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Merck
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P7122

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

affinity isolated antibody, buffered aqueous solution

Synonym(s):

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

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About This Item

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

Key Documents

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Product Name

Anti-Protein Disulfide Isomerase (DL-11) antibody produced in rabbit, affinity isolated antibody, buffered aqueous solution

biological source

rabbit

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

mouse, human, rat

packaging

antibody small pack of 25 μL

enhanced validation

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

UniProt accession no.

P07237

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Quality Level

200

Gene Information

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

Related Categories

Application

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

Biochem/physiol Actions

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.

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.

General description

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.

Immunogen

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

Physical form

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

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Storage Class

12 - Non Combustible Liquids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

Regulatory Information

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Certificates of Analysis (COA)

Lot/Batch Number
0000243318
0000232652
0000243318
0000232652
066M4867

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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)
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
Jun-Yi Zhu et al.
Disease models & mechanisms, 16(12) (2023-11-16)
People of African ancestry who carry the APOL1 risk alleles G1 or G2 are at high risk of developing kidney diseases through not fully understood mechanisms that impair the function of podocytes. It is also not clear whether the APOL1-G1
Interchain disulfide bonds promote protein cross-linking during protein folding
Gao Y and Mehta K
Journal of Biochemistry, 129(1), 179-183 (2001)
Red/ox states of human protein disulfide isomerase regulate binding affinity of 17 beta-estradiol.
Karamzadeh R
Archives of Biochemistry and Biophysics (2017)
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Related Content

Data Sheet - P7122

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