Analytical Data
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Gene name
NAA30
- Application
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Alternative Names
NAA30;C14orf35;MAK3;NAT12;N-alpha-acetyltransferase 30
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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
Q147X3
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Expression Region
1-362aa
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AA Sequence
MAEVPPGPSS LLPPPAPPAP AAVEPRCPFP AGAALACCSE DEEDDEEHEG GGSRSPAGGE SATVAAKGHP CLRCPQPPQE QQQLNGLISP ELRHLRAAAS LKSKVLSVAE VAATTATPDG GPRATATKGA GVHSGERPPH SLSSNARTAV PSPVEAAAAS DPAAARNGLA EGTEQEEEEE DEQVRLLSSS LTADCSLRSP SGREVEPGED RTIRYVRYES ELQMPDIMRL ITKDLSEPYS IYTYRYFIHN WPQLCFLAMV GEECVGAIVC KLDMHKKMFR RGYIAMLAVD SKYRRNGIGT NLVKKAIYAM VEGDCDEVVL ETEITNKSAL KLYENLGFVR DKRLFRYYLN GVDALRLKLW LR
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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
NAA30, or N-alpha-acetyltransferase 30, is a member of the N-terminal acetyltransferase (NAT) family, which plays a crucial role in protein post-translational modifications. This modification, the acetylation of the N-terminal amino acid, is essential for various cellular processes, including protein stability, localization, and interaction with other biomolecules. Research has shown that NAA30 is involved in regulating gene expression and influencing the cellular response to stress. Dysregulation of NAA30 has been associated with several diseases, including cancer, where altered acetylation patterns can lead to aberrant signaling pathways. Consequently, understanding the molecular mechanisms and functions of NAA30 has garnered significant interest within the scientific community. Recent studies have focused on elucidating its specific roles in cellular metabolism and development, as well as its potential as a therapeutic target. With advancements in biochemical techniques and structural biology, researchers are now able to investigate the substrate specificity and catalytic mechanisms of NAA30, paving the way for potential applications in drug development and disease management. As a result, NAA30 is emerging as a pivotal protein in the field of cellular biology, pushing the boundaries of our understanding of post-translational modifications and their implications in health and disease.
