Analytical Data
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Gene name
SIRT2
- Application
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Alternative Names
SIRT2;SIR2L;SIR2L2;NAD-dependent Protein deacetylase sirtuin-2
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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
Q8IXJ6
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Expression Region
50-356aa
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AA Sequence
MASSLGSQKERLLDELTLEGVARYMQSERCRRVICLVGAGISTSAGIPDF RSPSTGLYDNLEKYHLPYPEAIFEISYFKKHPEPFFALAKELYPGQFKPT ICHYFMRLLKDKGLLLRCYTQNIDTLERIAGLEQEDLVEAHGTFYTSHCV SASCRHEYPLSWMKEKIFSEVTPKCEDCQSLVKPDIVFFGESLPARFFSC MQSDFLKVDLLLVMGTSLQVQPFASLISKAPLSTPRLLINKEKAGQSDPF LGMIMGLGGGMDFDSKKAYRDVAWLGECDQGCLALAELLGWKKELEDLVR REHASIDAQSLEHHHHHH
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Molecular Weight
36 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
SIRT2, a member of the sirtuin family of proteins, is a NAD+-dependent deacetylase that plays a crucial role in various cellular processes, including regulation of the cell cycle, metabolism, and stress response. Its involvement in deacetylating lysine residues on target proteins links it to significant biological pathways, particularly in neurodegenerative diseases and cancer. As SIRT2 is predominantly localized in the cytoplasm and is implicated in the regulation of the cell division cycle and the maintenance of genome stability, its dysregulation can lead to tumorigenesis. Over the years, researchers have shown interest in developing SIRT2 as a potential therapeutic target, making its recombinant protein an essential tool for studying its molecular mechanisms and interactions. By producing and purifying recombinant SIRT2, scientists aim to explore its enzymatic activity, substrate specificity, and the impact of acetylation on various proteins. Furthermore, understanding the structural characteristics of SIRT2 can provide insights into its functional dynamics and the development of small-molecule modulators for clinical applications. The study of SIRT2 recombinant proteins is therefore vital for advancing our comprehension of its roles in health and disease, paving the way for innovative therapeutic strategies.
