Analytical Data
-
Gene name
PPARa
- Application
-
Alternative Names
NR1C1; PPAR-A; HPPAR; Nuclear Receptor Subfamily 1 Group C Member 1
-
Species
Rat
-
Source
E. coli
-
Tag
N- His & GST
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
-
-
Expression Region
Ser280~Leu433
-
Molecular Weight
47kDa
-
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
Peroxisome proliferator-activated receptor alpha (PPARα) is a crucial nuclear receptor that plays a significant role in lipid metabolism, inflammation, and energy homeostasis. Since its discovery, PPARα has garnered attention for its involvement in various metabolic disorders, including obesity, type 2 diabetes, and cardiovascular diseases. The receptor functions by regulating the expression of genes associated with fatty acid oxidation and inflammation, making it a key target for therapeutic intervention. Research into recombinant PPARα proteins has advanced our understanding of its structural and functional dynamics, facilitating the development of specific agonists and antagonists. These studies often utilize methods such as protein crystallization and molecular modeling to elucidate the receptor's binding mechanisms and activation pathways. The recombinant proteins serve as valuable tools for investigating the effects of various ligands on PPARα activity and for screening potential pharmacological agents. Additionally, the exploration of PPARα polymorphisms and their implications in disease susceptibility underscores the receptor's importance in personalized medicine. As the field of metabolic research continues to evolve, the study of recombinant PPARα proteins remains essential in advancing therapeutic strategies aimed at combating metabolic diseases and enhancing overall health outcomes.











