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A9232

Sigma-Aldrich

AMI-1 sodium salt hydrate

≥98% (HPLC)

Sinónimos:

7,7′-Carbonylbis(azanediyl)bis(4-hydroxynaphthalene-2-sulfonic acid) sodium salt hydrate

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About This Item

Fórmula empírica (notación de Hill):
C21H16N2O9S2 · xNa+ · yH2O
Peso molecular:
504.49 (anhydrous free acid basis)
UNSPSC Code:
12352200
NACRES:
NA.77

Quality Level

100

assay

≥98% (HPLC)

form

powder

storage condition

desiccated
protect from light

color

purple

solubility

H2O: >10 mg/mL

storage temp.

2-8°C

Biochem/physiol Actions

Protein arginine N-methyltransferases (PRMTs) are involved in post-translational modification implicated in protein trafficking, signal transduction, and transcriptional regulation. AMI-1 does not inhibit lysine methyltransferase activity and does not interact with S-adenosylmethionine (AdoMet), unlike most methyltransferase inhibitors which compete for the AdoMet binding site. AMI-1 can modulate nuclear receptor-regulated transcription from estrogen and androgen response elements; and is a HIV-1 reverse transcriptase inhibitor. AMI-1 is a potent antagonist of NADPH-oxidase-derived superoxide production, but acts as a direct antioxidant rather than indirectly through methyltransferase inhibition.

Features and Benefits

This compound is a featured product for Gene Regulation research. Click here to discover more featured Gene Regulation products. Learn more about bioactive small molecules for other areas of research at sigma.com/discover-bsm.

pictograms

Exclamation mark
GHS07

signalword

Warning

Hazard Classifications

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

dust mask type N95 (US), Eyeshields, Gloves

Certificados de análisis (COA)

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Cingulate protein arginine methyltransferases 1 regulates peripheral hypersensitivity via fragile X messenger ribonucleoprotein.
Wu, et al.
Frontiers in Molecular Neuroscience, 16, 1153870-1153870 (2023)
Wenya Hou et al.
Developmental cell, 45(2), 262-275 (2018-04-25)
The complex architecture of neuronal networks in the brain requires tight control of the actin cytoskeleton. The actin nucleator Cobl is critical for neuronal morphogenesis. Here we reveal that Cobl is controlled by arginine methylation. Coprecipitations, coimmunoprecipitations, cellular reconstitutions, and in vitro
Kirti Lathoria et al.
Autophagy, 19(7), 1997-2014 (2023-01-18)
Mutations in the Krebs cycle enzyme IDH1 (isocitrate dehydrogenase (NADP(+)) 1) are associated with better prognosis in gliomas. Though IDH1 mutant (IDH1R132H) tumors are characterized by their antiproliferative signatures maintained through hypermethylation of DNA and chromatin, mechanisms affecting cell death

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