Analytical Data
-
Gene name
TRIM9
- Application
-
Alternative Names
RING finger protein 91Tripartite motif-containing protein 9
-
Species
Human
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9C026
-
Expression Region
1-550aa
-
Molecular Weight
77.3 kDa
-
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
TRIM9, a member of the tripartite motif (TRIM) family of proteins, has garnered increasing interest due to its potential roles in various biological processes, including neuronal development, immune responses, and cellular signaling. This protein contains characteristic RING, B-box, and coiled-coil domains, which suggest its involvement in ubiquitination and tethering functions. Recent studies have indicated that TRIM9 plays a crucial role in synaptic plasticity and neuronal survival, implicating it in neurodegenerative diseases such as Alzheimer's and Parkinson's. Furthermore, TRIM9 has been shown to interact with specific viral proteins, highlighting its significance in antiviral responses. The study of TRIM9 recombinant protein aims to elucidate its structural and functional properties, enabling researchers to understand how it modulates signaling pathways and influences physiological and pathological processes. As a result, TRIM9 is a promising target for therapeutic intervention in various diseases, warranting detailed exploration through recombinant protein studies to clarify its mechanisms of action and potential as a biomarker or therapeutic target. Understanding TRIM9's role in cellular contexts can provide insights into its implications for neurobiology and virology, positioning it as a valuable subject for further research in molecular biology and medicine.
