Analytical Data
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Gene name
HECTD1
- Application
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Alternative Names
E3 ligase for inhibin receptor; E3 ubiquitin protein ligase HECTD1; E3 ubiquitin-protein ligase HECTD1; EULIR; HECD1_HUMAN; HECT domain containing protein 1; HECT domain-containing protein 1; HECTD1; KIAA1131
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9ULT8
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Expression Region
3-110aa
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AA Sequence
DVDPDTLLEWLQMGQGDERDMQLIALEQLCMLLLMSDNVDRCFETCPPRTFLPALCKIFLDESAPDNVLEVTARAITYYLDVSAECTRRIVGVDGAIKALCNRLVVVE
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Molecular Weight
37.62 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
HECTD1, a member of the HECT (Homologous to the E6-AP Carboxyl Terminus) E3 ubiquitin ligase family, plays a critical role in regulating various cellular processes, including protein degradation, cell cycle progression, and signal transduction. Dysregulation of HECTD1 has been implicated in several diseases, particularly cancer, where abnormal ubiquitination leads to the stabilization of oncogenes or the degradation of tumor suppressors. Recent studies have revealed that HECTD1 may also be involved in developmental processes and neurodegenerative diseases, highlighting its importance in maintaining cellular homeostasis. Given its multifaceted functions, the characterization and understanding of HECTD1's mechanisms of action are vital. Researchers are increasingly focusing on the functional analysis of recombinant HECTD1 proteins to elucidate the specific pathways it influences. Recombinant protein studies allow for the exploration of HECTD1's enzymatic activity, substrate specificity, and interactions with other proteins, providing insights into its role within the ubiquitin-proteasome system. Additionally, the potential therapeutic implications of modulating HECTD1 activity render its investigation particularly relevant in biomedical research. Overall, studying recombinant HECTD1 proteins contributes to a deeper understanding of ubiquitin ligase functions and highlights novel avenues for therapeutic intervention in related pathologies.
