot Description

PDIA1: This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Homodimer. Monomers and homotetramers may also occur. Also constitutes the structural subunit of prolyl 4-hydroxylase and of the microsomal triacylglycerol transfer protein MTTP in mammalian cells. Stabilizes both enzymes and retain them in the ER without contributing to the catalytic activity. Binds UBQLN1. Binds to CD4, and upon HIV-1 binding to the cell membrane, is part of a P4HB/PDI-CD4-CXCR4-gp120 complex. Belongs to the protein disulfide isomerase family.

Protein type: EC 5.3.4.1; Endoplasmic reticulum; Oxidoreductase; Isomerase; Nuclear receptor co-regulator

Chromosomal Location of Human Ortholog: 17q25

Cellular Component: focal adhesion; endoplasmic reticulum lumen; endoplasmic reticulum; extracellular region; ER-Golgi intermediate compartment; plasma membrane; melanosome

Molecular Function: protein binding; enzyme binding; procollagen-proline 4-dioxygenase activity; protein heterodimerization activity; endopeptidase activity; protein disulfide isomerase activity

Biological Process: extracellular matrix organization and biogenesis; response to reactive oxygen species; protein folding; cell redox homeostasis; lipoprotein metabolic process; peptidyl-proline hydroxylation to 4-hydroxy-L-proline; proteolysis

Disease: Cole-carpenter Syndrome 1

Research Articles on PDI

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Product Notes

The PDI p4hb (Catalog #AAA142403) is an Active Protein produced from E Coli and is intended for research purposes only. The product is available for immediate purchase. The amino acid sequence is listed below: The sequence of the first five N-terminal amino acids was determined and was found to be Met-Leu-Ar g-Arg-Ala. It is sometimes possible for the material contained within the vial of "Disulfide Isomerase, Active Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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