Analytical Data
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Gene name
pucL
- Application
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Alternative Names
pucL；yunL；Uric acid degradation bifunctional Protein PucL
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O32141
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Expression Region
1-494aa
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AA Sequence
MFTMDDLNQMDTQTLTDTLGSIFEHSSWIAERSAALRPFSSLSDLHRKMTGIVKAADRETQLDLIKKHPRLGTKKTMSDDSVREQQNAGLGKLEQQEYEEFLMLNEHYYDRFGFPFILAVKGKTKQDIHQALLARLESERETEFQQALIEIYRIARFRLADIITEKGETQMKRTMSYGKGNVFAYRTYLKPLTGVKQIPESSFAGRDNTVVGVDVTCEIGGEAFLPSFTDGDNTLVVATDSMKNFIQRHLASYEGTTTEGFLHYVAHRFLDTYSHMDTITLTGEDIPFEAMPAYEEKELSTSRLVFRRSRNERSRSVLKAERSGNTITITEQYSEIMDLQLVKVSGNSFVGFIRDEYTTLPEDGNRPLFVYLNISWQYENTNDSYASDPARYVAAEQVRDLASTVFHELETPSIQNLIYHIGCRILARFPQLTDVSFQSQNHTWDTVVEEIPGSKGKVYTEPRPPYGFQHFTVTREDAEKEKQKAAEKCRSLKA
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Molecular Weight
64.0 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
Related Products
Protein Description
The research on the pucL recombinant protein centers around its role in the Photosynthetic Unit of certain bacteria and its potential applications in biotechnology. PucL, a key component of the light-harvesting complex, is primarily found in purple bacteria, where it assists in capturing light energy for photosynthesis. Understanding the structure and function of pucL is crucial as it can contribute to the development of efficient bioenergy solutions and enhance our comprehension of photosynthetic processes. Recent advancements in molecular biology techniques have enabled the production of recombinant pucL, allowing researchers to analyze its properties in detail. This recombinant protein can be used for various applications, including the design of biosensors, the bioengineering of photosynthetic organisms, and the exploration of synthetic biology approaches to improve energy capture in non-photosynthetic bacteria. Moreover, the study of pucL may shed light on evolutionary processes in photosynthetic systems, providing insights into how these mechanisms have adapted over time. As the global demand for sustainable energy sources rises, the investigation of proteins like pucL stands as a promising avenue for developing innovative technologies that harness solar energy efficiently and sustainably.
