Analytical Data
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Gene name
USP37
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简介
The USP37 protein is a multifunctional deubiquitinase that regulates critical cellular processes. During the G1/S transition, it deubiquitinates cyclin A, promotes S phase entry, and enhances activity through Ser-628 phosphorylation. USP37 Protein, Human (sf9, His) is the recombinant human-derived USP37 protein, expressed by sf9 insect cells , with N-8*His labeled tag.
- Application
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Alternative Names
USP37; Ubiquitin carboxyl-terminal hydrolase 37; Deubiquitinating enzyme 37; Ubiquitin thioesterase 37; Ubiquitin-specific-processing protease 37
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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
Q86T82
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Expression Region
S2-L979
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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
USP37 (Ubiquitin Specific Peptidase 37) is a member of the ubiquitin-specific protease family, known for its role in deubiquitination, a critical process that affects various cellular functions, including protein stability, signal transduction, and the regulation of cell cycle progression. The study of USP37 has gained attention due to its involvement in several key biological processes and its potential implications in cancer biology. Research indicates that USP37 can deubiquitinate and stabilize various oncoproteins, thereby contributing to tumorigenesis. Moreover, aberrant expression of USP37 has been linked to poor prognosis in several cancers, emphasizing its potential as a therapeutic target. Understanding the structural and functional characteristics of USP37, along with its regulatory mechanisms, can provide insights into the molecular pathways underlying cancer progression. Current studies are focused on elucidating the enzymatic activities of USP37, identifying its substrates, and exploring its interactions with other proteins. These investigations aim to unravel the complexities of USP37's role in cellular homeostasis and its disruption in disease states, ultimately contributing to the development of novel strategies for cancer treatment. In addition, the development of USP37 inhibitors is of interest, as they may enhance the efficacy of existing therapies by targeting the ubiquitin-proteasome system. Overall, research on USP37 is crucial for understanding its multifaceted influence in cellular regulation and its potential as a biomarker and therapeutic target in oncology.
