MOG (35-55) (human) peptide

MOG (35-55) (human) peptide

• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

H-MEVGWYRPPFSRVVHLYRNGK-OH

H-Met-Glu-Val-Gly-Trp-Tyr-Arg-Pro-Pro-Phe-Ser-Arg-Val-Val-His-Leu-Tyr-Arg-Asn-Gly-Lys-OH

21

95.1%

C₁₂₀H₁₇₉N₃₅O₂₈S

2591.98

Synthetic

Powder

MOG (35-55) (human) is a truncated fragment of human myelin oligodendrocyte glycoprotein (MOG), the transmembrane glycoprotein expressed at the surface of oligodendrocyte cells and on the outermost surface of the myelin sheath, which can be used for the induction of experimental autoimmune encephalomyelitis in mouse and rat models. In contrast to MOG (35-55) (rat), Mog (35-55) (human) is only weakly encephalitogenic but both induce antibodies that are equivalent in titer and IgG subclass, demonstrating that EAE can be induced in C57BL/6 mice by two different mechanisms

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

• Oliver et al (2003) Rat and Human Myelin Oligodendrocyte Glycoproteins Induce Experimental Autoimmune Encephalomyelitis by Different Mechanisms in C57BL/6 Mice. J. Immunol. 171 (1) 462 PMID: 12817031
• Haas et al (2005) Reduced suppressive effect of CD4+CD25high regulatory T cells on the T cell immune response against myelin oligodendrocyte glycoprotein in patients with multiple sclerosis. Eur. J. Immunol. 35(11) 3343 PMID: 16206232

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.