Natriuretic peptide PaNP-d

Natriuretic peptide PaNP-d

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

Batch to batch variation of the purity

SGSKTAEIDDGCFGLPLDPIGSTSGMGCRSVPKPIPGGS

Ser-Gly-Ser-Lys-Thr-Ala-Glu-Ile-Asp-Asp-Gly-Cys-Phe-Gly-Leu-Pro-Leu-Asp-Pro-Ile-Gly-Ser-Thr-Ser-Gly-Met-Gly-Cys-Arg-Ser-Val-Pro-Lys-Pro-Ile-Pro-Gly-Gly-Ser

39

95.14%

C₁₆₀H₂₆₀N₄₄O₅₆S₃

3792.21

Synthetic

Powder

Natriuretic peptide PtNP-d is a natriuretic peptide that has been isolated from the venom of the Australian elapid snake, Pseudechis australis. It is one of the isoforms of natriuretic peptides found in these snakes.
The natriuretic peptides from Australian snakes, including PaNP-d, have conserved amino acid residues that are important for binding and stimulation of the natriuretic peptide receptor.
It is worth noting that the activity of PaNP-d may be influenced by variations in its amino acid composition.

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

• St pierre L, Flight S, Masci PP, et al. Cloning and characterisation of natriuretic peptides from the venom glands of Australian elapids. Biochimie. 2006;88(12):1923-31.

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.