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P7372

Sigma-Aldrich

Anti-Protein Disulfide Isomerase (MD-12) antibody produced in rabbit

enhanced validation

affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-Erp58, Anti-PDI

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About This Item

MDL number:
MFCD01094568
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

200

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
Learn more about Antibody Enhanced Validation

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.

P07237

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.

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Certificates of Analysis (COA)

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Formation of transitory intrachain and interchain disulfide bonds accompanies the folding and oligomerization of simian virus 40 Vp1 in the cytoplasm
Li PP, et al.
Proceedings of the National Academy of Sciences of the USA, 99(3), 1353-1358 (2002)
Facilitated protein aggregation effects of calcium on the chaperone and anti-chaperone activity of protein disulfide-isomerase
Primm TP, et al.
The Journal of Biological Chemistry, 271(52), 33664-33669 (1996)
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
Isabel Fernández de Castro Martin et al.
Nature communications, 8(1), 1396-1396 (2017-11-11)
Transport of neo-synthesized influenza A virus (IAV) viral ribonucleoproteins (vRNPs) from the nucleus to the plasma membrane involves Rab 11 but the precise mechanism remains poorly understood. We used metal-tagging and immunolabeling to visualize viral proteins and cellular endomembrane markers
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)
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