Analytical Data
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Gene name
SIRT5
- Application
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Alternative Names
SIRT5;SIR2L5;NAD-dependent Protein deacylase sirtuin-5. 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
Q9NXA8
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Expression Region
34-310aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSARPSSSM ADFRKFFAKA KHIVIISGAG VSAESGVPTF RGAGGYWRKW QAQDLATPLA FAHNPSRVWE FYHYRREVMG SKEPNAGHRA IAECETRLGK QGRRVVVITQ NIDELHRKAG TKNLLEIHGS LFKTRCTSCG VVAENYKSPI CPALSGKGAP EPGTQDASIP VEKLPRCEEA GCGGLLRPHV VWFGENLDPA ILEEVDRELA HCDLCLVVGT SSVVYPAAMF APQVAARGVP VAEFNTETTP ATNRFRFHFQ GPCGTTLPEA LACHENETVS
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Molecular Weight
33 kDa i
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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
SIRT5, a member of the sirtuin family of proteins, has garnered significant interest in recent years due to its unique enzymatic functions and implications in cellular metabolism, aging, and disease. Unlike other sirtuins that primarily act as lysine deacetylases, SIRT5 exhibits distinct deacylation activities, including the removal of succinyl, malonyl, and glutaryl modifications from lysine residues on various target proteins. This ability to regulate multiple acylations suggests that SIRT5 plays a crucial role in mitochondrial function and metabolic pathways. Research has indicated that SIRT5 can influence key processes such as oxidative stress responses, insulin signaling, and overall energy metabolism, thereby impacting age-related conditions and metabolic disorders. The recombinant expression of SIRT5 protein allows scientists to investigate its functional roles in vitro and in vivo, enabling the exploration of its potential as a therapeutic target for diseases linked to metabolic dysfunction and aging. Understanding the precise mechanisms through which SIRT5 modulates metabolic processes could pave the way for novel interventions aimed at enhancing cellular health and longevity. As interests in personalized medicine and targeted therapies expand, elucidating the biochemical properties and regulatory mechanisms of recombinant SIRT5 is pivotal for developing innovative strategies to combat age-associated diseases and improve metabolic resilience.
