Analytical Data
-
Gene name
NAA10
- Application
-
Alternative Names
NAA10;ARD1;ARD1A;TE2;N-alpha-acetyltransferase 10
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P41227
-
Expression Region
1-235aa
-
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
-
Molecular Weight
29 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
NAA10, also known as NatA, is a crucial protein in the N-terminal acetylation process, which is an essential post-translational modification for numerous proteins in eukaryotic cells. This acetylation helps regulate protein stability, localization, and function, impacting various cellular processes such as cell cycle progression, signal transduction, and gene expression. Mutations or dysregulation of NAA10 have been associated with several diseases, including cancer and developmental disorders, highlighting its significance in maintaining cellular homeostasis. Research into recombinant NAA10 has gained momentum as scientists seek to understand its enzymatic mechanisms and broader biological implications. Generating recombinant NAA10 allows for detailed structural and functional studies that can uncover its role in pathophysiology and therapeutic potential. By employing techniques such as X-ray crystallography and enzymatic assays, researchers aim to elucidate the specific interactions and regulatory pathways involved in NAA10-mediated acetylation. Moreover, characterizing NAA10’s interactions with other cellular factors could pave the way for targeted drug design and innovative treatment strategies for NAA10-related diseases. Overall, the study of recombinant NAA10 is vital for advancing our understanding of post-translational modifications and their impact on cellular function and disease.
