Analytical Data
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Gene name
USP29
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简介
USP29 protein, as a deubiquitinating enzyme, plays a crucial role in innate antiviral immunity by mediating "Lys-48" deubiquitination of CGAS. This effect stabilizes CGAS, an important sensor of the cellular response to viral infection, emphasizing the importance of USP29 in regulating CGAS activity. USP29 Protein, Human (sf9, FLAG) is the recombinant human-derived USP29 protein, expressed by sf9 insect cells , with N-Flag labeled tag.
- Application
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Alternative Names
USP29; Ubiquitin carboxyl-terminal hydrolase 29; Deubiquitinating enzyme 29; Ubiquitin thioesterase 29; Ubiquitin-specific-processing protease 29
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Species
Human
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Source
Baculovirus
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Tag
N-Flag
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9HBJ7
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Expression Region
I2-A922
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Protein Length
Partial
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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
USP29, a member of the ubiquitin-specific protease (USP) family, plays a crucial role in regulating the ubiquitin-proteasome system, which is vital for maintaining cellular homeostasis and regulating various biological processes. The dysregulation of this system is often linked to numerous diseases, including cancer, neurodegenerative disorders, and immune diseases. Recent studies have indicated that USP29 is involved in modulating key signaling pathways, such as those related to tumor suppression and inflammation. By deubiquitinating specific substrate proteins, USP29 can alter their stability and activity, thus influencing cellular responses to stress and promoting cell survival. Furthermore, emerging evidence suggests that USP29 has potential as a therapeutic target, as manipulating its activity may restore normal cellular functions in disease contexts. These insights into USP29's molecular mechanisms have propelled research into its structural properties and interactions with substrates, paving the way for potential drug development aimed at targeting aberrant USP29 activity in various pathologies. The study of USP29 recombinant proteins not only enhances our understanding of its biological functions but also provides valuable tools for pharmacological interventions that could lead to novel treatments for diseases associated with USP dysregulation.
