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Merck
모든 사진(2)

주요 문서

P7496

Sigma-Aldrich

Anti-Protein Disulfide Isomerase antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

동의어(들):

Anti-Erp58, Anti-PDI

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About This Item

MDL number:
UNSPSC 코드:
12352203
NACRES:
NA.41

생물학적 소스

rabbit

Quality Level

결합

unconjugated

항체 형태

IgG fraction of antiserum

항체 생산 유형

primary antibodies

클론

polyclonal

양식

buffered aqueous solution

분자량

antigen 57 kDa

종 반응성

mouse, bovine, rat, human

기술

immunoprecipitation (IP): 10-20 μg using RIPA lysate from rat NRK cells
indirect immunofluorescence: 1:250 using human HeLa cells
western blot: 1:2,000 using whole extract of mouse NIH3T3 cells

UniProt 수납 번호

배송 상태

dry ice

저장 온도

−20°C

타겟 번역 후 변형

unmodified

유전자 정보

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

일반 설명

Prolyl 4-hydroxylase subunit β (P4HB) or protein disulfide isomerase is a redox-regulated thiol-containing protein. The gene encoding this protein is localized on human chromosome 17q25.3.
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. It consists of four tandem domains, two of which contain a catalytic site for disulfide bond formation. A mitochondrial isoform of PDI (approx. 54 kDa) has been recently described. PDI has an N-terminal endoplasmic reticulum (ER) signal and a C-terminal ER- retention KDEL signal sequences. PDI was found on the cell surface of several cell types including endothelial cells, platelets and hepatocytes.

면역원

protein disulfide isomerase purified from bovine liver.

애플리케이션

Anti-Protein Disulfide Isomerase antibody produced in rabbit has been used in immunoblotting, immunoprecipitation and immunofluorescence.

생화학적/생리학적 작용

Prolyl 4-hydroxylase subunit β (P4HB) or protein disulfide isomerase 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 (PDI) catalyzes the formation and rearrangements of both intrachain and interchain disulfide bonds in secreted proteins. It plays an important role in various cellular processes including cell adhesion. PDI has calcium-dependent transglutaminase activity and is involved in the catalysis of isopeptide bond formation. PDI participates in the hydroxylation of proline in procollagen during collagen synthesis and in the transfer of neutral lipid onto nascent lipoprotein particles. Estrogen binding by PDI has also been reported.

물리적 형태

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

면책조항

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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Storage Class Code

10 - Combustible liquids

WGK

nwg

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable


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문서 라이브러리 방문

The Nuclear Pore Complex Function of Sec13 Protein Is Required for Cell Survival during Retinal Development*
Xubo Niu
The Journal of Biological Chemistry (2014)
Novel roles for protein disulphide isomerase in disease states: a double edged sword?
Parakh S and Atkin JD
Frontiers in Cell and Developmental Biology, 3, 30-30 (2015)
Quantitative Transcriptomic Profiling of Branching in a
Glycosphingolipid Biosynthetic Pathway
Hiromu Takematsu
The Journal of Biological Chemistry (2011)
Characterization of the estradiol-binding site structure of human protein disulfide isomerase (PDI)
Fu XM, et al.
Testing, 6(11), e27185-e27185 (2011)
Hiromu Takematsu et al.
The Journal of biological chemistry, 286(31), 27214-27224 (2011-06-15)
Cellular biosynthesis of macromolecules often involves highly branched enzyme pathways, thus cellular regulation of such pathways could be rather difficult. To understand the regulatory mechanism, a systematic approach could be useful. We genetically analyzed a branched biosynthetic pathway for glycosphingolipid

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