P3818
Protein Disulfide Isomerase from bovine liver
≥100 units/mg protein, lyophilized powder
Sinônimo(s):
PDI
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0.1 MG
R$ 1.333,00
250 μG
R$ 2.783,00
R$ 1.333,00
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0.1 MG
R$ 1.333,00
250 μG
R$ 2.783,00
About This Item
Número CAS:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54
R$ 1.333,00
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Formulário
lyophilized powder
Nível de qualidade
atividade específica
≥100 units/mg protein
peso molecular
107 kDa
composição
Protein, ~10% Lowry
temperatura de armazenamento
−20°C
cadeia de caracteres SMILES
[S](=O)(=O)(ON)c1c(cc(c(c1)C(=O)O)Cl)Cl
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)
chave InChI
DHUYKLYJBKXDBM-UHFFFAOYSA-N
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Descrição geral
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.[1] The enzyme is a glycoprotein with 12% total carbohydrate content comprising of mannose, galactose, N-acetyl neuraminic acid (NANA) and 2-acetamido-2-deoxyglucose.[2] PDI is an ubiquitous redox chaperone enzyme. It belongs to the, thioredoxin superfamily and is high conserved.[3]
Aplicação
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[3]
- in the in vitro translation reaction for the generation of disulfide bonds[4]
- in insulin-disulfide reduction assay and peptide binding assay[5]
- as a positive control in thiol-disulfide oxidoreductase activity assay[6]
Ações bioquímicas/fisiológicas
Protein Disulfide Isomerase (PDI) is mainly located in the endoplasmic reticulum (ER), where it assists in protein-folding and thiol-disulfide exchanges.[4] It aids protein refolding in vitro allowing recombinant proteins to achieve their native state.[7]
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.[8]
Embalagem
Package size based on protein content.
propriedades físicas
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.
Definição da unidade
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.
forma física
Lyophilized powder containing potassium phosphate buffer salts and stabilizer.
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 3
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Equipamento de proteção individual
Eyeshields, Gloves, type N95 (US)
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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)
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)
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
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)
Artigos
Cellular oxidative stress is countered by enzymatic scavengers and antioxidant modulators against reactive oxygen species damage.
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