Analytical Data
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Gene name
USP6NL
- Application
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Alternative Names
RNTRE; TRE2NL; Related to the N-terminus of tre
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q92738
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Expression Region
Met1~Gly292
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Molecular Weight
39kDa
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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
The research on USP6NL (Ubiquitin-Specific Peptidase 6 N-terminal-like) recombinant protein is rooted in its potential implications in cellular processes and disease mechanisms, particularly in cancer. USP6NL is a member of the deubiquitinating enzyme family, which plays a crucial role in regulating protein stability and degradation by removing ubiquitin moieties from target proteins. This function is vital for maintaining cellular homeostasis, influencing pathways related to cell cycle progression, apoptosis, and DNA repair. Abnormalities in deubiquitination processes have been linked to various diseases, including tumors. Recent studies have identified USP6NL as a significant player in oncogenic signaling pathways, suggesting its involvement in tumorigenesis. Therefore, understanding the structure and function of USP6NL through recombinant protein studies may reveal novel insights into its role in cancer development and present potential targets for therapeutic intervention. Furthermore, the generation of USP6NL recombinant protein allows for detailed biochemical characterization and the exploration of its interactions with other cellular proteins, providing essential data for developing strategies aimed at modulating its activity in disease contexts. The broader perspective on USP6NL’s function is essential for elucidating its contributions to biochemical pathways and understanding its significance in health and disease.
