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Key Documents

P3818

Sigma-Aldrich

Protein Disulfide Isomerase from bovine liver

≥100 units/mg protein, lyophilized powder

Synonym(s):

PDI

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

form

lyophilized powder

Quality Level

specific activity

≥100 units/mg protein

mol wt

107 kDa

composition

Protein, ~10% Lowry

storage temp.

−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)

InChI key

DHUYKLYJBKXDBM-UHFFFAOYSA-N

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General description

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

Biochem/physiol Actions

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.

Packaging

Package size based on protein content.

Physical properties

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.

Unit Definition

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.

Physical form

Lyophilized powder containing potassium phosphate buffer salts and stabilizer.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Célio X C Santos et al.
Journal of leukocyte biology, 86(4), 989-998 (2009-07-01)
PDI, a redox chaperone, is involved in host cell uptake of bacteria/viruses, phagosome formation, and vascular NADPH oxidase regulation. PDI involvement in phagocyte infection by parasites has been poorly explored. Here, we investigated the role of PDI in in vitro
The chaperone activity of protein disulfide isomerase is affected cyclophilin B and cyclosporin A in vitro
Horibe T, et al.
Journal of Biochemistry, 132(3), 401-407 (2002)
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)
Novel processing and localization of catA, ccdA associated thiol-disulfide oxidoreductase, in protein hyper-producing bacterium Brevibacillus choshinensis
Tanaka R, et al.
Protein and peptide letters, 12(1), 95-98 (2005)

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