Description

Product Description

Copeptin (human) (CAS 78362-34-2) is a peptide biomarker derived from the 39-amino acid C-terminal portion of the arginine vasopressin (AVP) precursor peptide, pre-proAVP. Synthesized and secreted from the magnocellular neurons of the hypothalamus, copeptin is co-released with AVP into the bloodstream from the posterior pituitary in equimolar amounts.

AVP, also known as antidiuretic hormone (ADH), is a key regulator of water homeostasis, vascular tone, and stress response. However, the direct measurement of AVP in serum is technically challenging due to its instability and short half-life. Copeptin overcomes these limitations as a biologically inert yet highly stable surrogate marker that accurately reflects vasopressin release and neuroendocrine activity.

Since its identification, copeptin has revolutionized the diagnostic landscape of cardiovascular, renal, and metabolic disorders. In particular, copeptin levels serve as a reliable prognostic marker in acute myocardial infarction (AMI), heart failure, sepsis, stroke, and stress-induced syndromes.

Molecular and Structural Insights

Copeptin is a glycosylated peptide comprising the C-terminal segment of pre-proAVP, which includes the signal peptide, AVP, neurophysin II, and copeptin domains. During post-translational processing in the endoplasmic reticulum and Golgi apparatus, pre-proAVP is cleaved into arginine vasopressin, neurophysin II (carrier protein), and copeptin. These three components are stored in secretory granules within the posterior pituitary and released simultaneously upon physiological stimulation.

Unlike AVP, copeptin exhibits exceptional thermal and enzymatic stability, making it a preferred biomarker for clinical and translational research applications. Its circulating half-life allows for reproducible and quantitative assessment using standard immunoassay platforms such as ELISA, ECLIA, and immunoluminometric assays (ILMA).

Biological and Clinical Significance

Copeptin release is stimulated by a variety of physiological stressors, including:

• Hypovolemia and hypotension (via baroreceptor activation)

• Hyperosmolality (plasma osmolality regulation)

• Infection and sepsis

• Acute myocardial ischemia

• Surgical trauma and metabolic stress

In clinical studies, copeptin demonstrates strong predictive value for short-term and long-term mortality in patients with heart failure, acute coronary syndromes, stroke, and critical illness. It serves as an early marker of neuroendocrine activation in response to systemic stress, correlating closely with cortisol, ACTH, and catecholamine levels.

Additionally, copeptin levels can distinguish between central diabetes insipidus, nephrogenic diabetes insipidus, and primary polydipsia, making it an important tool in endocrine diagnostic research.

Applications in Research

• Cardiovascular and ischemic biomarker discovery

• Neuroendocrine and stress physiology studies

• Vasopressin secretion and osmoregulation modeling

• Clinical diagnostics development

• Translational research on acute and chronic diseases

Summary

Copeptin (human) bridges fundamental peptide biochemistry with clinical relevance, offering a stable, quantifiable, and biologically correlated indicator of vasopressin system activation. Its integration into diagnostic panels enhances early detection, risk stratification, and monitoring of patients in critical care, cardiology, and endocrinology research domains.

Product Specifications

Synonyms

• Pre-proAVP C-terminal peptide

• Copeptin peptide fragment

• Human copeptin

• AVP precursor peptide

Mechanism of Action

Copeptin (human) serves primarily as a surrogate marker for vasopressin secretion rather than an active biological effector. It is co-synthesized and co-released with arginine vasopressin (AVP) in equimolar quantities.

In the hypothalamic-pituitary axis, pre-proAVP is processed within the magnocellular neurons of the supraoptic (SON) and paraventricular (PVN) nuclei. Upon release, copeptin mirrors vasopressin’s secretion patterns, which are triggered by plasma osmolality, blood pressure, and stress signals.

Vasopressin itself acts on V1 (vascular), V2 (renal), and V3 (pituitary) receptors, regulating water reabsorption, vasoconstriction, and ACTH release. Although copeptin does not bind these receptors, its stoichiometric release with AVP provides an indirect yet accurate measure of neuroendocrine activity.

Mechanistically, copeptin is processed as follows:

1. Synthesis of pre-proAVP (164 amino acids) in the hypothalamus.

2. Proteolytic cleavage yields three peptides: AVP, neurophysin II, and copeptin.

3. Co-storage and co-secretion from the posterior pituitary.

4. Circulation in plasma, where copeptin remains stable and measurable.

By quantifying copeptin concentrations, researchers can infer the vasopressinergic system’s activation level under stress, hemodynamic changes, and endocrine feedback loops.

The use of copeptin as a diagnostic biomarker has been validated in multiple studies, showing its superiority to AVP assays in terms of stability, reproducibility, and clinical practicality.

Side Effects / Safety Notes

Copeptin (human) is intended strictly for research use only. It exhibits no known biological toxicity in vitro or in vivo as it is biologically inactive. Laboratory personnel should handle the compound using appropriate biosafety standards and avoid direct contact or ingestion.

Disclaimer

This product is not intended for human or veterinary use. All data are provided for research and educational purposes only. Copeptin (human) should be handled in accordance with institutional biosafety and chemical hygiene protocols. Users are responsible for ensuring compliance with local regulatory standards.

Keywords

Copeptin human peptide, AVP precursor peptide, vasopressin biomarker, cardiovascular disease biomarker, endocrine research peptide, stress marker peptide, copeptin ELISA standard, pre-proAVP fragment, diagnostic peptide standard, human copeptin CAS 78362-34-2

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