Analytical Data
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Gene name
HERC1
- Application
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Alternative Names
HECT domain and RCC1-like domain-containing protein 1 (HECT-type E3 ubiquitin transferase HERC1) (p532) (p619)
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Species
Human
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q15751
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Expression Region
3975-4360aa
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Molecular Weight
48.1 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
Related Products
Protein Description
HERC1 (HECT and RLD domain containing E3 ubiquitin-protein ligase 1) is a member of the HECT-type E3 ubiquitin ligases, which play critical roles in cellular processes such as protein degradation, signal transduction, and cellular stress responses through the ubiquitin-proteasome pathway. Research has indicated that HERC1 is involved in various biological functions, including the regulation of immune responses and the modulation of neurological functions. Its dysregulation has been associated with several diseases, including neurodegenerative disorders and cancer, making it a significant target in therapeutic research. Investigating recombinant HERC1 proteins provides insights into its functional mechanisms and interactions with substrates, enhancing our understanding of its role in cellular homeostasis and disease pathology. Furthermore, the production of HERC1 as a recombinant protein allows for structural studies and the development of potential inhibitors that could serve as novel therapeutic agents. Given its importance, ongoing research focuses on characterizing the enzymatic activity of HERC1, identifying its substrates, and exploring its regulation under various physiological and pathological conditions. This research not only contributes to our understanding of HERC1's biological roles but also holds promise for the development of innovative strategies to manipulate its activity for therapeutic purposes.
