Analytical Data
-
Gene name
LRAT
- Application
-
Alternative Names
Phosphatidylcholine--retinol O-acyltransferase
-
Species
Human
-
Source
E. coli
-
Tag
-Free
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O95237
-
Expression Region
1-230aa
-
Molecular Weight
25.8 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
LRAT ( lecithin retinol acyltransferase) is an enzyme primarily recognized for its critical role in the visual cycle and retinoid metabolism. It facilitates the conversion of all-trans-retinol to all-trans-retinyl ester, a crucial step in the storage of vitamin A in the retinal pigment epithelium. Research into LRAT has gained momentum due to its significance in various ocular diseases, including retinitis pigmentosa and age-related macular degeneration, where vitamin A homeostasis is disrupted. Understanding LRAT's function and regulation offers insights into its potential as a therapeutic target. Moreover, the investigation of its recombinant protein form has enabled scientists to explore its biochemical properties, interaction partners, and structural characteristics in greater detail. The ability to produce LRAT as a recombinant protein accelerates the study of its enzymatic activity and its role in the retinoid cycle, while also facilitating the development of assays for drug screening and the discovery of novel compounds that may enhance LRAT function or modulate its activity. Overall, ongoing research on recombinant LRAT protein not only furthers our understanding of retinoid biology but also opens up new avenues for potential therapeutic interventions in retinal diseases linked to vitamin A dysregulation.
