irbp (120), human

IRBP (1-20), human is the 1-20 fragment of interphotoreceptor retinoid binding protein (IRBP).This peptide is a 1 to 20 amino acid fragment of the interphotoreceptor retinoid binding protein (IRBP). IRBP is a 140-kDa glycolipoprotein residing in the inter

Interphotoreceptor retinoid-binding protein (1-20) (IRBP1-20), a dodecapeptide fragment of retinoid-binding protein 3, plays a crucial role in pigment regeneration by facilitating the transport of retinol and retinal between photoreceptor cells and the retinal pigment epithelium. It has been utilized to provoke autoimmune uveoretinitis in C57BL/6 mice, possessing the H-2b haplotype. Furthermore, IRBP1-20 at a concentration of 3 µM enhances the secretion of IL-4, IL-5, and IL-6 from primary mouse spleen lymphocytes. Immunization and subsequent rechallenge with IRBP1-20 lead to increased ear swelling, inflammation of ocular blood vessels, infiltration by immune cells, damage to the photoreceptor layer, and retinal detachment in IFN-γ-deficient mice.

Interphotoreceptor retinoid-binding protein (651-670) (IRBP651-670), a peptide fragment of retinoid-binding protein 3 (also known as IRBP), plays a crucial role in the visual cycle by facilitating the transport of retinol and retinal between photoreceptor cells and the retinal pigment epithelium. This transport is essential for the regeneration of pigments necessary for vision. When administered at a dose of 300 µg/animal, IRBP651-670 induces autoimmune uveoretinitis in C57BL/6 mice, a model possessing the H-2b haplotype. This immunization leads to increased levels of ocular cytokines including IL-1β, IL-6, IL-17, TNF-α, and IFN-γ, promotes immune cell infiltration into the eye, and results in photoreceptor cell damage.

IRBP (1-20), human TFA, contains a prominent epitope recognized by the H-2b haplotype and is known to elicit experimental autoimmune uveoretinitis (EAU) in H-2b mouse models [1] [2].