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Merck

P7496

Sigma-Aldrich

Anti-Protein Disulfide Isomerase antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

別名:

Anti-Erp58, Anti-PDI

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About This Item

MDL番号:
UNSPSCコード:
12352203
NACRES:
NA.41

由来生物

rabbit

結合体

unconjugated

抗体製品の状態

IgG fraction of antiserum

抗体製品タイプ

primary antibodies

クローン

polyclonal

形状

buffered aqueous solution

分子量

antigen 57 kDa

化学種の反応性

mouse, bovine, rat, human

テクニック

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アクセッション番号

輸送温度

dry ice

保管温度

−20°C

ターゲットの翻訳後修飾

unmodified

遺伝子情報

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

詳細

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.

免疫原

protein disulfide isomerase purified from bovine liver.

アプリケーション

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

生物化学的/生理学的作用

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.

物理的形状

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

免責事項

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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保管分類コード

10 - Combustible liquids

WGK

nwg

引火点(°F)

Not applicable

引火点(℃)

Not applicable


適用法令

試験研究用途を考慮した関連法令を主に挙げております。化学物質以外については、一部の情報のみ提供しています。 製品を安全かつ合法的に使用することは、使用者の義務です。最新情報により修正される場合があります。WEBの反映には時間を要することがあるため、適宜SDSをご参照ください。

Jan Code

IXO11750:
P7496-VAR:
P7496-BULK:
P7496-200UL:


試験成績書(COA)

製品のロット番号・バッチ番号を入力して、試験成績書(COA) を検索できます。ロット番号・バッチ番号は、製品ラベルに「Lot」または「Batch」に続いて記載されています。

以前この製品を購入いただいたことがある場合

文書ライブラリで、最近購入した製品の文書を検索できます。

文書ライブラリにアクセスする

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

ライフサイエンス、有機合成、材料科学、クロマトグラフィー、分析など、あらゆる分野の研究に経験のあるメンバーがおります。.

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