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Pdi1p Antibody, mAb, Mouse


*This product has been discontinued! *


Abbreviated name-1 Mouse Anti-Pdi1p mAb; Anti-Pdi1p
Description S. cerevisiae PDI (Pdi1p), encoded by the PDI1 gene, is essential for growth. The critical function of Pdi1p may be the isomerization of non-native disulfide bonds, and its chaperone activity is thought to depend on this isomerase activity. Moreover, S. cerevisiae contains four nonessential genes with homology to PDI1: MPD1, MPD2, EUG1, and EPS1. Genetic analyses of strains lacking PDI genes indicated that Mpd1p is the only homologue that can fully compensate for the absence of Pdi1p. Furthermore, mutant Eug1p, which contains two mutated CXXC active site motifs, is functionally equivalent to Pdi1p.
Immunogen Pdi1p, yeast protein disulfide isomerase
Host Species Mouse
Conjugation Unconjugated
Purification Method Immunoaffinity purification

Formulation 1 mg/ml in PBS, pH 7.4 with 0.05% sodium azide, frozen liquid
Clone ID A00112.01
Ig Subclass IgG
Specificity Yeast protein disulfide isomerase, localized in ER and nuclear envelope
Storage The antibody will remain stable for one year from the date of shipment if stored at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Aliquot to avoid repeated freezing and thawing. Aliquots will remain stable for three months if stored at 4°C.
Note Briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container's cap because small volumes of antibody will occasionally become entrapped in the seal of the product vial during shipment and storage.

Western blot of yeast protein extract: 1:10,000 (ECL detection) reveal a ≈65,000 Da band. Intial dilution range: 1:2,500 to 1:5,000
Immunofluorescnce: 1:250 to 1:2,500



Dias-Gunasekara S, et al. Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Ero1beta. J. Biol. Chem. Sep 2005; 280(38): 33066-33075.

Kimura T, et al. Interactions among yeast protein-disulfide isomerase proteins and endoplasmic reticulum chaperone proteins influence their activities. J. Biol. Chem. Sep 2005; 280(36): 31438-31441.

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