P7496
Anti-Protein Disulfide Isomerase antibody produced in rabbit
IgG fraction of antiserum, buffered aqueous solution
别名:
Anti-Erp58, Anti-PDI
产品名称
Anti-Protein Disulfide Isomerase antibody produced in rabbit, IgG fraction of antiserum, buffered aqueous solution
biological source
rabbit
conjugate
unconjugated
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen 57 kDa
species reactivity
mouse, bovine, rat, human
technique(s)
immunoprecipitation (IP): 10-20 μg using RIPA lysate from rat NRK cells
indirect immunofluorescence: 1:250 using human HeLa cells
western blot: 1:2,000 using whole extract of mouse NIH3T3 cells
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... P4HB(5034)
mouse ... P4hb(18453)
rat ... P4hb(25506)
Application
Anti-Protein Disulfide Isomerase antibody produced in rabbit has been used in immunoblotting, immunoprecipitation and immunofluorescence.
Biochem/physiol Actions
Prolyl 4-hydroxylase subunit β (P4HB) or protein disulfide isomerase acts as a molecular chaperone in the endoplasmic reticulum of cells and also as an oxidoreductase. It associates with steroid hormones and modulates their actions, concentrations and storage. P4HB accelerates the formation of disulphide bonds in proteins and hence aids in their folding.
Protein Disulfide Isomerase (PDI) catalyzes the formation and rearrangements of both intrachain and interchain disulfide bonds in secreted proteins. It plays an important role in various cellular processes including cell adhesion. PDI has calcium-dependent transglutaminase activity and is involved in the catalysis of isopeptide bond formation. PDI participates in the hydroxylation of proline in procollagen during collagen synthesis and in the transfer of neutral lipid onto nascent lipoprotein particles. Estrogen binding by PDI has also been reported.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
General description
Prolyl 4-hydroxylase subunit β (P4HB) or protein disulfide isomerase is a redox-regulated thiol-containing protein. The gene encoding this protein is localized on human chromosome 17q25.3.
Protein Disulfide Isomerase (PDI, Erp58) is an abundant multifunctional, soluble enzyme (E.C. 5.3.4.1) that resides in the lumen of the endoplasmic reticulum of eukaryotic cells. It consists of four tandem domains, two of which contain a catalytic site for disulfide bond formation. A mitochondrial isoform of PDI (approx. 54 kDa) has been recently described. PDI has an N-terminal endoplasmic reticulum (ER) signal and a C-terminal ER- retention KDEL signal sequences. PDI was found on the cell surface of several cell types including endothelial cells, platelets and hepatocytes.
Immunogen
protein disulfide isomerase purified from bovine liver.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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存储类别
10 - Combustible liquids
wgk
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
常规特殊物品
此项目有
Henry D Galvin et al.
The Journal of biological chemistry, 294(52), 20207-20221 (2019-11-24)
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Novel roles for protein disulphide isomerase in disease states: a double edged sword?
Parakh S and Atkin JD
Frontiers in Cell and Developmental Biology, 3, 30-30 (2015)
The Nuclear Pore Complex Function of Sec13 Protein Is Required for Cell Survival during Retinal Development*
Xubo Niu
The Journal of Biological Chemistry (2014)
Quantitative Transcriptomic Profiling of Branching in a
Glycosphingolipid Biosynthetic Pathway
Glycosphingolipid Biosynthetic Pathway
Hiromu Takematsu
The Journal of Biological Chemistry (2011)
Characterization of the estradiol-binding site structure of human protein disulfide isomerase (PDI)
Fu XM, et al.
Testing, 6(11), e27185-e27185 (2011)
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