Analytical Data
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Gene name
SENP8
- Application
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Alternative Names
SENP8;DEN1;NEDP1;PRSC2;Sentrin-specific protease 8
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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
Q96LD8
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Expression Region
1-212aa
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AA Sequence
MDPVVLSYMDSLLRQSDVSLLDPPSWLNDHIIGFAFEYFANSQFHDCSDH VSFISPEVTQFIKCTSNPAEIAMFLEPLDLPNKRVVFLAINDNSNQAAGG THWSLLVYLQDKNSFFHYDSHSRSNSVHAKQVAEKLEAFLGRKGDKLAFV EEKAPAQQNSYDCGMYVICNTEALCQNFFRQQTESLLQLLTPAYITKKRG EWKDLITTLAKK
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Molecular Weight
23 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
Related Products
Protein Description
SENP8 is a member of the SUMO-specific protease (SENP) family, which plays a crucial role in the post-translational modification of target proteins by regulating SUMO (Small Ubiquitin-like Modifier) conjugation and deconjugation processes. Initially identified for its involvement in cellular stress responses and the regulation of various biological processes, SENP8 is particularly significant in the context of cancer biology, cell differentiation, and apoptosis. The enzyme has garnered attention due to its potential implications in tumorigenesis and its role in modulating the stability and function of key oncogenic proteins. Functional studies have demonstrated that SENP8 can regulate the SUMOylation of specific substrates, thereby influencing their activity and interactions. The recombinant production of SENP8 protein has become essential for in vitro studies aimed at elucidating its enzymatic mechanisms and substrate specificity. Furthermore, understanding the dynamics of SENP8 activity and its influence on signaling pathways could provide insights into novel therapeutic targets for cancer treatment and other diseases associated with dysregulated SUMOylation.
