ANP (Human, 5-27) – Research Use Only

ANP (Human, 5-27) is a bioactive fragment of human Atrial Natriuretic Peptide (also known as atrial natriuretic factor, ANF) corresponding to residues 5–27 of the mature hormone. This 23-amino-acid peptide retains the critical disulfide-linked ring structure (Cys7–Cys23) essential for biological activity. Supplied as a high-purity 500 µg lyophilized powder (MW 2404.4 g/mol), it serves as a valuable research tool for studying natriuretic peptide receptor signaling, cardiovascular homeostasis, and renal physiology.

Scientific Overview

Atrial Natriuretic Peptide (ANP) is a cardiac hormone that plays a central role in the regulation of blood pressure, fluid and electrolyte balance, and cardiovascular homeostasis. The ANP (5-27) fragment contains the conserved 17-amino-acid disulfide-linked ring that is essential for binding to natriuretic peptide receptors (NPR-A and NPR-C) and eliciting biological responses such as natriuresis, diuresis, and vasodilation.

This ANP (Human, 5-27) peptide is suitable for:

• Receptor binding and competition assays with NPR-A and NPR-C
• Signal transduction studies (cGMP production, kinase pathways)
• Cardiovascular and renal physiology research
• Modeling of natriuretic peptide effects in hypertension, heart failure, and renal disease models
• Development of immunoassays and standardization of ANP-related measurements

Usage & Handling Guidance

Store the lyophilized powder at −20 °C. Reconstitute in sterile ultrapure water or 0.1% acetic acid to the desired concentration. Prepare fresh working solutions or single-use aliquots to maintain stability. Avoid repeated freeze–thaw cycles.

• Recommended applications: Receptor binding, cGMP assays, physiological modeling, and immunoassay development
• Working concentration: Optimize empirically (typically nM to μM range depending on the assay)
• Solubility: Soluble in water or dilute acetic acid; sonication may be used if needed
• Handling: Keep on ice during experiments; protect from alkaline conditions that may affect disulfide stability

What You Get

• 500 µg ANP (Human, 5-27) as a high-purity lyophilized powder
• Defined sequence with intact disulfide bond (Cys7–Cys23)
• Molecular weight 2404.4 g/mol
• Biotechnology-grade peptide manufactured under strict quality controls
• For research use only (RUO)

Why Researchers Choose It

• Authentic human ANP fragment containing the biologically active disulfide-linked ring
• High purity and precise molecular weight for reproducible results
• Ideal for receptor pharmacology, signaling studies, and cardiovascular modeling
• Stable powder format for convenient long-term storage and easy reconstitution
• Supports both in vitro mechanistic studies and physiological research applications

Frequently Asked Questions (FAQ)

• What is the sequence and structure of this peptide?
  Sequence: Ser-Ser-Cys-Phe-Gly-Gly-Arg-Met-Asp-Arg-Ile-Gly-Ala-Gln-Ser-Gly-Leu-Gly-Cys-Asn-Ser-Phe-Arg with a disulfide bond between Cys7 and Cys23.
• Why is the disulfide bond important?
  The intramolecular disulfide bridge (Cys7–Cys23) forms the conserved ring structure required for high-affinity binding to natriuretic peptide receptors and biological activity.
• How should I reconstitute the peptide?
  Reconstitute in sterile ultrapure water or 0.1% acetic acid. Prepare aliquots and store at −20 °C to avoid repeated freeze–thaw cycles.
• Is this the full-length ANP or a fragment?
  This is the ANP (5-27) fragment, which retains the functional core and disulfide ring of the mature human ANP hormone.
• What assays is this peptide suitable for?
  It is widely used in receptor binding assays, cGMP signaling studies, immunoassay development, and cardiovascular/renal physiology research.

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References

• 1: Nakagawa Y, Nishikimi T, Kuwahara K. Atrial and brain natriuretic peptides: Hormones secreted from the heart Peptides. 2019 Jan;111:18-25.
• 2: Rubattu S, Gallo G. The Natriuretic Peptides for Hypertension Treatment High Blood Press Cardiovasc Prev. 2022 Jan;29(1):15-21.
• 3: Zheng Q, Li Y, Zhang D, Cui X, Dai K, Yang Y, Liu S, Tan J, Yan Q. ANP promotes proliferation and inhibits apoptosis of ovarian granulosa cells by NPRA/PGRMC1/EGFR complex and improves ovary functions of PCOS rats Cell Death Dis. 2017 Oct 26;8(10):e3145.
• 4: Theilig F, Wu Q. ANP-induced signaling cascade and its implications in renal pathophysiology Am J Physiol Renal Physiol. 2015 May 15;308(10):F1047-55.
• 5: Chen C, Zhang Y, Tao M, Zhao X, Feng Q, Fei X, Fu Y. Atrial Natriuretic Peptide Attenuates Colitis via Inhibition of the cGAS-STING Pathway in Colonic Epithelial Cells Int J Biol Sci. 2022 Feb 7;18(4):1737-1754.
• 6: Hirsch JR, Meyer M, Forssmann WG. ANP and urodilatin: who is who in the kidney Eur J Med Res. 2006 Oct 27;11(10):447-54.
• 7: Sugawara A, Nakao K, Morii N, Yamada T, Itoh H, Shiono S, Saito Y, Mukoyama M, Arai H, Nishimura K, et al. Synthesis of atrial natriuretic polypeptide in human failing hearts. Evidence for altered processing of atrial natriuretic polypeptide precursor and augmented synthesis of beta-human ANP J Clin Invest. 1988 Jun;81(6):1962-70.
• 8: Itoh H, Nakao K, Sugawara A, Saito Y, Mukoyama M, Morii N, Yamada T, Shiono S, Arai H, Hosoda K, et al. Gamma-atrial natriuretic polypeptide (gamma ANP)-derived peptides in human plasma: cosecretion of N-terminal gamma ANP fragment and alpha ANP J Clin Endocrinol Metab. 1988 Sep;67(3):429-37.
• 9: Matsuo A, Nagai-Okatani C, Nishigori M, Kangawa K, Minamino N. Natriuretic peptides in human heart: Novel insight into their molecular forms, functions, and diagnostic use Peptides. 2019 Jan;111:3-17.
• 10: Therrien JP, Kim SM, Terunuma A, Qin Y, Tock CL, Pfützner W, Ohyama M, Schnermann J, Vogel JC. A gene therapy approach for long-term normalization of blood pressure in hypertensive mice by ANP-secreting human skin grafts Proc Natl Acad Sci U S A. 2010 Mar 16;107(11):5118-23.