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Key Documents

P3818

Sigma-Aldrich

Protein Disulfide Isomerase from bovine liver

≥100 units/mg protein, lyophilized powder

Synonyme(s) :

PDI

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Forme

lyophilized powder

Niveau de qualité

Activité spécifique

≥100 units/mg protein

Poids mol.

107 kDa

Composition

Protein, ~10% Lowry

Température de stockage

−20°C

InChI

1S/C7H5Cl2NO5S/c8-4-2-5(9)6(16(13,14)15-10)1-3(4)7(11)12/h1-2H,10H2,(H,11,12)

Clé InChI

DHUYKLYJBKXDBM-UHFFFAOYSA-N

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Description générale

Protein disulfide isomerase (PDI) from bovine liver is a homodimer with a molecular weight of 107 kDa with the monomer corresponding to 57 kDa. The isoelectric point (pI) is approximately 4.2. The enzyme is a glycoprotein with 12% total carbohydrate content comprising of mannose, galactose, N-acetyl neuraminic acid (NANA) and 2-acetamido-2-deoxyglucose. PDI is an ubiquitous redox chaperone enzyme. It belongs to the, thioredoxin superfamily and is high conserved.

Application

Protein Disulfide Isomerase from bovine liver has been used:
  • to study the functional role of PDI in parasite infection and the interaction between macrophage PDI and L. chagasi
  • in the in vitro translation reaction for the generation of disulfide bonds
  • in insulin-disulfide reduction assay and peptide binding assay
  • as a positive control in thiol-disulfide oxidoreductase activity assay

Actions biochimiques/physiologiques

Protein Disulfide Isomerase (PDI) is mainly located in the endoplasmic reticulum (ER), where it assists in protein-folding and thiol-disulfide exchanges. It aids protein refolding in vitro allowing recombinant proteins to achieve their native state.
Protein Disulfide Isomerase(PDI) has the C-terminal ER retention sequence Lys-Asp-Glu-Leu. It has active, intracellular traffic to different cell compartments. PDI supports internalization of Chlamydia, cholera and diphtheria toxins in some hosts. PDI is required for Sindbis virus infection and aids in reducing HIV gp120 protein thiols. PDI facilitates formation of the correct disulfide bonds by promoting rapid reshuffling of disulfide pairings.

Conditionnement

Package size based on protein content.

Propriétés physiques

Protein Disulfide Isomerase (PDI) from bovine liver is a homodimer with a molecular weight of 107 kDa (gel filtration) and the molecular weight of the monomer has been reported at 57 kDA (SDS-PAGE). The enzyme is a glycoprotein with 12% total carbohydrate content, composed of 4.6% mannose, 2.5% galactose, 1.4% NANA, and 3.5% 2-acetamido-2-deoxyglucose.

Définition de l'unité

One unit cause a change in A650 of 0.01 per min of a 1.0 mg/mL solution of insulin in the presence of dithiothreitol at pH 7.5 at 25 °C.

Forme physique

Lyophilized powder containing potassium phosphate buffer salts and stabilizer.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Protein disulfide isomerase (PDI) associates with NADPH oxidase and is required for phagocytosis of Leishmania chagasi promastigotes by macrophages
Santos CXC, et al.
Journal of Leukocyte Biology, 86(4), 989-998 (2009)
Ribosome display: a technology for selecting and evolving proteins from large libraries
Dreier B and Pluckthun A
Methods in Molecular Biology, 283-306 (2011)
Recognition and ER Quality Control of Misfolded Formylglycine-Generating Enzyme by Protein Disulfide Isomerase
Schlotawa L, et al.
Testing, 24(1), 27-37 (2018)
Purification and characterization of a thiol: protein disulfide oxidoreductase from bovine liver.
Carmichael DF, et al.
The Journal of Biological Chemistry, 252(20), 7163-7167 (1977)
Structural properties of homogeneous protein disulphide-isomerase from bovine liver purified by a rapid high-yielding procedure
Lambert N and Freedman RB
The Biochemical Journal, 213(1), 225-234 (1983)

Articles

Oxidative stress is mediated, in part, by reactive oxygen species produced by multiple cellular processes and controlled by cellular antioxidant mechanisms such as enzymatic scavengers or antioxidant modulators. Free radicals, such as reactive oxygen species, cause cellular damage via cellular.

Oxidative stress is mediated, in part, by reactive oxygen species produced by multiple cellular processes and controlled by cellular antioxidant mechanisms such as enzymatic scavengers or antioxidant modulators. Free radicals, such as reactive oxygen species, cause cellular damage via cellular.

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