Analytical Data
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Gene name
USP51
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简介
The USP51 protein uniquely regulates the DNA damage response by deubiquitinating the "Lys-14" (H2AK13Ub) and "Lys-16" (H2AK15Ub) residues of histone H2A at double-strand breaks. After DNA damage, USP51 is recruited to chromatin and regulates TP53BP1 and BRCA1 assembly/disassembly, which is critical for DNA repair. USP51 Protein, Human (sf9, His, FLAG) is the recombinant human-derived USP51 protein, expressed by sf9 insect cells , with N-Flag, N-8*His labeled tag.
- Application
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Alternative Names
USP51; Ubiquitin carboxyl-terminal hydrolase 51; Deubiquitinating enzyme 51; Ubiquitin thioesterase 51; Ubiquitin-specific-processing protease 51
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Species
Human
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Source
Baculovirus
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Tag
N-Flag;N-8*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q70EK9
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Expression Region
R363-Q706
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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
USP51 is a recently characterized member of the ubiquitin-specific protease family, which plays a critical role in regulating protein degradation and modification through the ubiquitin-proteasome system. Dysregulation of ubiquitination processes has been implicated in various diseases, including cancer and neurodegenerative disorders, making USP51 a potential therapeutic target. Research into USP51 focuses on its biochemical pathways, cellular functions, and interactions with substrates, which are essential for understanding its role in cell signaling and homeostasis. The protein’s unique structure and catalytic activity suggest it may possess specific substrates distinct from other USP family members, prompting investigations into its function in cellular stress response and development. Current studies employ various biochemical and molecular biology techniques to elucidate USP51's mechanism of action and its influence on cellular processes, thereby offering insights that could lead to novel therapeutic strategies for diseases associated with aberrant protein ubiquitination. Moreover, the exploration of USP51's involvement in immune responses adds another layer of complexity, highlighting its potential as a biomarker or target in immunotherapy and inflammation-related diseases. Overall, the ongoing research on USP51 aims to delineate its biological significance, paving the way for its potential exploitation in clinical settings.
