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AB275559

Recombinant Human Pyruvate Dehydrogenase E2 protein (His tag)

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Recombinant Human Pyruvate Dehydrogenase E2 protein (His tag) is a Human Fragment protein, in the 374 to 631 aa range, expressed in Escherichia coli, with >95%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE.

View Alternative Names

DLTA, DLAT, 70 kDa mitochondrial autoantigen of primary biliary cirrhosis, Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex, M2 antigen complex 70 kDa subunit, Pyruvate dehydrogenase complex component E2, PBC, PDC-E2, PDCE2

1 Images
SDS-PAGE - Recombinant Human Pyruvate Dehydrogenase E2 protein (His tag) (AB275559)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human Pyruvate Dehydrogenase E2 protein (His tag) (AB275559)

SDS-PAGE analysis of ab275559.

Key facts

Purity

>95% SDS-PAGE

Endotoxin level

< 1 EU/µg

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

P10515

Animal free

No

Carrier free

No

Species

Human

Reconstitution

Reconstitute in PBS (pH7.4) to a concentration of 0.1-1.0 mg/mL. Do not vortex.

Storage buffer

pH: 7.4 Preservative: 0.82% Proclin 300 Constituents: PBS, 81.9% Trehalose, 0.25% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.16% Sodium-N-Lauroylsarcosinate

storage-buffer

Reactivity data

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

Sequence info

[{"sequence":"QVKGTGPDGRITKKDIDSFVPSKVAPAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLLVRKELNKILEGRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLVPADNEKGFDVASMMSVTLSCDHRVVDGAVGAQW","proteinLength":"Fragment","predictedMolecularWeight":"28.7 kDa","actualMolecularWeight":null,"aminoAcidEnd":631,"aminoAcidStart":374,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P10515","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

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

Pyruvate Dehydrogenase E2 (PDH-E2) also referred to as PDC-E2 or E2 protein is a central component of cellular metabolism. It is the inner core dihydrolipoamide acetyltransferase component of the pyruvate dehydrogenase complex. PDH-E2 facilitates the conversion of pyruvate to acetyl-CoA which is an important step in aerobic respiration. The E2 protein is expressed in the mitochondria where it actively engages in its enzymatic roles. With a molecular weight of approximately 55 kDa PDH-E2 functions through its interaction with other components of the pyruvate dehydrogenase complex.
Biological function summary

PDH-E2 plays a significant role in cellular energy production. It is an important part of the pyruvate dehydrogenase complex where its coordinated enzymatic activity drives the decarboxylation of pyruvate. This activity supplies acetyl-CoA for the citric acid cycle essential for ATP production. PDH-E2's function regulates the flow of carbon within cells linking glycolysis and the citric acid cycle making it essential for energy homeostasis. Its function integrates signals that regulate metabolic pathways helping maintain cellular energy balance.

Pathways

PDH-E2 integrates the glycolysis and citric acid cycle facilitating efficient energy production. It interacts with tightly linked enzymes in the pyruvate dehydrogenase complex important for catalyzing the conversion processes. Key related proteins include pyruvate dehydrogenase (E1) and dihydrolipoamide dehydrogenase (E3) which form the complex alongside E2. This complex is also critical in adjusting metabolic responses based on cellular energy needs efficiently managing substrate flux into the mitochondria.

Dysfunctional PDH-E2 activity associates with metabolic conditions like pyruvate dehydrogenase deficiency and primary biliary cholangitis (PBC). PDH deficiency leads to lactic acidosis and neurological dysfunction due to impaired energy production. In PBC the immune system aberrantly targets the E2 component causing liver damage and leading to cholestasis. These diseases highlight the critical role of PDH-E2 and its interaction with other mitochondrial proteins in maintaining metabolic health.

Specifications

Form

Lyophilized

General info

Function

The pyruvate dehydrogenase (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 (Probable). It contains multiple copies of three enzymatic components : pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and dihydrolipoamide dehydrogenase (E3); (Probable). Within this complex, the catalytic function of this enzyme is to accept, and to transfer to coenzyme A, acetyl groups from acetyl-lipoyl moiety generated by the pyruvate dehydrogenase, leading to acetyl-CoA formation (Probable).

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Post-translational modifications

Delipoylated at Lys-132 and Lys-259 by SIRT4, delipoylation decreases the PHD complex activity.

Subcellular localisation

Mitochondrion matrix

Product protocols

Target data

The pyruvate dehydrogenase (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 (Probable). It contains multiple copies of three enzymatic components : pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and dihydrolipoamide dehydrogenase (E3); (Probable). Within this complex, the catalytic function of this enzyme is to accept, and to transfer to coenzyme A, acetyl groups from acetyl-lipoyl moiety generated by the pyruvate dehydrogenase, leading to acetyl-CoA formation (Probable).
See full target information DLAT

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