Analytical Data
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Gene name
USP21
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简介
USP21 protein is a multifunctional deubiquitinase that plays a key role in the regulation of epigenetic transcriptional repression by deubiquitinating histone H2A. As a coactivator, it relieves the inhibition of dimethylation and trimethylation of histone H3 at "Lys-4", thereby regulating transcription initiation. USP21 Protein, Human (GST) is the recombinant human-derived USP21 protein, expressed by E. coli , with N-GST labeled tag.
- Application
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Alternative Names
USP21; Ubiquitin carboxyl-terminal hydrolase 21; Deubiquitinating enzyme 21; Ubiquitin thioesterase 21; Ubiquitin-specific-processing protease 21
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Species
Human
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Source
E. coli
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Tag
N-GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UK80
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Expression Region
P2-L565
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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
USP21, or Ubiquitin Specific Peptidase 21, is a member of theUSP family of deubiquitinating enzymes (DUBs), which play crucial roles in regulating protein degradation, signaling pathways, and cellular homeostasis by reversing ubiquitination. Ubiquitination serves as a post-translational modification that labels proteins for degradation via the proteasome or alters their function and localization. Research on USP21 has garnered attention due to its involvement in various cellular processes, including cell cycle regulation, immune responses, and tumorigenesis. Studies have shown that USP21 can deubiquitinate key oncogenic proteins, thereby influencing cancer progression and therapy resistance. Furthermore, alterations in USP21 expression and activity have been linked to various diseases, making it a potential therapeutic target. Understanding the structure and function of USP21, particularly its specificity and interaction with ubiquitinated substrates, is critical for developing targeted interventions in cancer and other diseases. Current research focuses on elucidating the molecular mechanisms underlying USP21's actions, exploring its regulatory networks, and investigating small-molecule inhibitors that can modulate its activity. Overall, the study of USP21 and its recombinant proteins offers significant insights into the intricate balance of ubiquitination and deubiquitination, contributing to our understanding of cell biology and disease mechanisms.
