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Urotensin II is a potent vasoconstrictor peptide that plays a significant role in the regulation of cardiovascular function. It is a cyclic undecapeptide, which means it consists of 11 amino acids arranged in a circular structure. Initially discovered in the urophysis, a specialized neurosecretory tissue in fish, urotensin II has since been identified in various mammalian species, including humans. This peptide exerts its effects by binding to the urotensin II receptor (UT), leading to vasoconstriction and increased blood pressure. It has been implicated in various physiological processes, such as the regulation of blood flow, fluid balance, and cardiovascular homeostasis. Additionally, urotensin II has been associated with the pathophysiology of hypertension and other cardiovascular diseases, making it a potential therapeutic target for the treatment of these conditions.

9047-55-6

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9047-55-6 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 9047-55-6 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 9,0,4 and 7 respectively; the second part has 2 digits, 5 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 9047-55:
(6*9)+(5*0)+(4*4)+(3*7)+(2*5)+(1*5)=106
106 % 10 = 6
So 9047-55-6 is a valid CAS Registry Number.

9047-55-6SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 14, 2017

Revision Date: Aug 14, 2017

1.Identification

1.1 GHS Product identifier

Product name UROTENSIN II, FROG

1.2 Other means of identification

Product number -
Other names UROSPERMAL I

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:9047-55-6 SDS

9047-55-6Downstream Products

9047-55-6Relevant academic research and scientific papers

Disulfide bond formation in S-Acetamidomethyl cysteine-containing peptides by the combination of silver trifluoromethanesulfonate and dimethylsulfoxide / aqueous HCI

Tamamura, Hirokazu,Otaka, Akira,Nakamura, Junko,Okubo, Kaori,Koide, Takaki,Ikeda, Kyoko,Fujii, Nobutaka

, p. 4931 - 4934 (2007/10/02)

S-Acetamidomethyl (Acm) cysteine was found to be converted quantitatively to cystine by deprotection of the Acm group with silver trifluoromethanesulfonate (AgOTf) followed by dimethylsulfoxide (DMSO) / aqueous hydrochloric acid (HCl) treatment. No significant side reactions were observed with oxidation-sensitive amino acids such as Met, Tyr, and Trp under these reaction conditions. This method has been applied successfully to the syntheses of oxytocin and a Trp-containing peptide, urotensin II.

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