PDI1 (yeast)

Protein Disulfide Isomerase1 (yeast) Description:
Recombinant yeast PDI is produced in E.Coli is as  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.

Recombinant Yeast 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.

Source:
Escherichia Coli.

Physical Appearance:
Sterile Filtered liquid form or lyophilized powder

Formulation:  
The PDI protein (10mg/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 99.0% as determined by  RP-HPLC.

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).