Angiotensinogen (1-14), human is a fragment of the renin substrate angiotensinogen, a precursor for all angiotensin peptides.
CAT No: R1205
CAS No:104180-23-6
Synonyms/Alias:ANGIOTENSINOGEN (1-14), HUMAN;104180-23-6;H-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Asn-OH;DA-74015;FA110836;
Angiotensinogen (1-14), human is a synthetic peptide fragment corresponding to the N-terminal 14 amino acids of the human angiotensinogen protein. As a key component of the renin-angiotensin system (RAS), this peptide serves as a valuable biochemical tool for dissecting the molecular mechanisms underlying blood pressure regulation, fluid balance, and cardiovascular homeostasis. Its sequence encompasses the region from which angiotensin I is enzymatically liberated by renin, making it highly relevant for research focused on the early events of angiotensin peptide generation and signaling. The ability to work with a defined angiotensinogen fragment provides researchers with precise control over experimental conditions, facilitating detailed studies in enzymology, receptor biology, and peptide structure-function relationships.
Enzymatic substrate studies: Angiotensinogen (1-14), human is frequently employed as a substrate in enzymatic assays designed to characterize the activity and specificity of renin and related proteases. By offering a defined peptide sequence, it enables accurate kinetic analyses and mapping of cleavage sites, supporting the investigation of enzyme-substrate interactions central to the RAS. Researchers can utilize this fragment to assess the efficiency of proteolytic processing, screen for potential inhibitors, and gain mechanistic insights into the regulation of angiotensin peptide generation.
Peptide-receptor interaction analysis: The defined sequence of this angiotensinogen fragment is valuable for exploring the binding affinities and selectivities of angiotensin receptors and associated binding proteins. In vitro binding studies utilizing this peptide can reveal critical determinants of receptor recognition and activation, inform on structure-activity relationships, and help elucidate the pharmacological profiles of novel receptor modulators. Such work is instrumental in advancing the understanding of peptide-receptor dynamics within the context of cardiovascular and renal research.
Peptide synthesis and modification research: As an authentic fragment of human angiotensinogen, the peptide serves as a starting point for the synthesis of analogs, labeled derivatives, or modified peptides. Researchers often use it to develop new molecular probes or to investigate the effects of sequence alterations on biological function. Its utility in solid-phase peptide synthesis and post-synthetic modification protocols makes it a versatile platform for advancing peptide engineering and analytical chemistry applications.
Analytical method development: The unique sequence and biochemical properties of Angiotensinogen (1-14), human make it an effective standard or reference material in mass spectrometry, chromatography, and immunoassay development. It can be used to calibrate instruments, validate peptide detection protocols, and optimize sample preparation workflows. Its defined composition supports the establishment of reliable analytical methods for the quantification and characterization of angiotensin peptides in complex biological matrices.
Cell signaling and pathway elucidation: Researchers leverage this peptide to investigate the downstream signaling events triggered by angiotensin peptide fragments in cellular systems. By treating cultured cells or isolated tissues with the angiotensinogen (1-14) fragment, scientists can monitor changes in intracellular signaling cascades, gene expression profiles, or physiological responses. These studies contribute to a deeper understanding of the RAS's role in diverse biological processes and provide a foundation for the identification of novel regulatory mechanisms.
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