4973-51-7 Usage
Uses
Used in Pharmaceutical Industry:
3,5-Dimethoxy-4-hydroxybenzylamine is used as a building block for the synthesis of various bioactive compounds, contributing to the development of new drugs with potential therapeutic applications.
Used in Antioxidant Applications:
3,5-Dimethoxy-4-hydroxybenzylamine is used as an antioxidant agent, helping to protect cells from oxidative stress and damage, which can contribute to various diseases and aging.
Used in Anti-inflammatory Applications:
3,5-Dimethoxy-4-hydroxybenzylamine is used as an anti-inflammatory agent, potentially reducing inflammation and alleviating symptoms associated with inflammatory conditions.
Used in Neuroprotective Applications:
3,5-Dimethoxy-4-hydroxybenzylamine is used as a neuroprotective agent, offering potential benefits in the treatment and prevention of neurological disorders.
Used in Neurological Disorders Treatment:
3,5-Dimethoxy-4-hydroxybenzylamine is used as a therapeutic agent for the treatment of neurological disorders such as Parkinson's disease and Alzheimer's disease, due to its potential neuroprotective effects.
Check Digit Verification of cas no
The CAS Registry Mumber 4973-51-7 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 4,9,7 and 3 respectively; the second part has 2 digits, 5 and 1 respectively.
Calculate Digit Verification of CAS Registry Number 4973-51:
(6*4)+(5*9)+(4*7)+(3*3)+(2*5)+(1*1)=117
117 % 10 = 7
So 4973-51-7 is a valid CAS Registry Number.
4973-51-7Relevant academic research and scientific papers
Catechol O methyltransferase. VI. Affinity labeling with N haloacetyl 3,5 dimethoxy 4 hydroxyphenylalkylamines
Borchardt,Thakker
, p. 152 - 158 (2007/10/06)
Several N acyl 4 hydroxy 3,5 dimethoxy phenylalkylamines were synthesized and evaluated for ability to inactivate catechol O methyltransferase (COMT). 4 Hydroxy N iodoacetyl 3,5 dimethoxy phenylethylamine was found to rapidly and irreversibly inactivate this enzyme. The corresponding n concentrations bromoacetyl derivative also produced inactivation of COMT but at a slower rate than the N iodoacetyl derivative. The N acetyl and N fumaryl derivatives were completely inactive. Inactivation of COMT by these reagents appears to proceed by a unimolecular reaction within a dissociable complex rather than by a nonspecific bimolecular reaction. The proximity of the amino acid residue being modified relative to the site which binds the aromatic portion of these inhibitors was determined using N iodoactylphenylalkylamines of varying chain length. The number of methylene carbons separating the aromatic ring and the iodoacetamide moiety in these inhibitors did not greatly influence the binding to COMT nor did it affect how rapidly the enzyme was inactivated. From these observations it is concluded that the amino acid moiety being modified by this class of affinity labeling reagents must be relatively close to or part of the site which binds the aromatic region of these inhibitors.
