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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

Synonyme(s) :

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

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen 57 kDa

Espèces réactives

mouse, human, rat

Conditionnement

antibody small pack of 25 μL

Validation améliorée

independent
Learn more about Antibody Enhanced Validation

Technique(s)

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

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

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

Description générale

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.

Immunogène

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

Application

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

Actions biochimiques/physiologiques

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.

Forme physique

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

Clause de non-responsabilité

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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Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

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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