Analytical Data
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Gene name
HERC1
- Application
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Alternative Names
HERC1；Probable E3 ubiquitin-Protein ligase HERC1
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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
Q15751
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Expression Region
3975-4360aa
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AA Sequence
GMDEQIMSWATSRPEDWHLGGKCDVYLWGAGRHGQLAEAGRNVMVPAAAPSFSQAQQVICGQNCTFVIQANGTVLACGEGSYGRLGQGNSDDLHVLTVISALQGFVVTQLVTSCGSDGHSMALTESGEVFSWGDGDYGKLGHGNSDRQRRPRQIEALQGEEVVQMSCGFKHSAVVTSDGKLFTFGNGDYGRLGLGNTSNKKLPERVTALEGYQIGQVACGLNHTLAVSADGSMVWAFGDGDYGKLGLGNSTAKSSPQKIDVLCGIGIKKVACGTQFSVALTKDGHVYTFGQDRLIGLPEGRARNHNRPQQIPVLAGVIIEDVAVGAEHTLALASNGDVYAWGSNSEGQLGLGHTNHVREPTLVTGLQGKNVRQISAGRCHSAAWTA
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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, a member of the HECT-type ubiquitin ligase family, plays a critical role in various cellular processes, including protein degradation, signal transduction, and cellular response to stress. Research on HERC1 has gained momentum due to its involvement in key regulatory pathways linked to cancer, neurodegenerative diseases, and immune responses. The protein is known to interact with multiple substrates, influencing their stability and function through ubiquitination. Additionally, mutations and dysregulation of HERC1 have been associated with various pathologies, highlighting its potential as a therapeutic target. Recent studies have focused on characterizing HERC1's structure and enzymatic activity, as well as elucidating its molecular mechanisms. Advances in recombinant protein technology have facilitated the production of HERC1, enabling detailed investigations into its function and interactions. Understanding HERC1 at the molecular level could pave the way for novel therapeutic strategies, making it an important focus within the field of protein research.
