Analytical Data
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Gene name
SIRT4
- Application
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Alternative Names
SIRT4；SIR2L4；NAD-dependent Protein lipoamidase sirtuin-4. mitochondrial
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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
Q9Y6E7
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Expression Region
1-314aa
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AA Sequence
MKMSFALTFRSAKGRWIANPSQPCSKASIGLFVPASPPLDPEKVKELQRF ITLSKRLLVMTGAGISTESGIPDYRSEKVGLYARTDRRPIQHGDFVRSAP IRQRYWARNFVGWPQFSSHQPNPAHWALSTWEKLGKLYWLVTQNVDALHT KAGSRRLTELHGCMDRVLCLDCGEQTPRGVLQERFQVLNPTWSAEAHGLA PDGDVFLSEEQVRSFQVPTCVQCGGHLKPDVVFFGDTVNPDKVDFVHKRV KEADSLLVVGSSLQVYSGYRFILTAWEKKLPIAILNIGPTRSDDLACLKL NSRCGELLPLIDPC
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Molecular Weight
62 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
SIRT4, a member of the sirtuin family of proteins, has garnered significant attention in recent years due to its critical roles in cellular metabolism, stress response, and potential implications in age-related diseases. Initially identified in mammalian cells, SIRT4 is localized in the mitochondria and is characterized by its NAD+-dependent deacetylase activity. Research has revealed that SIRT4 plays a pivotal role in regulating various metabolic pathways, including fatty acid oxidation and amino acid metabolism, thereby influencing energy homeostasis and overall mitochondrial function. Furthermore, SIRT4 has been implicated in the cellular response to oxidative stress and has been linked to various pathophysiological conditions such as diabetes, cancer, and neurodegeneration. The exploration of SIRT4's function through the study of its recombinant protein has become increasingly important, as it provides insights into its enzymatic activity and potential therapeutic targets. Understanding the regulatory mechanisms and interaction networks of SIRT4 through recombinant studies could illuminate its contributions to mitochondrial dynamics and cellular health, paving the way for novel strategies in addressing metabolic disorders and age-associated diseases. Overall, the continued investigation of SIRT4 as a recombinant protein represents a promising frontier in biomedical research, with the potential to uncover new avenues for intervention in metabolic and age-related conditions.
