Analytical Data
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Gene name
crnA
- Application
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Alternative Names
Creatininase
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Species
Pseudomonas putida
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P83772
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Expression Region
1-260aa
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Molecular Weight
55.6 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 study of crnA recombinant protein is rooted in the growing interest in understanding the functional role of proteins in various biological processes. crnA, a gene known to encode a protein involved in critical cellular functions, has gained attention for its potential implications in areas such as cellular signaling, metabolism, and disease mechanisms. Research has shown that recombinant proteins can be produced using various expression systems, allowing for detailed functional assays and structural analyses. The ability to generate crnA recombinant protein facilitates the investigation of its interaction with other biomolecules, which can provide insights into its physiological roles and potential therapeutic applications. Furthermore, the exploration of crnA protein has opened avenues for the development of novel biotechnological tools and medicines. As the demand for proteins with specific functions in research and therapeutic contexts increases, understanding the properties and functionalities of crnA through recombinant technology is becoming increasingly significant for advancing molecular biology, biochemistry, and medical science. This research aims to elucidate the structure-function relationships of crnA and its mechanisms of action, which may ultimately lead to innovations in treatment strategies for diseases linked to its functional pathways.
