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.
James J Galligan et al.
Human genomics, 6, 6-6 (2012-12-19)
Enzyme-mediated disulfide bond formation is a highly conserved process affecting over one-third of all eukaryotic proteins. The enzymes primarily responsible for facilitating thiol-disulfide exchange are members of an expanding family of proteins known as protein disulfide isomerases (PDIs). These proteins
Harshavardhan Kenche et al.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 27(3), 965-977 (2012-11-22)
The endoplasmic reticulum (ER) stress response (ERSR) and associated protein aggregation, is under investigation for its role in human diseases, including chronic obstructive pulmonary disease (COPD) where cigarette smoking (CS) is a risk factor for disease development. Our hypothesis states
[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)
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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