P7372
Anti-Protein Disulfide Isomerase (MD-12) antibody produced in rabbit
affinity isolated antibody, buffered aqueous solution
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Synonym(s):
Anti-Erp58, Anti-PDI
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biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen 57 kDa
species reactivity
human, bovine, rat, mouse
enhanced validation
independent
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technique(s)
immunoprecipitation (IP): 2-5 μg using RIPA lysate (500 μg) of rat NRK cells
indirect immunofluorescence: 2-5 μg/mL using human HeLa cells
western blot (chemiluminescent): 0.1-0.2 μg/mL using whole extract of mouse NIH3T3 cells
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... P4HB(5034)
mouse ... P4hb(18453)
rat ... P4hb(25506)
Related Categories
General description
Anti-Protein Disulfide Isomerase (PDI) (MD-12) is developed in rabbit using as immunogen a synthetic peptide corresponding to amino acid residues of human PDI with N-terminal added cysteine, conjugated to KLH. 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. The mammalian PDI family comprises several highly divergent proteins that contain one or more thioredoxin like structural domains. PDI consists of four tandem domains, two of which contain a catalytic site for S-S bond formation. PDI has an N-terminal ER signal and C-terminal ER retention KDEL signal sequences. PDI may also be expressed in other cellular localizations such as the cell surface, cytosol, and nucleus. PDI was found on the cell surface of several cell types including platelets, lymphoid cells, pancreatic exocrine cells, retinal cells, thyroid cells, and hepatocytes.
Immunogen
synthetic peptide corresponding to amino acid residues 495-506 of human protein disulfide isomerase.
Application
Anti-Protein Disulfide Isomerase (MD-12) antibody produced in rabbit has been used in:
- immunoblotting
- immunoprecipitation
- immunofluorescence
Biochem/physiol Actions
Protein disulfide isomerase (PDI) catalyses the formation and rearrangements of both intrachain and interchain disulfide bonds in secreted proteins. PDI also serves as a molecular chaperone that can suppress protein aggregation, or as an anti-chaperone that mediates aggregate formation. PDI respectively participates in the hydroxylation of prolines in procollagen during collagen synthesis and in the transfer of neutral lipid onto nascent lipoprotein particles. PDI has calcium-dependent transglutaminase activity, which catalyses the formation of isopeptide bonds.
Physical form
Solution in 0.01 M phosphate buffered saline containing 1% bovine serum abumin and 15 mM sodium azide.
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.
WGK
nwg
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
含少量动物源组分生物产品
常规特殊物品
Certificates of Analysis (COA)
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Hongge Wang et al.
Molecular and cellular biology, 42(6), e0052221-e0052221 (2022-05-03)
Ferroptosis is a form of regulated cell death resulting predominantly from catastrophic accumulation of lipid reactive oxygen species (ROS). While the antioxidant systems that counter ferroptosis have been well characterized, the mechanism underlying ferroptosis-associated accumulation of lipid ROS remains unclear.
Dual targeting of the protein disulfide isomerase RB60 to the chloroplast and the endoplasmic reticulum
Levitan A, et al.
Proceedings of the National Academy of Sciences of the USA, 102(17), 6225-6230 (2005)
Protein disulfide isomerase. A multifunctional protein resident in the lumen of the endoplasmic reticulum.
Noiva R and Lennarz WJ
The Journal of Biological Chemistry, 267(6), 3553-3556 (1992)
Ming-Jie Hou et al.
Acta biochimica et biophysica Sinica, 55(5), 853-865 (2023-05-30)
Ferroptosis is a new form of nonapoptotic cell death closely associated with glutathione (GSH) peroxidase 4 inhibition and/or GSH depletion, resulting in the accumulation of cellular iron and lipid peroxides. The exact mechanism by which GSH depletion causes the accumulation
Xinmiao Fu et al.
The Biochemical journal, 447(1), 115-123 (2012-07-04)
E(2) (17β-oestradiol), a female sex hormone, has important biological functions in a woman's body. The pancreas, often considered a non-classical E(2)-targeting organ, is known to be functionally regulated by E(2), but little is known about how oestrogen actions are regulated
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