IRBP (1-20), human peptide

IRBP (1-20), human peptide

• COA/MS/HPLC Report
• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

H-GPTHLFQPSLVLDMAKVLLD-OH

H-Gly-Pro-Thr-His-Leu-Phe-Gln-Pro-Ser-Leu-Val-Leu-Asp-Met-Ala-Lys-Val-Leu-Leu-Asp-OH

20

95.2%

C₁₀₁H₁₆₄N₂₄O₂₈S

2194.58

Synthetic

Powder

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 interphotoreceptor matrix between the neural retina and the retinal pigment epithelium. Human IRBP peptide 1-20 contains a major epitope for the H-2b haplotype. Immunization with IRBP (1 – 20) induces T-cell–mediated experimental autoimmune uveoretinitis (EAU) disease. The pathology of disease induced by the peptide, or by adoptive transfer of cells specific to the peptide, is similar to that induced by the whole IRBP protein.

Normally, this peptide will be delivered in lyophilized form and should be stored in a freezer at or below -20 °C. For more details, please refer to the manual:Handling and Storage of Synthetic Peptides

• Avichezer, D. et al. Invest. Ophthalmol. Visual Sci. 41, 127 (2000).

Trifluoroacetic acid (TFA) has a significant impact on peptides due to its role in the peptide synthesis process.

TFA is essential for the protonation of peptides that lack basic amino acids such as Arginine (Arg), Histidine (His), and Lysine (Lys), or ones that have blocked N-termini. As a result, peptides often contain TFA salts in the final product.

TFA residues, when present in custom peptides, can cause unpredictable fluctuations in experimental data. At a nanomolar (nM) level, TFA can influence cell experiments, hindering cell growth at low concentrations (as low as 10 nM) and promoting it at higher doses (0.5–7.0 mM). It can also serve as an allosteric regulator on the GlyR of glycine receptors, thereby increasing receptor activity at lower glycine concentrations.

In an in vivo setting, TFA can trifluoroacetylate amino groups in proteins and phospholipids, inducing potentially unwanted antibody responses. Moreover, TFA can impact structure studies as it affects spectrum absorption.