342878-90-4

Basic information

• Product Name: UROTENSIN II-RELATED PEPTIDE (HUMAN, MOUSE, RAT)
• Synonyms: UIIB (HUMAN, MOUSE, RAT);UROTENSIN IIB (HUMAN, MOUSE, RAT);UROTENSIN II-RELATED PEPTIDE;UROTENSIN II-RELATED PEPTIDE (HUMAN, MOUSE, RAT);UROTENSIN II RELATED PEPTIDE, HUMAN, RAT;UROTENSIN II-RELATED PEPTIDE (HUMAN, RAT) (MOUSE);URP (HUMAN, MOUSE, RAT);URP, HUMAN, RAT
• CAS NO: 342878-90-4
• Molecular Formula: C₄₉H₆₄N₁₀O₁₀S₂
• Molecular Weight: 1017.22
• Product Categories: Urotensin receptor
• Mol File: 342878-90-4.mol
• Article Data: 4

Chemical Properties

• Appearance: /
• CAS DataBase Reference: UROTENSIN II-RELATED PEPTIDE (HUMAN, MOUSE, RAT)(CAS DataBase Reference)
• NIST Chemistry Reference: UROTENSIN II-RELATED PEPTIDE (HUMAN, MOUSE, RAT)(342878-90-4)
• EPA Substance Registry System: UROTENSIN II-RELATED PEPTIDE (HUMAN, MOUSE, RAT)(342878-90-4)

Safety Data

• Hazardous Substances Data: 342878-90-4(Hazardous Substances Data)

Usage

General Description

Urotensin II-Related Peptide (URP) is a peptide hormone found in human, mouse, and rat species. URP is a member of the urotensin neuropeptide family and is involved in the regulation of various physiological processes, including cardiovascular function and smooth muscle contraction. It acts as a ligand for the urotensin II receptor and is known to have vasodilatory effects, as well as potential roles in inflammation and pain modulation. URP may also play a role in the pathophysiology of various diseases, making it a potential target for therapeutic intervention. Overall, Urotensin II-Related Peptide has important implications for understanding and potentially treating a variety of physiological and pathological conditions in humans, mice, and rats.

Upstream product

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Relevant articles and documents

Functional Selectivity Revealed by N-Methylation Scanning of Human Urotensin II and Related Peptides

In accordance with their common but also divergent physiological actions, human urotensin II (1) and urotensin II-related peptide (2) could stabilize specific urotensin II receptor (UTR) conformations, thereby activating different signaling pathways, a feature referred to as biased agonism or functional selectivity. Sequential N-methylation of the amides in the conserved core sequence of 1, 2, and fragment U-II4-11 (3) shed light on structural requirements involved in their functional selectivity. Thus, 18 N-methylated UTR ligands were synthesized and their biological profiles evaluated using in vitro competition binding assays, ex vivo rat aortic ring bioassays and BRET-based biosensor experiments. Biological activity diverged from that of the parent structures contingent on the location of amide methylation, indicating relevant hydrogen-bond interactions for the function of the endogenous peptides. Conformational analysis of selected N-methyl analogs indicated the importance of specific amide residues of 2 for the distinct pharmacology relative to 1 and 3.

An investigation into the origin of the biased agonism associated with the urotensin II receptor activation

The urotensin II receptor (UTR) has long been studied mainly for its involvement in the cardiovascular homeostasis both in health and disease state. Two endogenous ligands activate UTR, i.e. urotensin II (U-II) and urotensin II-related peptide (URP). Exte