Galanin (human) peptide

Galanin (human) peptide

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

Batch to batch variation of the purity

GWTLNSAGYLLGPHAVGNHRSFSDKNGLTS

H-Gly-Trp-Thr-Leu-Asn-Ser-Ala-Gly-Tyr-Leu-Leu-Gly-Pro-His-Ala-Val-Gly-Asn-His-Arg-Ser-Phe-Ser-Asp-Lys-Asn-Gly-Leu-Thr-Ser-OH

30

97.7%

C₁₃₉H₂₁₀N₄₂O₄₃

3157.45

119418-04-1

Synthetic

Powder

Human galanin, a 30-amino acid non-amidated peptide, has originally been isolated from colon and pituitary. Its sequence differs from that of rat and porcine galanins by 4 and 6 amino acids in the C-terminal moiety, respectively. Synthetic human galanin is equipotent to the rat peptide in the isolated rat fundus muscle strip bioassay. Both peptides also fully activate the rat galanin receptor, indicating the importance of the conserved N-terminal portion of galanin for receptor interaction.

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

• H.F.Evans and J.Shine, Endocrinology, 129, 1682 (1991)
• M.Bersani et al., FEBS Lett., 283, 189 (1991)
• W.E.Schmidt et al., Proc. Natl. Acad. Sci. USA, 88, 11435 (1991)

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.