Analytical Data
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Gene name
TRIM24
- Application
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Alternative Names
E3 ubiquitin-protein ligase TRIM24RING finger protein 82Tripartite motif-containing protein 24
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Species
Human
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Source
Yeast
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O15164
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Expression Region
891-1012aa
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Molecular Weight
16.5 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
TRIM24, also known as tripartite motif-containing protein 24, is a member of the TRIM family of proteins, which are characterized by their E3 ubiquitin ligase activity and play crucial roles in various cellular processes, including transcription regulation, cell proliferation, and immune responses. Emerging evidence suggests that TRIM24 is involved in oncogenesis, particularly in certain types of cancer where it may function as an oncoprotein or tumor suppressor depending on the context. Its ability to modulate gene expression via epigenetic mechanisms, such as methylation and ubiquitination of transcription factors, highlights its significance in regulating critical pathways associated with cell growth and differentiation. Moreover, recent studies have identified TRIM24 as a potential therapeutic target, as its dysregulation has been implicated in various malignancies, making it a focus of cancer research. Understanding the mechanistic roles of TRIM24 in cellular processes and its interactions within signaling networks is critical for developing targeted therapies that could improve clinical outcomes for patients with TRIM24-related malignancies. Investigating the structure and functions of TRIM24 reintroduces protein in the context of these pathways, revealing new insights that could lead to innovative strategies for cancer treatment and potentially other diseases involving TRIM24 dysregulation.
