18248
Protein Disulfide Isomerase from bovine liver
≥150 U/mg protein (protein ca. 40%)
Synonym(s):
PDI
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
form
powder
powder with small lumps
specific activity
≥150 U/mg protein (protein ca. 40%)
mol wt
107 kDa by gel filtration
57 kDa by SDS-PAGE
shipped in
wet ice
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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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
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.
Other Notes
Enzyme that accelerates the exchange reaction between disulfide bridges in proteins
replaced by
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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.
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
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
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
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
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