RLBP1 Human
Description
Product Specs
Product Science Overview
The cellular retinol-binding protein (CRBP) was first discovered in 1973 from lung tissues by Bashor et al. There are three categories of cellular retinol-binding proteins: cellular retinol-binding protein, cellular retinoic acid-binding protein, and cellular retinaldehyde-binding protein (CRALBP) . CRALBP was first discovered in 1977 after it was purified from retina and retinal pigment epithelial cells .
The RLBP1 gene is located on human chromosome 15, specifically on 15q26.1 . The gene is composed of 8 exons and 7 introns . The protein itself contains 360 amino acid residues .
RLBP1 is primarily involved in the visual cycle, where it acts as an 11-cis-retinal acceptor. This protein facilitates the enzymatic isomerization of all 11-trans-retinal to 11-cis-retinal, which is crucial for the function of rod and cone cells in the retina . The protein carries 11-cis-retinaldehyde or 11-cis-retinal as its physiological ligands .
While RLBP1 is predominantly found in the retina and retinal pigment epithelial cells, it is also expressed in other cell types. It is majorly found in the iris, cornea, ciliary epithelium, Muller cells, the pineal gland, and oligodendrocytes of the optic nerve and brain . The function of RLBP1 in cells not related to the eyes is not yet fully understood .
Mutations in the RLBP1 gene have been associated with several retinal dystrophies, including Bothnia retinal dystrophy, fundus albipunctatus, and Newfoundland rod-cone dystrophy . These conditions are characterized by progressive vision loss and other visual impairments. Studies have shown that recombinant CRALBP containing certain mutations, such as the R150Q substitution, lacks the ability to bind 11-cis-retinaldehyde, leading to disruptions in retinal vitamin A metabolism .
Human recombinant RLBP1 is produced using recombinant DNA technology, which involves inserting the human RLBP1 gene into a suitable expression system, such as bacteria or yeast. This allows for the production of large quantities of the protein for research and therapeutic purposes. Recombinant RLBP1 is used in various studies to understand its function, structure, and role in retinal diseases.
