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P7122

Sigma-Aldrich

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

enhanced validation

affinity isolated antibody, buffered aqueous solution

Sinônimo(s):

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

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About This Item

Número MDL:
Código UNSPSC:
12352203
NACRES:
NA.41

fonte biológica

rabbit

Nível de qualidade

conjugado

unconjugated

forma do anticorpo

affinity isolated antibody

tipo de produto de anticorpo

primary antibodies

clone

polyclonal

Formulário

buffered aqueous solution

peso molecular

antigen 57 kDa

reatividade de espécies

mouse, human, rat

embalagem

antibody small pack of 25 μL

validação aprimorada

independent
Learn more about Antibody Enhanced Validation

técnica(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

nº de adesão UniProt

Condições de expedição

dry ice

temperatura de armazenamento

−20°C

modificação pós-traducional do alvo

unmodified

Informações sobre genes

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

Descrição geral

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.

Imunogênio

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

Aplicação

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

Ações bioquímicas/fisiológicas

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.

forma física

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

Exoneração de responsabilidade

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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Código de classe de armazenamento

12 - Non Combustible Liquids

Classe de risco de água (WGK)

WGK 2

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


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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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