IRBP (651-670) (human) peptide

IRBP (651-670) (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-LAQGAYRTAVDLESLASQLT-OH

H-Leu-Ala-Gln-Gly-Ala-Tyr-Arg-Thr-Ala-Val-Asp-Leu-Glu-Ser-Leu-Ala-Ser-Gln-Leu-Thr-OH

20

95.42%

C₉₁H₁₅₁N₂₅O₃₂

2107.31

Synthetic

Powder

IRBP (651-670) (human), sometimes referred to as hIRBP651-670 or human IRBP651-670, is amino acid residues 651 to 670 of human interphotoreceptor retinoid binding protein (IRBP), which has been identified as a new uveitogenic epitope. IRBP (651-670) (human) is uveitogenic for mice of the H-2b haplotype and elicits experimental autoimmune uveitis (EAU) with a higher severity and incidence in C57BL/6 mice than the previously characterized IRBP (1-20) (human) epitope. Co-immunization with IRBP (1-20) (human) and IRBP (651-670) human is additive but not synergistic. IRBP (651-670) (human) appears to be an epitope naturally processed from a conserved region of native IRBP.

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

• Mattapallil MJ, Silver PB, Cortes LM, St Leger AJ, Jittayasothorn Y, Kielczewski JL, et al. Characterization of a New Epitope of IRBP That Induces Moderate to Severe Uveoretinitis in Mice With H-2b Haplotype. Invest Ophthalmol Vis Sci. 2015;56(9):5439-49

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.