Home > Compound List > Product Information
Deferoxamine mesylate salt_Molecular_structure_CAS_138-14-7)
Click picture or here to close

Deferoxamine mesylate salt

Catalog No. D9533 Name Sigma Aldrich
CAS Number 138-14-7 Website http://www.sigmaaldrich.com
M. F. C26H52N6O11S Telephone 1-800-521-8956
M. W. 656.78968 Fax
Purity ≥92.5% (TLC) Email
Storage Chembase ID: 134221

SYNONYMS

IUPAC name
N-(5-aminopentyl)-N-hydroxy-N'-[5-(N-hydroxy-3-{[5-(N-hydroxyacetamido)pentyl]carbamoyl}propanamido)pentyl]butanediamide; methanesulfonic acid
IUPAC Traditional name
deferoxamine; methanesulfonic acid
Synonyms
Deferoxamine methanesulfonate salt
Desferrioxamine mesylate salt
DFOM

DATABASE IDS

EC Number 205-314-3
CAS Number 138-14-7
PubChem SID 24894304
MDL Number MFCD00058605

PROPERTIES

Purity ≥92.5% (TLC)
Apperance white to off-white powder
Solubility H2O: soluble50 mg/mL
Personal Protective Equipment Eyeshields, Gloves, type N95 (US), type P1 (EN143) respirator filter
RTECS UG5310000
Storage Temperature -20°C
German water hazard class 2

DETAILS

Description (English)
Biochem/physiol Actions
An iron chelator used often in the studies of cell proliferation and apoptosis. Has been shown to have anti-proliferative effects on vascular smooth muscle cells in vitro and in vivo and to arrest cells in the G1 phase. Also reported to induce p53. Induces apoptosis in HL-60 cells by chelating iron. After 48 hrs treatment with 1μM deferoxamine, DNA fragmentation was apparent. Cells treated with 0.1 μM deferoxamine for as little as 24 hours were committed to apoptosis; by 48 hrs nuclear collapse was observed. In some studies it has been shown to have antioxidant properties and to protect cells against H2O2-induced damage.
Deferoxamine is used as a hypoxia-mimetic agent to stabilize Hypoxia Inducible Factor 1 (HIF-1). Deferoxamine stabilizes HIF-1 through the inhibition of Prolyl Hydroxylases (PHDs) which target HIF-1 through degradation. The mechanism of deferoxamine inhibition is likely through the chelation of Fe2+ bound to the active site of PHD which is required for enzymatic activity.

REFERENCES