Analytical Data
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Gene name
SENP7
- Application
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Alternative Names
SENP7；KIAA1707；SSP2；SUSP2；Sentrin-specific protease 7
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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
Q9BQF6
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Expression Region
695-864aa
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AA Sequence
MKLKSVSQPSNTDAAKPTYTFLQKQSSGCYSLSITSNPDEEWREVRHTGLVQKLIVYPPPPTKGGLGVTNEDLECLEEGEFLNDVIIDFYLKYLILEKASDELVERSHIFSSFFYKCLTRKENNLTEDNPNLSMAQRRHKRVRTWTRHINIFNKDYIFVPVNESSHWYLA
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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
SENP7 (Sentrin/SUMO-specific protease 7) is a member of the SENP family of proteases, which play crucial roles in the post-translational modification of proteins through SUMOylation— the attachment of Small Ubiquitin-like Modifier (SUMO) proteins. This modification regulates various cellular processes, including signal transduction, transcriptional control, and response to stress. The study of SENP7 has gained significant attention due to its implications in diverse biological functions and disease mechanisms, particularly in cancer progression and neurodegenerative disorders. Research has shown that SENP7 can remove SUMO chains, thereby regulating the stability and activity of target proteins. Dysregulation of SENP7 activity has been implicated in the pathogenesis of several diseases, leading to increased interest in its potential as a therapeutic target. Furthermore, explorations into the biochemical properties, substrate specificity, and interaction networks of SENP7 are ongoing, providing insights into its functional roles within the cell. Understanding SENP7's mechanisms and effects on cellular pathways is vital for developing novel strategies in disease treatment and therapy.
