18908-20-8 Usage
Uses
Used in Chemical Industry:
(2-METHYL-2-PROPEN-1-YL)SUCCINIC ANHHYDRIDE is used as a raw material for the production of various resins, plastics, and chemical intermediates due to its versatile chemical properties and reactivity.
Used in Pharmaceutical Industry:
(2-METHYL-2-PROPEN-1-YL)SUCCINIC ANHYDRIDE is used as a chemical reagent in the synthesis of pharmaceuticals, contributing to the development of new drugs and therapeutic agents.
Used in Agricultural Chemical Industry:
(2-METHYL-2-PROPEN-1-YL)SUCCINIC ANHYDRIDE is used as a chemical reagent in the synthesis of agricultural chemicals, aiding in the production of effective and efficient agrochemicals for crop protection and enhancement.
Used in Safety and Health Precautions:
(2-METHYL-2-PROPEN-1-YL)SUCCINIC ANHYDRIDE is used as a reference compound for safety and health precautions in industrial settings, as it is a skin and respiratory irritant, and exposure to high concentrations can cause irritation to the eyes, nose, and throat. This highlights the importance of proper handling and safety measures to protect workers and the environment.
Check Digit Verification of cas no
The CAS Registry Mumber 18908-20-8 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 1,8,9,0 and 8 respectively; the second part has 2 digits, 2 and 0 respectively.
Calculate Digit Verification of CAS Registry Number 18908-20:
(7*1)+(6*8)+(5*9)+(4*0)+(3*8)+(2*2)+(1*0)=128
128 % 10 = 8
So 18908-20-8 is a valid CAS Registry Number.
18908-20-8Relevant academic research and scientific papers
Matrix metalloproteinase inhibitors: A structure-activity study
Levy, Daniel E.,Lapierre, France,Liang, Weisheng,Ye, Wenqing,Lange, Christopher W.,Li, Xiaoyuan,Grobelny, Damian,Casabonne, Marie,Tyrrell, David,Holme, Kevin,Nadzan, Alex,Galardy, Richard E.
, p. 199 - 223 (2007/10/03)
Modifications around the dipeptide-mimetic core of a hydroxamic acid based matrix metalloproteinase inhibitor were studied. These variations incorporated a variety of natural, unnatural, and synthetic amino acids inaddition to modifications of the P1' and P3' substituents. The results of this study indicate the following structural requirements: (2) Potent inhibitorsmust possess string zinc-binding functionalities. (3) The potential importance of the hydrophobic group at position R3 as illustratedby itsability to impart greater relative potency against stromelysin when larger hydrophobic groups are used. (4) Requirements surrounding the nature of the amino acid appear to be more restrictive for stromelysin than for neutrophil collagenase, 72 kDa gelatinase, and 92 kDa gelatinase. These requirements may involve planar fused-ring aryl systems and possibly hydrogen-bonding capabilities.