97588-64-2 Usage
Description
(5Z,12Z,15S)-15-hydroxy-11-oxoprosta-5,9,12-trien-1-oic acid, a type of prostaglandin, is a lipid compound that functions as a hormone-like substance within the body. Derived from arachidonic acid, this prostaglandin is involved in various physiological processes, including inflammation, immune response, and smooth muscle contraction. Its unique chemical structure, characterized by an omega-6 fatty acid derivative with a hydroxyl group at the 15th carbon position, indicates its potential significance in health and disease, making it a crucial subject for pharmaceutical and biochemical research.
Uses
Used in Pharmaceutical Research:
(5Z,12Z,15S)-15-hydroxy-11-oxoprosta-5,9,12-trien-1-oic acid is used as a target compound for pharmaceutical research due to its involvement in critical physiological processes. Its role in inflammation, immune response, and smooth muscle contraction makes it a promising candidate for the development of new drugs targeting these pathways.
Used in Biochemical Research:
In the field of biochemical research, (5Z,12Z,15S)-15-hydroxy-11-oxoprosta-5,9,12-trien-1-oic acid serves as an important subject for understanding the complex interactions and mechanisms underlying various biological functions. Studying this prostaglandin can provide insights into the regulation of inflammation, immune response, and muscle contraction, potentially leading to the discovery of novel therapeutic approaches.
Used in the Development of Anti-inflammatory Agents:
Given its role in inflammation, (5Z,12Z,15S)-15-hydroxy-11-oxoprosta-5,9,12-trien-1-oic acid is used as a starting point for the development of anti-inflammatory agents. By modulating the activity of this prostaglandin, researchers aim to create medications that can alleviate inflammation and its associated symptoms.
Used in the Study of Smooth Muscle Contraction:
(5Z,12Z,15S)-15-hydroxy-11-oxoprosta-5,9,12-trien-1-oic acid is utilized in the study of smooth muscle contraction, as it plays a role in this process. Understanding its mechanism of action can help in the development of treatments for conditions involving abnormal muscle contractions, such as asthma or certain cardiovascular diseases.
Used in Immunomodulatory Research:
As this prostaglandin is involved in the immune response, (5Z,12Z,15S)-15-hydroxy-11-oxoprosta-5,9,12-trien-1-oic acid is used in immunomodulatory research. Its study can contribute to the development of immunomodulatory drugs that can either enhance or suppress the immune system, depending on the therapeutic goal.
Check Digit Verification of cas no
The CAS Registry Mumber 97588-64-2 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 9,7,5,8 and 8 respectively; the second part has 2 digits, 6 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 97588-64:
(7*9)+(6*7)+(5*5)+(4*8)+(3*8)+(2*6)+(1*4)=202
202 % 10 = 2
So 97588-64-2 is a valid CAS Registry Number.
97588-64-2Relevant articles and documents
Δ12-Prostaglandin J2 as a product and ligand of human serum albumin: Formation of an unusual covalent adduct at His146
Yamaguchi, Satoru,Aldini, Giancarlo,Ito, Sohei,Morishita, Nozomi,Shibata, Takahiro,Vistoli, Giulio,Carini, Marina,Uchida, Koji
body text, p. 824 - 832 (2010/03/25)
Human serum albumin (HSA), the most abundant protein in plasma, has a very unique function, catalyzing the conversion of prostaglandin J2 (PGJ2), a dehydration product of PGD2, to yield Δ12-PGJ2. These PGD2 metabolites are actively transported into cells and accumulated in the nuclei, where they act as potent inducers of cell growth inhibition and cell differentiation, and exhibit their own unique spectrum of biological effects. The facts that (i) arachidonic acid metabolites bind to human serum albumin (HSA) and the metabolism of these molecules is altered as a result of binding, (ii) HSA catalyzes the transformation of PGJ2 into Δ12-PGJ2, and (iii) Δ12-PGJ2 is stable in serum suggest that HSA may bind and stabilize Δ12-PGJ2 in a specific manner. A molecular interaction analysis using surface plasmon resonance (Biacore) indeed suggested the presence of a specific Δ12-PGJ 2-binding site in HSA. To investigate the molecular details of the binding of this PGD2 metabolite to albumin, we analyzed the cocrystal structure of the HSA-Δ12-PGJ2-myristate complex by X-ray crystallography and found that two Δ12-PGJ12 molecules bind to a primary site in subdomain IB of the protein. The electron density results suggested that one of the two Δ12-PGJ 12 molecules that specifically bind to the site covalently interacted with a histidine residue (His146). Using nano-LC-MS/MS analysis of the HSA-Δ12-PGJ2 complex, the formation of an unusual Δ12-PGJ2-histidine adduct at His146 was confirmed. Thus, our crystallographic and mass spectrometric analyses of the HSA-Δ12-PGJ2 complex provided intriguing new insights into the molecular details of how this electrophilic ligand interacts with its primary producer and transporter.
