C-type natriuretic peptide CNP-38

C-type natriuretic peptide CNP-38

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

Batch to batch variation of the purity

KDLSNNPLRFRGRSKKGPSRGCFGVKLDRIGAMSGLGC

H-Lys-Asp-Leu-Ser-Asn-Asn-Pro-Leu-Arg-Phe-Arg-Gly-Arg-Ser-Lys-Lys-Gly-Pro-Ser-Arg-Gly-Cys-Phe-Gly-Val-Lys-Leu-Asp-Arg-Ile-Gly-Ala-Met-Ser-Gly-Leu-Gly-Cys-OH (disulfide bond: Cys²²-Cys³⁸)

38

95.28%

C₁₇₃H₂₉₁N₅₉O₄₉S₃

4077.6

Synthetic

Powder

C-type natriuretic peptide (CNP) is a third member of the natriuretic peptide family to be identified subsequent to the identification of atrial natriuretic peptide (ANP) and brain natriuretic peptide (BNP). CNP has a considerable sequence homology to the ANP and BNP within the 17-residue ring structure formed by a disulphide bond, although it terminates at the second cysteine residue and lacks a C-terminal extension from the ring structure. This C-type natriuretic peptide CNP-38 was originally found in leopard shark (Triakis scyllaum / Triakis scylla).

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

• Suzuki R, Takahashi A, Takei Y. Different molecular forms of C-type natriuretic peptide isolated from the brain and heart of an elasmobranch, Triakis scyllia. J Endocrinol. 1992 Nov;135(2):317-23. doi: 10.1677/joe.0.1350317. PMID: 1474339.

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.