Analytical Data
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Gene name
deacetylase
- Application
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Alternative Names
Chitin deacetylase; EC 3.5.1.41
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Species
Amylomyces rouxii
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P50325
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Expression Region
22-421aa
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Molecular Weight
49.9 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
Deacetylases are a class of enzymes that play a critical role in various biological processes by removing acetyl groups from lysine residues on proteins, thereby influencing their function, stability, and interactions. The study of deacetylases, particularly in the context of recombinant protein research, has gained significant attention due to their essential roles in cellular regulation, gene expression, and metabolism. Deacetylases, such as histone deacetylases (HDACs), are involved in epigenetic regulation, impacting gene transcription and influencing processes like cell differentiation and apoptosis. The disruption of deacetylase activity has been linked to various diseases, including cancer, neurodegenerative disorders, and metabolic syndromes, highlighting their potential as therapeutic targets. The recombinant expression of deacetylases allows for detailed biochemical characterization and functional analysis, enabling researchers to understand their mechanisms and explore their applications in disease treatment. Advances in molecular biology techniques, such as CRISPR and protein engineering, further facilitate the study of deacetylases, providing insights into their structure-function relationship and opening new avenues for drug development. Understanding the intricate roles of deacetylases through recombinant protein studies not only enhances our comprehension of fundamental biological processes but also paves the way for innovative therapeutic strategies aimed at manipulating their activity for disease intervention.
