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Neuropeptides are small signaling molecules produced and released by neurons engaged in many physiological functions. Indeed, neuropeptides act on neural substrates such as G protein-coupled receptors (GPCRs), tyrosine-kinase receptors, insuline-like peptides and also ion channels. Actions of neuropeptides result in slow-onset, long-lasting modulation of synaptic transmission.


Neuropeptide NPSF (SQAFLFQPQRF-NH2) is part of the FMRFamide-related peptides family. Neuropeptide NPSF has shown an important role in pain regulation and plays a role of anti-opiate. Moreover, neuropeptide NPSF seems to be implicate in variety of physiological processes such as food intake, insulin release, blood pressure regulation and electrolyte balance. Neuropeptide NPSF (SQAFLFQPQRF-NH2) is useful in opioid research.


Technical specification

 Neuropeptide NPSF (SQAFLFQPQRF-NH2) MW : 1367,56 g/mol (C65H94N18O15)
 Neuropeptide NPSF (SQAFLFQPQRF-NH2) Purity : > 95%
 Neuropeptide NPSF (SQAFLFQPQRF-NH2) Counter-Ion : TFA Salts (see option TFA removal)
Peptide library synthesis Neuropeptide NPSF (SQAFLFQPQRF-NH2) Delivery format : Freeze dried in propylene 2mL microtubes
peptide solubility guidelines Peptide Solubility Guideline
buy synthesized peptides Other names : 192387-39-6
buy peptide price Bulk peptide quantities available


Product catalog Size Price € HT Price $ HT
SB115-1MG 1 mg 80 100
SB115-5MG 5 mg 280 350



1- Hinuma S. et al. Nat Cell Biol. 2(10):703-708 (2000)
New neuropeptides containing carboxy-terminal RFamide and their receptor in mammals

Only a few RFamide peptides have been identified in mammals, although they have been abundantly found in invertebrates. Here we report the identification of a human gene that encodes at least three RFamide-related peptides, hRFRP-1-3. Cells transfected with a seven-transmembrane-domain receptor, OT7T022, specifically respond to synthetic hRFRP-1 and hRFRP-3 but not to hRFRP-2. RFRP and OT7T022 mRNAs are expressed in particular regions of the rat hypothalamus, and intracerebroventricular administration of hRFRP-1 increases prolactin secretion in rats. Our results indicate that a variety of RFamide-related peptides may exist and function in mammals.

2- Murakami M. et al. J Endrocrinol. 199(1):105-112 (2008)
Hypophysiotropic role of RFamide-related peptide-3 in the inhibition of LH secretion in female rats

Gonadotropin-inhibitory hormone (GnIH), a newly discovered hypothalamic RFamide peptide, inhibits reproductive activity by decreasing gonadotropin synthesis and release in birds. The gene of the mammalian RFamide-related peptides (RFRP) is orthologous to the GnIH gene. This Rfrp gene gives rise to the two biologically active peptides RFRP-1 (NPSF) and RFRP-3 (NPVF), and i.c.v. injections of RFRP-3 suppress LH secretion in several mammalian species. In this study, we show whether RFRP-3 affects LH secretion at the pituitary level and/or via the release of GnRH at the hypothalamus in mammals. To investigate the suppressive effects of RFRP-3 on the mean level of LH secretion and the frequency of pulsatile LH secretion in vivo, ovariectomized (OVX) mature rats were administered RFRP-3 using either i.c.v. or i.v. injections. Furthermore, the effect of RFRP-3 on LH secretion was also investigated using cultured female rat pituitary cells. With i.v. administrations, RFRP-3 significantly reduced plasma LH concentrations when compared with the physiological saline group. However, after i.c.v. RFRP-3 injections, neither the mean level of LH concentrations nor the frequency of the pulsatile LH secretion was affected. When using cultured pituitary cells, in the absence of GnRH, the suppressive effect of RFRP-3 on LH secretion was not clear, but when GnRH was present, RFRP-3 significantly suppressed LH secretion. These results suggest that RFRP-3 does not affect LH secretion via the release of GnRH, and that RFRP-3 directly acts upon the pituitary to suppress GnRH-stimulated LH secretion in female rats.

3- DeLaney K. et al. J Exp Biol. 221(Pt 3):jeb151167 (2018)
New techniques, applications and perspectives in neuropeptide research

Neuropeptides are one of the most diverse classes of signaling molecules and have attracted great interest over the years owing to their roles in regulation of a wide range of physiological processes. However, there are unique challenges associated with neuropeptide studies stemming from the highly variable molecular sizes of the peptides, low in vivo concentrations, high degree of structural diversity and large number of isoforms. As a result, much effort has been focused on developing new techniques for studying neuropeptides, as well as novel applications directed towards learning more about these endogenous peptides. The areas of importance for neuropeptide studies include structure, localization within tissues, interaction with their receptors, including ion channels, and physiological function. Here, we discuss these aspects and the associated techniques, focusing on technologies that have demonstrated potential in advancing the field in recent years. Most identification and structural information has been gained by mass spectrometry, either alone or with confirmations from other techniques, such as nuclear magnetic resonance spectroscopy and other spectroscopic tools. While mass spectrometry and bioinformatic tools have proven to be the most powerful for large-scale analyses, they still rely heavily on complementary methods for confirmation. Localization within tissues, for example, can be probed by mass spectrometry imaging, immunohistochemistry and radioimmunoassays. Functional information has been gained primarily from behavioral studies coupled with tissue-specific assays, electrophysiology, mass spectrometry and optogenetic tools. Concerning the receptors for neuropeptides, the discovery of ion channels that are directly gated by neuropeptides opens up the possibility of developing a new generation of tools for neuroscience, which could be used to monitor neuropeptide release or to specifically change the membrane potential of neurons. It is expected that future neuropeptide research will involve the integration of complementary bioanalytical technologies and functional assays.