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AB286038

Recombinant Pyruvate phosphate dikinase protein (Active)

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Recombinant Pyruvate phosphate dikinase protein (Active) is a Full Length protein, in the 1 to 878 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, FuncS.
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Functional Studies - Recombinant Pyruvate phosphate dikinase protein (Active) (AB286038)
  • FuncS

Supplier Data

Functional Studies - Recombinant Pyruvate phosphate dikinase protein (Active) (AB286038)

Specific activity of PPDK ≥0.8 U/mg. PPDK reacts with 0.5 mM of PPi at pH 7 and 37°C. Pyruvate production rate was detected at 570 nm.

SDS-PAGE - Recombinant Pyruvate phosphate dikinase protein (Active) (AB286038)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Pyruvate phosphate dikinase protein (Active) (AB286038)

SDS-PAGE analysis of ab286038 loaded under reducing conditions and stained with Coomassie Blue.

M : MW markers

Lane 1 : ab286038 (1 μg) – purified PPDK.

Lane 2 : ab286038 (3 μg) - purified PPDK

The protein shows a predicted MW of ~ 95.5 kDa

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag C-Terminus

Applications

FuncS, SDS-PAGE

applications

Biologically active

Yes

Biological activity

Specific activity of PPDK ≥0.8 U/mg. PPDK reacts with 0.5 mM of PPi at pH 7 and 37°C. Pyruvate production rate was detected at 570 nm.

Animal free

Yes

Carrier free

No

Storage buffer

pH: 7 Preservative: 0.34% Imidazole Constituents: 50% Glycerol (glycerin, glycerine), 0.1321% Ammonium sulphate, 0.095% Magnesium chloride

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>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Product details

This product is manufactured by BioVision, an Abcam company and was previously called P1161 PDK, Active, M. rosea Recombinant. P1161-50 is the same size as the 50 μg size of ab286038.

Sequence info

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":"95.5 kDa","actualMolecularWeight":null,"aminoAcidEnd":878,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":null,"accessionNumber":null,"tags":[{"tag":"His","terminus":"C-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
True

Supplementary information

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

Pyruvate phosphate dikinase (PPDK) is an enzyme that catalyzes the conversion of pyruvate ATP and inorganic phosphate into phosphoenolpyruvate AMP and pyrophosphate. It is also known by its alternate name PPDK. The enzyme has a molecular mass of approximately 95 kDa. PPDK is expressed in a wide variety of organisms including plants some bacteria and certain protozoa. It plays an important role in cellular energy metabolism particularly in environments where anaerobic conditions require alternate metabolic strategies.
Biological function summary

PPDK offers a significant contribution to the processes of photosynthesis and gluconeogenesis in plants. In C4 plants PPDK acts as a part of the C4 photosynthetic pathway which efficiently fixes CO2 via a complex series of reactions. This enzyme is not typically found in animals highlighting its unique role in organisms that employ such specialized processes. Additionally it functions as a monomer unlike some enzymes which operate only as part of a multimeric complex.

Pathways

PPDK is an integral component of the C4 and CAM (Crassulacean Acid Metabolism) photosynthesis pathways. In these pathways it facilitates the regeneration of phosphoenolpyruvate acting in tandem with enzymes like phosphoenolpyruvate carboxylase. This relationship allows organisms to optimize energy use and carbon fixation under specific environmental conditions. In glycolysis and gluconeogenesis PPDK manipulates energy balance and carbon flow alongside other metabolic proteins.

PPDK is linked to parasitic infections notably those caused by Giardia lamblia. The enzyme's unique expression in these organisms makes it a potential target for treatments aimed at disrupting energy metabolism in the parasite. In this context researchers investigate D-lactate dehydrogenase as a related protein also vital for the energy metabolism of these parasites to find effective therapeutic strategies. Understanding PPDK's role in these conditions might lead to novel interventions for parasite-induced diseases.

Specifications

Form

Liquid

General info

Product protocols

Product promise

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