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Key Documents

18248

Sigma-Aldrich

Protein Disulfide Isomerase from bovine liver

≥150 U/mg protein (protein ca. 40%)

Synonyme(s) :

PDI

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro MDL:
Code UNSPSC :
12352204

Forme

powder
powder with small lumps

Activité spécifique

≥150 U/mg protein (protein ca. 40%)

Poids mol.

107 kDa by gel filtration
57 kDa by SDS-PAGE

Conditions d'expédition

wet ice

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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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

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.

Autres remarques

Enzyme that accelerates the exchange reaction between disulfide bridges in proteins

Remplacé(e)(s) par


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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.
Louise H Boyle et al.
Proceedings of the National Academy of Sciences of the United States of America, 110(9), 3465-3470 (2013-02-13)
Tapasin is an integral component of the peptide-loading complex (PLC) important for efficient peptide loading onto MHC class I molecules. We investigated the function of the tapasin-related protein, TAPBPR. Like tapasin, TAPBPR is widely expressed, IFN-γ-inducible, and binds to MHC
Franz-Xaver Kober et al.
The Journal of biological chemistry, 288(3), 2029-2039 (2012-11-30)
About one-third of all cellular proteins pass through the secretory pathway and hence undergo oxidative folding in the endoplasmic reticulum (ER). Protein-disulfide isomerase (PDI) and related members of the PDI family assist in the folding of substrates by catalyzing the
Joohyun Ryu et al.
Biochemical and biophysical research communications, 430(2), 610-615 (2012-12-12)
Anterior Gradient 2 (AGR2), an ER stress-inducible protein, has been reported to be localized in endoplasmic reticulum (ER) and its level is elevated in numerous metastatic cancers. Recently, it has been demonstrated that AGR2 is involved in the control of
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

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