Analytical Data
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Gene name
NAT5
- Application
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Alternative Names
NAT5；NAT5；N-alpha-acetyltransferase 20
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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
Q9GZZ1
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Expression Region
1-169aa
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AA Sequence
MKGSRIELGDVTPHNIKQLKRLNQVIFPVSYNDKFYKDVLEVGELAKLAYFNDIAVGAVCCRVDHSQNQKRLYIMTLGCLAPYRRLGIGTKMLNHVLNICEKDGTFDNIYLHVQISNESAIDFYRKFGFEIIETKKNYYKRIEPADAHVLQKNLKVPSGQNADVQKTDN
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Molecular Weight
46.4 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
NAT5, a member of the N-acetyltransferase family, has garnered attention in recent years due to its significant role in cellular processes, particularly in the modification of proteins through acetylation. This post-translational modification is crucial for regulating protein function, stability, and interactions. Studies have indicated that NAT5 is involved in various biological pathways, including those related to cell proliferation, differentiation, and apoptosis. The dysregulation of NAT5 has been implicated in several diseases, including cancer and metabolic disorders, highlighting its potential as a therapeutic target. Consequently, understanding the structure and function of NAT5 is vital for elucidating its mechanisms in health and disease. Researchers are exploring the recombinant expression of NAT5 to produce active protein for in-depth functional studies, structural characterization, and the development of inhibitors or enhancers. This research not only aims to advance the fundamental knowledge of NAT5 but also seeks to identify potential biomarkers for disease and novel strategies for therapeutic intervention. As a result, the study of NAT5 and its recombinant protein forms is an essential frontier in molecular and cellular biology, with promising implications for biomedical research and clinical applications.
