98462-03-4 Usage
Uses
Used in Pharmaceutical Industry:
8(S)-HETE is used as a pharmacological tool for studying the role of PKC and PPARα in various cellular processes and diseases. Its activation of these signaling molecules can provide insights into the development of novel therapeutic strategies for treating conditions associated with PKC and PPARα dysregulation.
Used in Research Applications:
8(S)-HETE is used as a research compound in the field of cell biology and molecular biology. It helps researchers investigate the mechanisms of action of PKC and PPARα, as well as their involvement in various physiological and pathological processes. This knowledge can contribute to a better understanding of the underlying causes of certain diseases and the identification of potential therapeutic targets.
Used in Drug Discovery and Development:
8(S)-HETE is used as a lead compound in the development of new drugs targeting PKC and PPARα. Its ability to modulate the activity of these signaling molecules can be harnessed to create innovative therapeutic agents for the treatment of various diseases, including metabolic disorders, inflammatory conditions, and cancer.
Check Digit Verification of cas no
The CAS Registry Mumber 98462-03-4 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 9,8,4,6 and 2 respectively; the second part has 2 digits, 0 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 98462-03:
(7*9)+(6*8)+(5*4)+(4*6)+(3*2)+(2*0)+(1*3)=164
164 % 10 = 4
So 98462-03-4 is a valid CAS Registry Number.
InChI:InChI=1/C20H32O3/c1-2-3-4-5-6-7-8-9-10-13-16-19(21)17-14-11-12-15-18-20(22)23/h6-7,9-11,13-14,16,19,21H,2-5,8,12,15,17-18H2,1H3,(H,22,23)/b7-6-,10-9-,14-11-,16-13+/t19-/m1/s1
98462-03-4Relevant academic research and scientific papers
Crystal structure of a lipoxygenase in complex with substrate: The arachidonic acid-binding site of 8R-lipoxygenase
Neau, David B.,Bender, Gunes,Boeglin, William E.,Bartlett, Sue G.,Brash, Alan R.,Newcomer, Marcia E.
, p. 31905 - 31913 (2015/02/19)
Lipoxygenases (LOX) play critical roles in mammalian biology in the generation of potent lipid mediators of the inflammatory response; consequently, they are targets for the development of isoform-specific inhibitors. The regio- and stereo-specificity of the oxygenation of polyunsaturated fatty acids by the enzymes is understood in terms of the chemistry, but structural observation of the enzyme-substrate interactions is lacking. Although several LOX crystal structures are available, heretofore the rapid oxygenation of bound substrate has precluded capture of the enzyme-substrate complex, leaving a gap between chemical and structural insights. In this report, we describe the 2.0 ? resolution structure of 8R-LOX in complex with arachidonic acid obtained under anaerobic conditions. Subtle rearrangements, primarily in the side chains of three amino acids, allow binding of arachidonic acid in a catalytically competent conformation. Accompanying experimental work supports a model in which both substrate tethering and cavity depth contribute to positioning the appropriate carbon at the catalytic machinery.
ENANTIOSPECIFIC TOTAL SYNTHESIS OF 8- and 12-HYDROXYEICOSATETRAENOIC ACID
Yadagiri, Pendri,Lumin, Sun,Mosset, Paul,Capdevila, Jorge,Falck, J. R.
, p. 6039 - 6040 (2007/10/02)
The R- and S-isomers of 8- and 12-hidroxyeicosatetraenoic acid (8- and 12-HETE) were synthesized from dimethyl malate derived precursors.
