RDH12 Human
Description
RDH12 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
RDH12 is a membrane-associated enzyme predominantly expressed in the retina, specifically at the base of photoreceptor inner segments . It is composed of 316 amino acids and has a molecular mass of approximately 35 kDa . The enzyme contains two highly conserved motifs among SDRs: the cofactor-binding site and catalytic residues .
The primary function of RDH12 is to catalyze the reduction of all-trans-retinal and its isomers (9-cis-, 11-cis-, and 13-cis-retinal) to their corresponding retinols in the presence of NADPH . This reaction is essential for the regeneration of 11-cis-retinal, a critical component of the visual cycle. RDH12 also metabolizes both all-trans- and cis-retinols, making it a dual-specificity enzyme .
Mutations in the RDH12 gene are associated with Leber congenital amaurosis (LCA) and early-onset severe retinal dystrophy (EOSRD) . These conditions are characterized by severe vision loss at an early age. RDH12 mutations account for approximately 3.4% to 10.5% of LCA cases . The enzyme’s role in the visual cycle makes it a potential target for gene therapy aimed at treating inherited retinal diseases .
Recombinant RDH12 has been expressed in insect cells as a membrane protein with enzymatic properties similar to those of the native enzyme . Studies have shown that RDH12 activity is inhibited by retinoic acids, recombinant cellular retinol-binding protein 1 (CRBP1), and cellular retinaldehyde-binding protein (CRALBP) . Understanding the enzyme’s function and regulation is crucial for developing therapeutic strategies for retinal diseases associated with RDH12 mutations.
In conclusion, Retinol Dehydrogenase 12 is a vital enzyme in the visual cycle and retinoid metabolism. Its role in retinal health and disease makes it an important target for research and potential therapeutic interventions.
