Analytical Data
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Gene name
PPAT
- Application
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Alternative Names
Amidophosphoribosyltransferase. ATase. EC:2.4.2.14. Glutamine phosphoribosylpyrophosphate amidotransferase. GPAT
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q06203
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Expression Region
1-517 aa
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AA Sequence
MELEELGIREECGVFGCIASGEWPTQLDVPHVITLGLVGLQHRGQESAGIVTSDGSSVPTFKSHKGMGLVNHVFTEDNLKKLYVSNLGIGHTRYATTGKCELENCQPFVVETLHGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTPPQEQDDTPDWVARIKNLMKEAPTAYSLLIMHRDVIYAVRDPYGNRPLCIGRLIPVSDINDKEKKTSETEGWVVSSESCSFLSIGARYYREVLPGEIVEISRHNVQTLDIISRSEGNPVAFCIFEYVYFARPDSMFEDQMVYTVRYRCGQQLAIEAPVDADLVSTVPESATPAALAYAGKCGLPYVEVLCKNRYVGRTFIQPNMRLRQLGVAKKFGVLSDNFKGKRIVLVDDSIVRGNTISPIIKLLKESGAKEVHIRVASPPIKYPCFMGINIPTKEELIANKPEFDHLAEYLGANSVVYLSVEGLVSSVQEGIKFKKQKEKKHDIMIQENGNGLECFEKSGHCTACLTGKYPVELEW
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Molecular Weight
83.8 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
The study of PPAT (phosphopantetheine adenylyltransferase) recombinant protein is of significant interest in the fields of biochemistry and molecular biology due to its crucial role in coenzyme A biosynthesis. Coenzyme A is vital for various metabolic pathways, including fatty acid metabolism, the citric acid cycle, and the synthesis of bioactive lipids. Understanding the structure and function of PPAT can provide insights into its mechanisms of action and regulation, which are essential for the proper functioning of cellular metabolism. The recombinant expression of PPAT allows for detailed investigations into its enzymatic properties, kinetics, and interactions with other cellular components. Additionally, studying PPAT may unveil potential therapeutic targets for diseases associated with metabolic dysregulation. Advances in recombinant DNA technology have made it possible to produce high yields of PPAT, enabling researchers to conduct extensive studies on its biological role and potential applications in biotechnology and medicine. Furthermore, the exploration of PPAT as a target for drug discovery has gained momentum, as inhibitors of this enzyme may offer novel strategies for treating conditions linked to altered coenzyme A levels. Through the production and characterization of recombinant PPAT, researchers aim to enhance our understanding of metabolic processes and contribute to the development of innovative therapeutic approaches.
