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γ-L-Glutamyl-L-cysteinyl-L-alanine, also known as N-acetylcysteine (NAC), is a tripeptide consisting of three amino acids: L-glutamate, L-cysteine, and L-alanine. It is a precursor to glutathione, a crucial antioxidant in the body that helps protect cells from oxidative stress and supports the immune system. NAC is used in various medical applications, including the treatment of acetaminophen overdose, chronic obstructive pulmonary disease (COPD), and as a mucolytic agent to break down mucus in the respiratory tract. Additionally, it has been studied for its potential benefits in liver disease, neurodegenerative disorders, and as an adjunct therapy in cancer treatment. NAC's antioxidant properties and ability to modulate immune responses make it a significant compound in both therapeutic and research settings.

34286-34-5

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34286-34-5 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 34286-34-5 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 3,4,2,8 and 6 respectively; the second part has 2 digits, 3 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 34286-34:
(7*3)+(6*4)+(5*2)+(4*8)+(3*6)+(2*3)+(1*4)=115
115 % 10 = 5
So 34286-34-5 is a valid CAS Registry Number.

34286-34-5Downstream Products

34286-34-5Relevant academic research and scientific papers

Synthesis of hydroxymethylglutathione from glutathione and L-serine catalyzed by carboxypeptidase Y.

Okumura, Ryosuke,Koizumi, Yukio,Sekiya, Jiro

, p. 434 - 437 (2003)

Hydroxymethylglutathione (gamma-L-glutamyl-L-cysteinyl-L-serine; hmGSH) occurs in many species belonging to the family Gramineae, but the biosynthetic pathway for hmGSH has not been identified. We found that carboxypeptidase Y (CPY), but not carboxypeptidase A, catalyzed hmGSH synthesis from glutathione and L-serine in vitro at acidic pH. CPY also catalyzed methylglutathione synthesis from glutathione and L-alanine. These findings suggested that a carboxypeptidase-like enzyme may be involved in hmGSH synthesis in vivo.

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