Analytical Data
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Gene name
U27
- Application
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Alternative Names
U27;UBCH10;Ubiquitin-conjugating enzyme E2 C
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P52439
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Expression Region
1-393aa
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AA Sequence
MCWSFHLFFKAHKARVGARTSFLTEMERGSRDHHRDHRDHREHRETREPPTLAFHMKSWKTINKSLKAFAKLLKENTTVTFTPQPSIIIQSAKNHLVQKLTIQAECLFLSDTDRFLTKTINNHIPLFESFMNIISNPEVTKMYIQHDSDLYTRVLVTASDTCTQASVPCVHGQEVVRDTGRSPLRIDLDHSTVSDVLKWLSPVTKTKRSGKSDALMAHIIVQVNPPTIKFVTEMNELEFSNSNKVIFYDVKNMRFNLSAKNLQQALSMCAVIKTSCSLRTVAAKDCKLILTSKSTLLTVEAFLTQEQLKEESRFERMGKQDDGKGDRSHKNDDGSALASKQEMQYKITNYMVPAKNGTAGSSLFNEKEDSESDDSMHFDYSSNPNPKRQRCVV
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Molecular Weight
46.8 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
The U27 recombinant protein has garnered significant interest in the field of molecular biology and biotechnology due to its potential applications in both research and therapeutic contexts. This protein is a member of the GTPase-activating protein family and plays a crucial role in regulating cellular signaling pathways, particularly those involved in cell growth, differentiation, and apoptosis. Understanding the structure and function of U27 is essential, as dysregulation of its activity has been implicated in various diseases, including cancer and neurodegenerative disorders. Recent studies have focused on elucidating the molecular mechanisms by which U27 influences cellular processes, as well as its interactions with other cellular proteins. The recombinant production of U27 not only facilitates detailed functional studies but also opens up avenues for the development of novel therapeutic strategies aimed at modulating its activity. By establishing stable expression systems and optimizing purification protocols, researchers aim to produce high-yield quantities of U27 suitable for biophysical characterization and potential drug development. The ongoing research into U27 and its implications for disease pathology underscores the importance of this protein in advancing our understanding of cellular signaling and therapeutic interventions. As such, U27 represents a promising target for further investigation in the context of molecular medicine and the development of innovative biotechnological applications.











