Analytical Data
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Gene name
LRAT
- Application
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Alternative Names
LRAT；Lecithin retinol acyltransferase
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O95237
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Expression Region
1-230aa
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AA Sequence
MKNPMLEVVSLLLEKLLLISNFTLFSSGAAGEDKGRNSFYETSSFHRGDVLEVPRTHLTHYGIYLGDNRVAHMMPDILLALTDDMGRTQKVVSNKRLILGVIVKVASIRVDTVEDFAYGANILVNHLDESLQKKALLNEEVARRAEKLLGFTPYSLLWNNCEHFVTYCRYGTPISPQSDKFCETVKIIIRDQRSVLASAVLGLASIVCTGLVSYTTLPAIFIPFFLWMAG
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Molecular Weight
25.8 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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 a critical enzyme involved in the metabolism of vitamin A, primarily functioning to facilitate the conversion of all-trans-retinol to its esterified form, retinyl esters, within the retinal pigment epithelium. This enzymatic process is vital for maintaining appropriate levels of retinol, a key component in vision and cellular signaling pathways. Dysregulation of LRAT has been associated with various retinal disorders, including retinitis pigmentosa and age-related macular degeneration, underscoring its significance in ocular health. The study of LRAT recombinant proteins has garnered attention in the field of biochemistry and ophthalmology, as researchers aim to elucidate the enzyme's structure-function relationship, kinetic properties, and regulatory mechanisms. Additionally, recombinant LRAT proteins hold potential for therapeutic applications, including gene therapy and the development of novel treatments for vitamin A-related deficiencies. By understanding the molecular dynamics of LRAT, researchers are hopeful that innovative strategies can be designed to mitigate the effects of retinal diseases and enhance visual function, contributing to the overall advancement of eye care and treatment methodologies.
