Cortistatin-29 (human) peptide

Cortistatin-29 (human) peptide

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

Batch to batch variation of the purity

Pyr-EGAPPQQSARRDRMPCRNFFWKTFSSCK (Disulfide bridge: Cys17-Cys28)

pGlu-Glu-Gly-Ala-Pro-Pro-Gln-Gln-Ser-Ala-Arg-Arg-Asp-Arg-Met-Pro-Cys-Arg-Asn-Phe-Phe-Trp-Lys-Thr-Phe-Ser-Ser-Cys-Lys (Disulfide bridge: Cys17-Cys28)

28

97.9%

C₁₄₉H₂₂₃N₄₇O₄₂S₃

3440.7

1815618-16-6

171920966

Synthetic

Powder

Cortistatin-29 (CST-29) is a peptide derived from the preprocortistatin protein. CST-29 is produced by cleavage at the C-terminal dibasic cleavage sites of the preprocortistatin gene. CST-29 is structurally similar to somatostatin-28 (SST-28), but there are significant differences in the N-terminal 15/14 residues between cortistatin and somatostatin. Within the Cys-Cys loop, there are also some differences between CST-29 and SST-28. Cortistatin has been shown to have sleep-promoting properties, reduce locomotor activity, and modulate cholinergic activity in the cortex. It may also have effects on memory and is neuroprotective against kainate-induced neurotoxicity. Cortistatin, including CST-29, has similar effects to somatostatin on hippocampal neurons, such as increasing the amplitude of the M-current and the hyperpolarization-activated cationic h-current.

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

• Spier AD, de Lecea L. Cortistatin: a member of the somatostatin neuropeptide family with distinct physiological functions. Brain Res Brain Res Rev. 2000 Sep;33(2-3):228-41. doi: 10.1016/s0165-0173(00)00031-x. PMID: 11011067.

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.