Analytical Data
-
Gene name
CHLP
- Application
-
Alternative Names
Geranylgeranyl reductase
-
Species
Arabidopsis thaliana
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9CA67
-
Expression Region
44-467aa
-
Molecular Weight
63.1 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
The CHLP (Cholesterol-Lowering Protein) recombinant protein is a subject of growing interest in the field of cardiovascular health and metabolic research. This protein is associated with mechanisms that influence lipid metabolism and cholesterol homeostasis, which are crucial factors in the prevention of atherosclerosis and cardiovascular diseases. Elevated cholesterol levels are a well-known risk factor for these conditions, leading to extensive investigation into potential therapeutics that target cholesterol regulation. Studies have shown that CHLP may function through pathways that enhance cholesterol uptake and utilization, thereby reducing overall levels in the bloodstream. Additionally, research on CHLP’s structural characteristics and functional domains allows for the development of engineered variants that could possess enhanced properties for clinical applications. The use of recombinant DNA technology facilitates the production of CHLP in significant quantities, enabling further studies on its biological activity and therapeutic potential. As global health challenges rise due to increased incidences of heart disease, the exploration of CHLP not only aims to clarify its role in lipid metabolism but also to pave the way for novel interventions that could provide effective strategies for cholesterol management.











