Analytical Data
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Gene name
ARD1
- Application
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Alternative Names
Activator of RNA decay; ARD 1; ARD-1; ARD1; Homolog of E.coli RNase E; NIPP 1
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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
Q12972
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Expression Region
1-209aa
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AA Sequence
MGGEDDELKGLLGLPEEETELDNLTEFNTAHNKRISTLTIEEGNLDIQRPKRKRKNSRVTFSEDDEIINPEDVDPSVGRFRNMVQTAVVPVKKKRVEGPGSLGLEESGSRRMQNFAFSGGLYGGLPPTHSEAGSQPHGIHGTALIGGLPMPYPNLAPDVDLTPVVPSAVNMNPAPNPAVYNPEAVNEPKKKKYAKEAWPGKKPTPSLLILENGTHMASSDACHECKSMIAAAG
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Molecular Weight
52.1 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
ARD1 (N-terminal acetyltransferase 1) is an essential enzyme involved in the post-translational modification of proteins through N-terminal acetylation, a process that plays a crucial role in regulating protein stability, localization, and function. Dysregulation of ARD1 has been linked to various diseases, including cancer and neurodegenerative disorders, highlighting its importance in cellular physiology. Research into ARD1 encompasses its structural biology, enzymatic mechanisms, and interaction with various substrates, which can reveal insights into its functional roles within the cell. Additionally, understanding ARD1's regulation and activity could lead to the development of novel therapeutic strategies that target protein acetylation pathways. Recent studies have employed advanced techniques such as X-ray crystallography, mass spectrometry, and genetic manipulation to elucidate the nuances of ARD1's catalysis and its broader implications in health and disease. The exploration of ARD1 as a potential drug target is gaining traction, offering hope for innovative treatments that could modify disease outcomes by modulating acetylation processes. Ultimately, ongoing research on ARD1 contributes to the broader understanding of protein modification dynamics and their significance in biological systems.
