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Documentos Principais

18248

Sigma-Aldrich

Protein Disulfide Isomerase from bovine liver

≥150 U/mg protein (protein ca. 40%)

Sinônimo(s):

PDI

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About This Item

Número CAS:
Número da licença da enzima:
Número MDL:
Código UNSPSC:
12352204

Formulário

powder
powder with small lumps

atividade específica

≥150 U/mg protein (protein ca. 40%)

peso molecular

107 kDa by gel filtration
57 kDa by SDS-PAGE

Condições de expedição

wet ice

temperatura de armazenamento

−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)

chave InChI

DHUYKLYJBKXDBM-UHFFFAOYSA-N

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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

1 unit corresponds to the amount of enzyme, which, in a glutathione-dithiothreitol-system, causes a change of absorbance of 0.001 per minute at pH 4.0 and 25°C.

Outras notas

Enzyme that accelerates the exchange reaction between disulfide bridges in proteins[1]

substituído por


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Pamela A Wearsch et al.
Methods in molecular biology (Clifton, N.J.), 960, 67-79 (2013-01-19)
The stability of the MHC (major histocompatibility complex) class I peptide repertoire is optimized during assembly in the endoplasmic reticulum (ER) and depends on the collective function of components of the peptide-loading complex (PLC). The chaperone-like molecule tapasin is the
Zegbeh Z Kpadeh et al.
Journal of bacteriology, 195(8), 1825-1833 (2013-02-26)
The extracytoplasmic assembly of the Dot/Icm type IVb secretion system (T4SS) of Legionella pneumophila is dependent on correct disulfide bond (DSB) formation catalyzed by a novel and essential disulfide bond oxidoreductase DsbA2 and not by DsbA1, a second nonessential DSB
Florian Langer et al.
Blood, 121(12), 2324-2335 (2013-01-15)
Lymphocyte depletion with antithymocyte globulin (ATG) can be complicated by systemic coagulation activation. We found that ATG activated tissue factor procoagulant activity (TF PCA) on monocytic cells more potently than other stimuli that decrypt TF, including cell disruption, TF pathway
[Protein disulfide bond formation system in mammalian cells].
Yoshimi Sato et al.
Seikagaku. The Journal of Japanese Biochemical Society, 84(9), 767-772 (2012-12-04)
Pryank Patel et al.
Journal of molecular biology, 425(5), 929-943 (2013-01-01)
Anterior gradient 2 (AGR2) is a normal endoplasmic reticulum protein that has two important abnormal functions, amphibian limb regeneration and human cancer metastasis promotion. These normal intracellular and abnormal extracellular roles can be attributed to the multidomain structure of AGR2.

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