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Key Documents

P7122

Sigma-Aldrich

Anti-Protein Disulfide Isomerase (DL-11) antibody produced in rabbit

enhanced validation

affinity isolated antibody, buffered aqueous solution

Sinonimo/i:

Prolyl 4-hydroxylase subunit β (P4HB), Anti-Erp58, Anti-PDI

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About This Item

Numero MDL:
Codice UNSPSC:
12352203
NACRES:
NA.41

Origine biologica

rabbit

Livello qualitativo

Coniugato

unconjugated

Forma dell’anticorpo

affinity isolated antibody

Tipo di anticorpo

primary antibodies

Clone

polyclonal

Forma fisica

buffered aqueous solution

PM

antigen 57 kDa

Reattività contro le specie

mouse, human, rat

Confezionamento

antibody small pack of 25 μL

Convalida avanzata

independent
Learn more about Antibody Enhanced Validation

tecniche

immunoprecipitation (IP): 1-2 μg using RIPA lysate (250-500 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

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

human ... P4HB(5034)
mouse ... P4hb(18453)
rat ... P4hb(25506)

Descrizione generale

Prolyl 4-hydroxylase subunit β (P4HB) is a redox-regulated thiol-containing protein. The gene encoding this protein is localized on human chromosome 17q25.3.
Protein Disulfide Isomerase is an abundant multifunctional, soluble enzyme (E.C. 5.3.4.1). PDI is expressed in cellular localizations such as the cell surface, cytosol and nucleus. PDI consists of four tandem domains, two of which contain a catalytic site for S-S bond formation. One domain is the main site of noncovalent interaction with other peptides or proteins. PDI has an N-terminal ER signal and C-terminal ER retention KDEL signal sequences.

Immunogeno

synthetic peptide corresponding to amino acid residues 498-508 of human protein disulfide isomerase.

Applicazioni

Anti-Protein Disulfide Isomerase (DL-11) antibody produced in rabbit has been used in:
  • immunofluorescence
  • immunoprecipitation
  • immunoblotting

Azioni biochim/fisiol

Prolyl 4-hydroxylase subunit β (P4HB) 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 serves as a molecular chaperone, that can suppress protein aggregation. PDI has functions as an essential component of two protein complexes: the heterotetramer collagen prolyl 4-hydroxylase and the heterodimer microsomal triglyceride transfer protein. PDI 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 catalyzes the formation of isopeptide bonds.

Stato fisico

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide.

Esclusione di responsabilità

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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Codice della classe di stoccaggio

12 - Non Combustible Liquids

Classe di pericolosità dell'acqua (WGK)

WGK 2

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

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Blake R Chaffee et al.
Development (Cambridge, England), 141(17), 3388-3398 (2014-08-21)
Lens epithelial cells and early lens fiber cells contain the typical complement of intracellular organelles. However, as lens fiber cells mature they must destroy their organelles, including nuclei, in a process that has remained enigmatic for over a century, but
Lia S Nakao et al.
The Journal of biological chemistry, 290(9), 5685-5695 (2015-01-07)
Thioredoxin (Trx)-fold proteins are protagonists of numerous cellular pathways that are subject to thiol-based redox control. The best characterized regulator of thiols in proteins is Trx1 itself, which together with thioredoxin reductase 1 (TR1) and peroxiredoxins (Prxs) comprises a key
Mechanism of the antichaperone activity of protein disulfide isomerase: facilitated assembly of large, insoluble aggregates of denatured lysozyme and PDI
Sideraki V and Gilbert HF
Biochemistry, 39(5), 1180-1188 (2000)
Red/ox states of human protein disulfide isomerase regulate binding affinity of 17 beta-estradiol.
Karamzadeh R
Archives of Biochemistry and Biophysics (2017)
Protein disulfide isomerase: Structure, mechanism of oxidative protein folding and multiple functional roles
Khan R, et al.
Journal of Biochemistry and Molecular Biology Research, 2(3), 173-179 (2016)

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