Neuropeptide Y NPYb

Neuropeptide Y NPYb

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

Batch to batch variation of the purity

H-YPVKPASPREGAPPEELARYYSALRHYINLITRQRY-OH

H-Tyr-Pro-Val-Lys-Pro-Ala-Ser-Pro-Arg-Glu-Gly-Ala-Pro-Pro-Glu-Glu-Leu-Ala-Arg-Tyr-Tyr-Ser-Ala-Leu-Arg-His-Tyr-Ile-Asn-Leu-Ile-Thr-Arg-Gln-Arg-Tyr-OH

36

95.01%

C₁₉₅H₃₀₀N₅₆O₅₃

4276.79

Synthetic

Powder

Neuropeptide Y NPYb has been found in teleost fish such as three-spined stickleback (Gasterosteus aculeatus), medaka fish / Japanese ricefish (Oryzias latipes) and is predominantly expressed in the brain.
The gene of Neuropeptide Y NPYb is a duplicate of the neuropeptide Y (NPY) gene, located in the same chromosomal region as the HoxAb cluster.
Neuropeptide Y NPYb is a member of the neuropeptide Y family of peptides, which includes NPY, peptide YY (PYY), and pancreatic polypeptide (PP) in vertebrates.

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

• Sundström G, Larsson TA, Brenner S, Venkatesh B, Larhammar D. Evolution of the neuropeptide Y family: new genes by chromosome duplications in early vertebrates and in teleost fishes. Gen Comp Endocrinol. 2008 Feb 1;155(3):705-16.
• Yan P, Jia J, Yang G, Wang D, Sun C, Li W. Duplication of neuropeptide Y and peptide YY in Nile tilapia Oreochromis niloticus and their roles in food intake regulation. Peptides. 2017 Feb;88:97-105.
• Tolås I, Kalananthan T, Gomes AS, Lai F, Norland S, Murashita K, Rønnestad I. Regional Expression of npy mRNA Paralogs in the Brain of Atlantic Salmon (Salmo salar, L.) and Response to Fasting. Front Physiol. 2021 Aug 26;12:720639.
• Giaquinto D, De Felice E, Attanasio C, Palladino A, Schiano V, Mollo E, Lucini C, de Girolamo P, D'Angelo L. Central and Peripheral NPY Age-Related Regulation: A Comparative Analysis in Fish Translational Models. Int J Mol Sci. 2022 Mar 30;23(7):3839.

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.