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CIS-9-OCTADECENOYL COENZYME A POTASSIUM SALT is a chemical compound that is a derivative of coenzyme A (CoA), which is an essential component in biochemical reactions responsible for energy production from nutrients. This specific variant, with its potassium salt form, may possess unique properties or functions that make it valuable for certain scientific research applications, particularly in biochemistry and pharmacology. Its complex structure and functionality may lead to various alternative names or tags in different scientific contexts.

1716-06-9

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1716-06-9 Usage

Uses

Used in Scientific Research:
CIS-9-OCTADECENOYL COENZYME A POTASSIUM SALT is used as a research compound for its potential roles in biochemical and pharmacological studies. Its unique properties as a derivative of coenzyme A with a potassium salt form may provide insights into energy metabolism and related biological processes.
Used in Biochemistry:
In the field of biochemistry, CIS-9-OCTADECENOYL COENZYME A POTASSIUM SALT is used as a tool to investigate the mechanisms of energy production and the role of coenzyme A in various metabolic pathways. Its potassium salt form may offer specific advantages in these studies, such as improved stability or reactivity.
Used in Pharmacology:
In pharmacological research, CIS-9-OCTADECENOYL COENZYME A POTASSIUM SALT may be employed to explore its potential therapeutic applications, particularly in the context of energy metabolism disorders or diseases related to mitochondrial function. Its unique structure and properties could lead to the development of new drugs or therapeutic strategies.

Check Digit Verification of cas no

The CAS Registry Mumber 1716-06-9 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 1,7,1 and 6 respectively; the second part has 2 digits, 0 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 1716-06:
(6*1)+(5*7)+(4*1)+(3*6)+(2*0)+(1*6)=69
69 % 10 = 9
So 1716-06-9 is a valid CAS Registry Number.
InChI:InChI=1/C39H68N7O17P3S/c1-4-5-6-7-8-9-10-11-12-13-14-15-16-17-18-19-30(48)67-23-22-41-29(47)20-21-42-37(51)34(50)39(2,3)25-60-66(57,58)63-65(55,56)59-24-28-33(62-64(52,53)54)32(49)38(61-28)46-27-45-31-35(40)43-26-44-36(31)46/h11-12,26-28,32-34,38,49-50H,4-10,13-25H2,1-3H3,(H,41,47)(H,42,51)(H,55,56)(H,57,58)(H2,40,43,44)(H2,52,53,54)/b12-11-/t28-,32-,33-,34?,38-/m1/s1

1716-06-9SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 20, 2017

Revision Date: Aug 20, 2017

1.Identification

1.1 GHS Product identifier

Product name oleoyl-CoA

1.2 Other means of identification

Product number -
Other names <U-14C>-Oleyl-CoA

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:1716-06-9 SDS

1716-06-9Upstream product

1716-06-9Downstream Products

1716-06-9Relevant academic research and scientific papers

The β oxidative cleavage of long chain fatty acids in rat liver cytoplasm

Fiecchi,Galli-Kienle,Scala,Galli,Paoletti

, p. 516 - 528 (2007/10/09)

A β oxidative cleavage of oleyl and stearyl CoA has been obtained with soluble enzymes of rat liver homogenate. The transformation requires NAD+ as an oxido reductive cofactor and is enhanced by ATP and CoA. Under the reported conditions 2,9 octadecadienoic, 3,9 octadecadienoic, 3 hydroxy 9 octadecenoic, 7 hexadecenoic, 3 hydroxy 7 hexadecenoic and 5 tetradecenoic acids are present after incubation of oleyl CoA, while no detectable amounts of shorter fatty acids are formed. A similar oxidation pattern is obtained with stearyl CoA when Mg2+ ions are also added to the system. The cytoplasmic origin of these enzymes is established by comparing their activity with that of the mitochondrial β oxidation enzymes.

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