(Asn10,Leu11,D-Trp12)-pTH-Related Protein (7-34) amide (human, mouse, rat) carries targeted substitutions that reshape the pharmacophore of the parental peptide. Introduction of D-Trp modifies local geometry and proteolytic stability. Researchers quantify how these changes impact receptor engagement and secondary structure. Applications include antagonist-motif studies, peptide analog design, and receptor-mapping research.
CAT No: R2509
CAS No:129622-68-0
Synonyms/Alias:(Asn10,Leu11,D-Trp12)-pTH-Related Protein (7-34) amide (human, mouse, rat) H-Leu-Leu-His-Asn-Leu-D-Trp-Lys-Ser-Ile-Gln-Asp-Leu-Arg-Arg-Arg-Phe-Phe-Leu-His-His-Leu-Ile-Ala-Glu-Ile-His-Thr-Ala-NH2;129622-68-0;(Asn10,Leu11,D-Trp12)-pTH-Related Protein (7-34) amide (human, mouse, rat) H-Leu-Leu-His-Asn-Leu-D-Trp-Lys-Ser-Ile-Gln-Asp-Leu-Arg-Arg-Arg-Phe-Phe-Leu-His-His-Leu-Ile-Ala-Glu-Ile-His-Thr-Ala-NH2;
(Asn10,Leu11,D-Trp12)-pTH-Related Protein (7-34) amide (human, mouse, rat) is a specialized peptide analog designed for advanced research in peptide hormone signaling and receptor modulation. Characterized by the substitution of Asn at position 10, Leu at position 11, and D-Trp at position 12, this compound exhibits unique receptor-binding properties that distinguish it from native parathyroid hormone-related protein fragments. Its sequence, H-Leu-Leu-His-Asn-Leu-D-Trp-Lys-Ser-Ile-Gln-Asp-Leu-Arg-Arg-Arg-Phe-Phe-Leu-His-His-Leu-Ile-Ala-Glu-Ile-His-Thr-Ala-NH2, enables selective investigation of PTHrP receptor interactions across human, mouse, and rat models. The amide modification at the C-terminus further enhances its stability and bioactivity in experimental settings, making it a valuable tool for probing peptide-receptor dynamics. Researchers benefit from its structural modifications, which allow for precise dissection of signaling pathways and functional domains within the broader parathyroid hormone family.
Receptor Antagonism Studies: (Asn10,Leu11,D-Trp12)-pTH-Related Protein (7-34) amide is widely utilized in studies focused on receptor antagonism, particularly targeting the parathyroid hormone 1 receptor (PTH1R). By competitively inhibiting endogenous ligand binding, this peptide analog enables researchers to delineate the specific contributions of PTHrP signaling in various physiological and pathophysiological contexts. Its ability to selectively block receptor activity aids in the identification of downstream signaling cascades and the mapping of receptor-ligand interaction sites, which are critical for understanding receptor pharmacology and for the development of novel modulators.
Signal Transduction Pathway Analysis: Application of this peptide in cellular and molecular biology laboratories facilitates the dissection of signal transduction pathways activated by PTHrP and related peptides. Through its antagonistic properties, the compound is instrumental in experiments designed to parse out the roles of cyclic AMP, phospholipase C, and other second messenger systems downstream of PTH1R activation. Researchers can use this tool to differentiate between receptor-dependent and independent effects, thereby clarifying the molecular mechanisms underpinning hormone action in bone, kidney, and other tissues.
Comparative Endocrinology: The cross-species compatibility of (Asn10,Leu11,D-Trp12)-pTH-Related Protein (7-34) amide makes it invaluable for comparative endocrinology studies involving human, mouse, and rat models. By employing this analog in parallel experiments, investigators can explore evolutionary conservation and divergence in parathyroid hormone-related peptide signaling. Such studies provide insights into species-specific receptor-ligand interactions, guiding the translation of fundamental findings across different biological systems and informing the selection of appropriate animal models for further research.
Peptide Structure-Activity Relationship (SAR) Investigations: The unique sequence modifications present in this peptide facilitate structure-activity relationship (SAR) studies aimed at identifying critical residues responsible for receptor binding and activity modulation. By systematically comparing the functional outcomes of analogs with distinct amino acid substitutions, scientists can pinpoint key determinants of potency and selectivity. This information is essential for rational design of next-generation peptide therapeutics and for enhancing our understanding of hormone-receptor interface architecture.
Bone and Mineral Research: (Asn10,Leu11,D-Trp12)-pTH-Related Protein (7-34) amide plays a pivotal role in bone and mineral research, where it is employed to investigate the regulatory mechanisms of calcium and phosphate homeostasis. Through targeted receptor inhibition, researchers can assess the contribution of PTHrP signaling to osteoblast and osteoclast function, mineralization processes, and skeletal development. Such studies advance knowledge of bone biology and support the identification of novel molecular targets for modulating bone remodeling in experimental models.
In summary, (Asn10,Leu11,D-Trp12)-pTH-Related Protein (7-34) amide (human, mouse, rat) stands as a versatile and scientifically robust tool for diverse research applications, including receptor antagonism studies, signal transduction pathway analysis, comparative endocrinology, peptide structure-activity relationship investigations, and bone and mineral research. Its tailored sequence and functional specificity empower researchers to unravel complex biological processes, elucidate receptor mechanisms, and drive innovation in peptide-based research across multiple fields of biomedical science.
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