Analytical Data
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Gene name
THAP11
- Application
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Alternative Names
CTG B43a; CTG B45d; HRIHFB2206; RONIN; THA11_HUMAN; THAP 11; THAP domain containing 11; THAP domain-containing protein 11; Thap11
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Species
Human
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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
Q96EK4
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Expression Region
1-313aa
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Molecular Weight
50.3 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
THAP11 is a member of the THAP (THAP-type zinc finger) protein family, which plays a crucial role in various biological processes, including gene regulation, cell differentiation, and development. Research into THAP11 has gained attention due to its potential involvement in transcriptional regulation and its implications in various diseases, including cancer and neurodegenerative disorders. Understanding the structure and function of THAP11 is essential for elucidating its biological roles. Its unique THAP domain facilitates binding to DNA, suggesting a mechanism for its regulatory functions in gene expression. Additionally, THAP11 has been found to interact with other proteins, indicating its participation in complex cellular networks. Investigating the properties of THAP11, particularly through the development of recombinant proteins, offers significant insights into its mechanisms of action, functional roles in vivo, and potential therapeutic applications. By exploring the protein's interactions and regulatory effects in various cellular contexts, researchers aim to uncover its contributions to disease pathology and identify potential targets for therapeutic intervention. Overall, the study of THAP11 recombinant proteins serves as a foundation for advancing our understanding of gene regulation and the biological significance of this intriguing protein family member.
