irbp

Interphotoreceptor retinoid-binding protein(668-687) TFA is the 668-687 amino acid residue of human Interphotoreceptor retinoid binding protein(IRBP), which can induce uveitis.

Interphotoreceptor Retinoid Binding Protein Fragment (IRBP 161-180) is a 20-residue peptide that acts as a major pathogenic epitope, located in the first homologous repeat of interstitial visual pigment Binding Protein, and can induce post-uveitis (EAU).

Interphotoreceptor retinoid-binding protein (668-687) is an amino acid residue of human retinoid-binding protein (IRBP 668-687) that can induce uveitis.

IRBP acetate(211426-18-5 free base) (Interphotoreceptor Retinoid Binding Protein Fragment IRBP) is a 20-residue peptide, which is a major pathogenic epitope. It exists in the first homologous repeat of interstitial visual pigment Binding Protein peptide (IRBP 161-180) and can induce post-uveitis (EAU).

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].

IRBP-derived peptide R16, an active biological peptide, is a segment of the interphotoreceptor retinoid-binding protein (IRBP) known to induce experimental autoimmune uveitis (EAU) in susceptible animal strains.

R16, an interphotoreceptor retinoid binding protein (IRBP)-derived peptide, exhibits biological activity with the capability to induce experimental autoimmune uveitis (EAU) in susceptible animal strains as a photoreceptor cell protein.

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 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 TFA is the amino acid residue 668 to 687 of human interphotoreceptor retinoid-binding protein (IRBP). It also induces uveitis.

Interphotoreceptor retinoid-binding protein(668-687) TFA, a peptide fragment corresponding to amino acids 668-687 of the human interphotoreceptor retinoid-binding protein (IRBP), has been implicated in the induction of uveitis [1].