P3818
Protein Disulfide Isomerase from bovine liver
≥100 units/mg protein, lyophilized powder
Synonym(s):
PDI
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Recommended Products
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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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)
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)
Recognition and ER Quality Control of Misfolded Formylglycine-Generating Enzyme by Protein Disulfide Isomerase
Schlotawa L, et al.
Testing, 24(1), 27-37 (2018)
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)
Articles
Cellular oxidative stress is countered by enzymatic scavengers and antioxidant modulators against reactive oxygen species damage.
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