LRAT Protein, Human (Cell-Free)

LRAT, a crucial enzyme in vitamin A metabolism, transfers the acyl group from phosphatidylcholine to all-trans retinol, forming storage retinyl esters essential for vision. Integral to the visual cycle, LRAT contributes to the generation of chromophores for rhodopsin and cone photopigments, ensuring the survival of cone photoreceptors and proper morphology of rod photoreceptor cells. LRAT Protein, Human (Cell-Free) is the recombinant human-derived LRAT protein, expressed by E. coli Cell-free , with tag free. The total length of LRAT Protein, Human (Cell-Free) is 230 a.a., with molecular weight of 25.8 kDa.

LRAT, a key enzyme in vitamin A metabolism, facilitates the transfer of the acyl group from the sn-1 position of phosphatidylcholine to all-trans retinol, yielding all-trans retinyl esters. These retinyl esters serve as storage forms of vitamin A, playing a crucial role in vision. LRAT is integral to the visual cycle, providing substrates for isomerohydrolase, which further processes the esters into 11-cis-retinol in the retinal pigment epithelium. This process is essential for the generation of the chromophore for rhodopsin and cone photopigments. LRAT's involvement is vital for the survival of cone photoreceptors and the proper morphology of rod photoreceptor cells.

Human

E. coli Cell-free

Tag Free

O95237 (M1-G230)

9227

MKNPMLEVVSLLLEKLLLISNFTLFSSGAAGEDKGRNSFYETSSFHRGDVLEVPRTHLTHYGIYLGDNRVAHMMPDILLALTDDMGRTQKVVSNKRLILGVIVKVASIRVDTVEDFAYGANILVNHLDESLQKKALLNEEVARRAEKLLGFTPYSLLWNNCEHFVTYCRYGTPISPQSDKFCETVKIIIRDQRSVLASAVLGLASIVCTGLVSYTTLPAIFIPFFLWMAG

25.8 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.