Analytical Data
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Gene name
TRRAP
- Application
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Alternative Names
STAF40; TR-AP; Tra1; 350/400 kDa PCAF-associated factor
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Species
Human
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Source
E. coli
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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
Q9Y4A5
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Expression Region
Ala3534~Leu3770
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Molecular Weight
31kDa
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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
TRRAP (Transformation/transcription domain-associated protein) is a key component in multiple cellular processes, including transcription regulation, DNA damage response, and cellular transformation. As a scaffolding and co-activator protein, TRRAP plays a critical role in the assembly of multisubunit complexes involved in gene expression and chromatin remodeling. Historically, TRRAP was identified for its involvement in the transcriptional activation of genes essential for cell growth and division, particularly in cancer cells where its expression is often upregulated. Its ability to interact with several important proteins, including histone acetyltransferases and other transcription factors, positions TRRAP as a pivotal player in modulating chromatin structure, thereby influencing gene accessibility and expression. The functional diversity of TRRAP has ignited interest in characterizing its mechanistic roles within various biological contexts, particularly in oncogenesis and cellular responses to DNA damage. Recent studies have employed recombinant protein techniques to dissect TRRAP’s functional domains and interactions, providing insights into its role in transcription regulation and the development of cancer therapies. Understanding TRRAP's structure-function relationship and its involvement in critical cellular pathways is anticipated to reveal novel therapeutic targets for malignancies characterized by aberrant transcription regulation.
