Analytical Data
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Gene name
USP30
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简介
USP30 protein is anchored on the outer mitochondrial membrane and severely inhibits mitophagy by antagonizing Parkin (PRKN). Hydrolyzing ubiquitin on RHOT1/MIRO1 and target proteins such as TOMM20 and USP30 blocks Parkin-mediated mitophagy, thereby regulating the clearance of damaged mitochondria. USP30 Protein, Human (sf9, His) is the recombinant human-derived USP30 protein, expressed by sf9 insect cells , with N-8*His labeled tag.
- Application
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Alternative Names
USP30; Ubiquitin carboxyl-terminal hydrolase 30; Deubiquitinating enzyme 30; Ubiquitin thioesterase 30; Ubiquitin-specific-processing protease 30; Ub-specific protease 30
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Species
Human
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Source
Baculovirus
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Tag
N-8*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q70CQ3
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Expression Region
T57-E517
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Protein Length
Cytoplasmic Domain
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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
USP30, or Ubiquitin-Specific Protease 30, is a deubiquitinating enzyme that plays a critical role in the regulation of cellular processes by removing ubiquitin moieties from target proteins, thereby influencing their stability, function, and localization. Understanding the biological significance of USP30 has gained traction in recent years due to its involvement in various cellular pathways, including mitochondrial function and the stress response. Researchers have identified USP30 as a key player in the regulation of mitophagy, the process by which damaged mitochondria are selectively degraded, which is crucial for cellular health and energy homeostasis. Dysregulation of USP30 activity has been linked to several diseases, including neurodegenerative disorders, where impaired mitochondrial quality control may contribute to pathogenesis. Investigating the structure and function of USP30, particularly through the development of recombinant protein models, provides essential insights into its catalytic mechanisms and regulatory roles. Moreover, elucidating the interactions of USP30 with its substrates and other cellular components holds promise for therapeutic interventions. As such, the study of USP30 not only enhances our understanding of fundamental cellular processes but also offers potential targets for drug development in the context of diseases characterized by mitochondrial dysfunction and oxidative stress. The continued exploration of USP30's biological relevance and mechanistic pathways represents a promising avenue of research in the fields of cell biology and molecular medicine.
