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AB125602

Recombinant ヒト PDHA1 protein (His tag N-Terminus)

Recombinant Human PDHA1 protein (His tag N-Terminus)

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Recombinant Human PDHA1 protein (His tag N-Terminus) is a Human Full Length protein, in the 30 to 390 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE, WB.

別名を表示する

PHE1A, PDHA1, PDHE1-A type I

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SDS-PAGE - Recombinant Human PDHA1 protein (His tag N-Terminus) (AB125602)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human PDHA1 protein (His tag N-Terminus) (AB125602)

Key facts

精製度

>85% Densitometry

発現系

Escherichia coli

タグ

His tag N-Terminus

アプリケーション

SDS-PAGE, WB

applications

生物活性

No

アクセッション番号

P08559

アニマルフリー

No

キャリアフリー

No

種

Human

バッファー組成

pH: 7 Preservative: 1.02% Imidazole Constituents: 25% Glycerol (glycerin, glycerine), 1.75% Sodium chloride, 0.81% Sodium phosphate, 0.004% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.002% PMSF

storage-buffer

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組合せ製品

Reagents, Controls & Accessories

AB133411

Low Fluorescence Western Membrane (PVDF)

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  • 1
Proteins & Peptides

AB125580

Recombinant human PDK1 protein (GST tag N-Terminus)

Functional Studies - Recombinant human PDK1 protein (AB125580)

  • 0
  • 0
Proteins & Peptides

AB125560

Recombinant human PDK4 protein (GST tag N-Terminus)

Functional Studies - Recombinant human PDK4 protein (AB125560)

  • 0
  • 0
Proteins & Peptides

AB99238

Recombinant human MDH2 protein (His tag N-Terminus)

SDS-PAGE - Recombinant human MDH2 protein (His tag N-Terminus) (AB99238)

  • 0
  • 0
Proteins & Peptides

AB291253

Recombinant human GAPDH protein (Active)

Functional Studies - Recombinant human GAPDH protein (Active) (AB291253)

  • 0
  • 0
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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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配列情報

[{"linker":null,"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":"47 kDa","actualMolecularWeight":null,"aminoAcidEnd":390,"aminoAcidStart":30,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"P08559","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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出荷温度及び保存条件

製品の状態
Liquid
出荷温度
Dry Ice
短期保存温度
-80°C
長期保存温度
-80°C
分注に関する情報
Upon delivery aliquot
保管に関する情報
Avoid freeze / thaw cycle
False
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補足情報

This supplementary information is collated from multiple sources and compiled automatically.

PDHA1 also known as the pyruvate dehydrogenase E1 alpha subunit plays a mechanical role in cellular metabolism. It forms part of the larger pyruvate dehydrogenase (PDH) complex where it serves as a critical catalytic component. PDHA1 is expressed ubiquitously across different tissue types reflecting its fundamental function in energy production. The molecular weight of the PDHA1 protein is approximately 43 kDa. Alternate names for this protein include the PDH E1 component and it partners closely with other components in the PDH complex to facilitate its role.
Biological function summary

PDHA1 engages in the conversion of pyruvate into acetyl-CoA an important step in cellular respiration. This protein is part of the PDH complex which consists of multiple copies of three catalytic and two regulatory subunits. The conversion process is essential for linking glycolysis to the citric acid cycle efficiently channeling energy substrates within the cell. Furthermore the functional activity of PDHA1 is regulated through phosphorylation by the pyruvate dehydrogenase kinases (PDKs) and dephosphorylation by PDH phosphatases.

Pathways

PDHA1 is integral to the metabolic pathway of cellular respiration and energy production. It enables the transition between glycolysis and the citric acid cycle by facilitating the conversion of pyruvate to acetyl-CoA which enters the citric acid cycle. Related proteins in this pathway include PDHA2 and the regulatory PDKs that modulate PDHA1 activity. These interactions ensure energy metabolism adapts to various cellular conditions influencing energy balance and substrate utilization.

Mutations or dysfunctions in PDHA1 can lead to disorders such as pyruvate dehydrogenase deficiency and Leigh syndrome. These conditions result from impaired energy metabolism leading to severe neurological symptoms and overall energy deficits in tissues with high metabolic demands. The link between PDHA1 and diseases highlights the importance of maintaining its function. Additionally altered interaction with proteins involved in phosphorylation such as the PDKs can exacerbate pathogenic conditions by further disbalancing metabolic activities.
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一般的な情報

機能

Together with PDHB forms the heterotetrameric E1 subunit of the pyruvate dehydrogenase (PDH) complex (PubMed : 17474719, PubMed : 19081061). The PDH complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links cytoplasmic glycolysis and the mitochondrial tricarboxylic acid (TCA) cycle (PubMed : 19081061, PubMed : 7782287). It contains multiple copies of three enzymatic components : pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) (Probable). The E1 subunit catalyzes both the thiamine pyrophosphate (TPP)-dependent decarboxylation of pyruvate and the reductive acetylation of a lipoyl group covalently linked to the lipoyl-bearing domains of E2 (PubMed : 17474719, PubMed : 19081061, PubMed : 7782287).

翻訳後修飾

Phosphorylation at Ser-232, Ser-293 and Ser-300 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient. Dephosphorylation at all three sites, i.e. at Ser-232, Ser-293 and Ser-300, is required for reactivation.. Acetylation alters the phosphorylation pattern. Deacetylated by SIRT3 (By similarity).

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製品プロトコール

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ターゲットの情報

Together with PDHB forms the heterotetrameric E1 subunit of the pyruvate dehydrogenase (PDH) complex (PubMed : 17474719, PubMed : 19081061). The PDH complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links cytoplasmic glycolysis and the mitochondrial tricarboxylic acid (TCA) cycle (PubMed : 19081061, PubMed : 7782287). It contains multiple copies of three enzymatic components : pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) (Probable). The E1 subunit catalyzes both the thiamine pyrophosphate (TPP)-dependent decarboxylation of pyruvate and the reductive acetylation of a lipoyl group covalently linked to the lipoyl-bearing domains of E2 (PubMed : 17474719, PubMed : 19081061, PubMed : 7782287).
See full target information PDHA1
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