Catalogue number
ENZ-262
Synonyms
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.
Introduction
Protein disulfide isomerases (PDIs) constitute a family of structurally related enzymes which catalyze disulfide bonds formation, reduction, or isomerization of newly synthesized proteins in the lumen of the endoplasmic reticulum (ER). They act also as chaperones, and are, therefore, part of a quality-control system for the correct folding of the proteins in the same subcellular compartment. PDI has been found to have moderate effects (25-fold) on the rate of oxidative folding of proteins in vitro.
Recombinant Human Protein Disulfide Isomerase is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. Recombinant PDI has been found to have moderate effects (25-fold) on the rate of oxidative folding of proteins in vitro.
Description
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.
Source
Escherichia Coli.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation
The PDI protein (1mg/ml)solution was lyophilized from PBS pH-7.
Solubility
It is recommended to reconstitute the lyophilized PDI in sterile 18MΩ-cm H2O not less than 100μg/ml, which can then be further diluted to other aqueous solutions.
Stability
Lyophilized Protein Disulfide Isomerase although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Human PDI should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please avoid freeze-thaw cycles.
Purity
Greater than 95.0% as determined by:
a) Analysis by RP-HPLC.
b) Analysis by SDS-PAGE.
Amino acid sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Leu-Arg-Arg-Ala.
Reductase Activity
0.001 650nm/ min-2. By measuring the turbidity increase at 650 nm due to insulin reduction (Holmgren, A. (1979) J. Biol. Chem. 254, 9627–9632). The activity is expressed as the ratio of the slope of a linear part of the turbidity curve to the lag time (Mart?′nez-Galisteo, E., Padilla, C. A., Garcia-Alfonso, C., Lo′pez-Barea, J., and Barcena, J. A. (1993) Biochimie (Paris) 75, 803–809).
Isomerase Activity
0.5 μmol active RNase A min-1 μmol 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).
References
Title: Protein disulfide isomerases are antibody targets during immune-mediated tumor destruction
Publications: ?Blood?113.8 (2009): 1681-1688.
Link:?http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2647666/
Safety Data Sheet
Usage
Prospec'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.
