mouse gp100 (25 - 33) peptide

mouse gp100 (25 - 33) peptide

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

Batch to batch variation of the purity

H-EGSRNQDWL-OH

H-Glu-Gly-Ser-Arg-Asn-Gln-Asp-Trp-Leu-OH

9

97.82%

C₄₆H₆₉N₁₅O₁₇

1104.12

Synthetic

Powder

This peptide sequence is found in residues 25 to 33 of the mouse self/tumor antigen glycoprotein (mgp100). This fragment is a H-2Db–restricted epitope recognized by CD8+ T cells. Mgp100 is an enzyme normally involved in pigment synthesis, and the epitope fragment is typically expressed in both normal melanocytes and melanoma cells. Pyroglutamyl (pGlu) peptides may spontaneously form when either Glutamine (Q) or Glutamic acid (E) is located at the sequence N-terminus. The conversion of Q or E to pGlu is a natural occurrence and in general it is believed that the hydrophobic γ-lactam ring of pGlu may play a role in peptide stability against gastrointestinal proteases. Pyroglutamyl peptides are therefore considered a normal subset of such peptides and are included as part of the peptide purity during HPLC analysis.

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

• Finkelstein, S. et al. J Leukoc Biol 76, 333 (2004); Hosoi, A. et al. Cancer Res 68, 3941 (2008); Overwijk, WW. et al. J Exp Med 188, 277 (1998).

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.