Analytical Data
-
Gene name
TRRAP
- Application
-
Alternative Names
TRRAP；PAF400；Transformation/transcription domain-associated Protein
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9Y4A5
-
Expression Region
全长
-
AA Sequence
full
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
TRRAP (Transformation/Transcription Domain-Associated Protein) is a crucial coactivator involved in various cellular processes, including transcription regulation, DNA damage response, and cancer development. Its multifunctional nature is underscored by its interactions with numerous proteins, including histone acetyltransferases and transcription factors, which facilitate chromatin remodeling and gene expression. Research into TRRAP has gained momentum due to its pivotal role in the cellular mechanisms that govern tumorigenesis and the potential therapeutic implications of targeting TRRAP-associated pathways. Notably, mutations and dysregulation of TRRAP have been implicated in several cancers, adding urgency to the investigation of its functional properties and the development of recombinant TRRAP proteins. Recombinant protein studies enable the exploration of TRRAP’s biochemical characteristics, interaction networks, and influence on transcriptional activity. Understanding how TRRAP participates in the modulation of genetic expression and its contribution to pathological conditions could provide insights for novel therapeutic strategies in oncology. Advances in recombinant DNA technology and protein purification methods are facilitating comprehensive studies of TRRAP, revealing its intricate role within the cell and presenting opportunities for intervention in diseases characterized by aberrant gene expression and regulation. As such, the development of TRRAP as a recombinant protein is not only significant for basic biological understanding but also holds promise for translational research aiming to combat cancer and other disorders linked to TRRAP dysregulation.
