Analytical Data
-
Gene name
BCAT1
- Application
-
Alternative Names
Protein ECA39 (BCAT(c)) (Eca39)
-
Species
Mouse
-
Source
E. coli
-
Tag
N- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P24288
-
Expression Region
1-386aa
-
Molecular Weight
46.4 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
BCAT1 (branched-chain amino acid transaminase 1) is an enzyme that plays a critical role in the metabolism of branched-chain amino acids (BCAAs), which are essential for various physiological processes, including muscle protein synthesis and energy production. Abnormal BCAT1 expression has been associated with several diseases, including cancer, neurodegenerative disorders, and metabolic syndromes, highlighting its importance in maintaining cellular homeostasis. Recent studies have indicated that elevated BCAT1 levels may contribute to tumorigenesis by promoting cancer cell proliferation and survival, making it a potential target for therapeutic intervention. Furthermore, the recombinant expression of BCAT1 protein in various systems allows researchers to study its biochemical properties and regulatory mechanisms in detail. Purified BCAT1 can be utilized in enzyme assays and kinetic studies, enabling the exploration of its substrate specificity and inhibition by various compounds, which is crucial for drug development. Understanding the functional implications of BCAT1 can provide insights into its role in metabolic pathways and its potential as a biomarker or therapeutic target in diseases where it is dysregulated. Overall, the recombinant study of BCAT1 not only enhances our comprehension of its biological functions but also opens avenues for the development of novel strategies in disease management, particularly in cancer therapy and metabolic regulation.
