Analytical Data
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Gene name
ugl
- Application
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Alternative Names
Glycosaminoglycan hydrolase Glycuronidase Unsaturated uronic acid hydrolase
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Species
Bacillus sp.
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9RC92
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Expression Region
1-377aa
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Molecular Weight
58.9 kDa
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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
Ugl (Ubiquitin-like protein) is increasingly recognized for its significant roles in cellular processes such as protein degradation, signaling, and cellular stress responses. Research into Ugl and its recombinant proteins focuses on understanding its structure-function relationships and exploring its potential therapeutic applications. The ability to produce Ugl recombinantly allows for detailed studies of its various isoforms, interactions with other proteins, and the implications of its post-translational modifications. This has implications in fields ranging from cancer biology, where dysregulation of ubiquitination pathways can lead to tumorigenesis, to neurodegenerative diseases, where proper protein homeostasis is crucial. Moreover, Ugl's role in modulating immune responses and its potential as a drug target for various diseases further underline the importance of this research. As scientists develop novel recombinant technologies, the characterization and functionality of Ugl proteins will provide insights needed for innovative therapeutic strategies and biomarker development, ultimately enhancing our understanding of fundamental biological mechanisms and their applications in medicine.
