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Chemical structure of CAS 1504-06-9

3-Methyl-2-indolinone

In Stock•Starting at $8 for 250 mg•Purity ≥ 97%
CAS No.1504-06-9
MDL No.MFCD04037370
MFC9H9NO
MW147.17
InChI KeyBBZCPUCZKLTAJQ-UHFFFAOYSA-N
CUSTOM SYNTHESIS

Pricing & Availability

Pack SizePurityPriceAvailabilityAction
250 mg97%$8In Stock
1 g97%$12In Stock
5 g97%$32In Stock
10 g97%$59In Stock
25 g97%$143In Stock
Custom synthesis and bulk supply options are available upon request.

Product Information

3-Methyloxindole is an oxindole in which a methyl group replaces a hydrogen at position 3 of the oxindole (1,3-dihydro-2H-indol-2-one) ring. It belongs to the class of oxindoles and is also classified as a methylindole.

CAS No.1504-06-9
Product Name3-Methyl-2-indolinone
IrritantIrritant
Signal Word:Warning
HCode:H315-H319-H335
PCode:P261-P264-P264+P265-P271-P280-P302+P352-P304+P340-P305+P351+P338-P319-P321-P332+P317-P337+P317-P362+P364-P403+P233-P405-P501

Related Articles

Studies related to this compound and its mechanism of action

End-product inhibition of skatole-metabolising enzymes CYP1A, CYP2A19 and CYP2E1 in porcine and piscine hepatic microsomes.

Toxicology letters • Vol. 303 • 2019
PMID: 30599194DOI: 10.1016/j.toxlet.2018.12.017

Respective roles of CYP2A5 and CYP2F2 in the bioactivation of 3-methylindole in mouse olfactory mucosa and lung: studies using Cyp2a5-null and Cyp2f2-null mouse models.

Drug metabolism and disposition: the biological fate of chemicals • Vol. 40, Issue 4 • 2012
PMID: 22228748PMC: PMC3310420DOI: 10.1124/dmd.111.044081

The pneumotoxin 3-methylindole is a substrate and a mechanism-based inactivator of CYP2A13, a human cytochrome P450 enzyme preferentially expressed in the respiratory tract.

Drug metabolism and disposition: the biological fate of chemicals • Vol. 37, Issue 10 • 2009
PMID: 19608696PMC: PMC2769036DOI: 10.1124/dmd.109.027300

Porcine CYP2A19, CYP2E1 and CYP1A2 forms are responsible for skatole biotransformation in the reconstituted system.

Neuro endocrinology letters • Vol. 30 Suppl 1 • 2009
PMID: 20027142

Documentation

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