An iron chelator and inhibitor of prolyl hydroxylases
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Deferoxamine (mesylate)

Item No. 14595

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Formal Name
N4-[5-[[4-[[5-(acetylhydroxyamino)pentyl]amino]-1,4-dioxobutyl]hydroxyamino]pentyl]-N1-(5-aminopentyl)-N1-hydroxy-butanediamide, monomethanesulfonate
CAS Number
138-14-7
Synonyms
  • Ba 33112
  • DFO
  • DFOM
  • DFX
  • NSC 644468
Molecular Formula
C25H48N6O8 • CH3SO3H
Formula Weight
656.8
Purity
≥95%
Formulation (Request formulation change)
A crystalline solid
Solubility(Learn about Variance in Solubility)
DMSO: 5 mg/mlPBS (pH 7.2): 5 mg/ml
SMILES
NCCCCCN(O)C(CCC(NCCCCCN(O)C(CCC(NCCCCCN(O)C(C)=O)=O)=O)=O)=O.CS(=O)(O)=O
InChi Code
InChI=1S/C25H48N6O8.CH4O3S/c1-21(32)29(37)18-9-3-6-16-27-22(33)12-14-25(36)31(39)20-10-4-7-17-28-23(34)11-13-24(35)30(38)19-8-2-5-15-26;1-5(2,3)4/h37-39H,2-20,26H2,1H3,(H,27,33)(H,28,34);1H3,(H,2,3,4)
InChi Key
IDDIJAWJANBQLJ-UHFFFAOYSA-N
Shipping & Storage Information
Storage
-20°C
Shipping
Room temperature in continental US; may vary elsewhere
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    500 mg

    $83

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    1 g

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    5 g

    $590

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    10 g

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    Product Description

    Deferoxamine is a bacterial siderophore that chelates iron.1 It is used to experimentally inhibit iron-dependent prolyl hydroxylases (EC50 = 17.8 µM), thus preventing the degradation of isoforms of hypoxia inducible factor during normoxia.2,3,4 Deferoxamine has applications in diseases that are characterized by high levels of circulating iron, such as thalassemia major.5

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Steinmetz, W.L., Glick, M.R., and Oei, T.O. Modified aca method for determination of iron chelated by deferoxamine and other chelators. Clin. Chem. 26(11), 1593-1597 (1980).

    2. Theriault, J.R., Felts, A.S., Bates, B.S., et al. Discovery of a new molecular probe ML228: An activator of the hypoxia inducible factor (HIF) pathway. Bioorg. Med. Chem. Lett. 22(1), 76-81 (2012).

    3. Jaakkola, P., Mole, D.R., Tian, Y.M., et al. Targeting of HIF-α to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation. Science 292(5516), 468-472 (2001).

    4. Sandau, K.B., Zhou, J., Kietzmann, T., et al. Regulation of the hypoxia-inducible factor 1α by the inflammatory mediators nitric oxide and tumor necrosis factor-α in contrast to desferroxamine and phenylarsine oxide. The Journal of Biological Chemisty 276(43), 39805-39811 (2001).

    5. Neufeld, E.J. Update on iron chelators in thalassemia. Hematology Am. Soc. Hematol. Educ. Program 2010, 451-455 (2010).

    Product Citations

    Zhang, L.J., Salekeen, R., Soto-Palma, C., et al. Article polyunsaturated lipid senolytics exploit a ferroptotic vulnerability in senescent cells. Cell Press Blue 1(1), 100004 (2026).

    Hendricks, J.M., Doubravsky, C., Wehri, E., et al. Identification of structurally diverse FSP1 inhibitors that sensitize cancer cells to ferroptosis. Cell Chem. Biol. 30(9), P1090-P1103 (2022).

    ­Wang, F., Graham, E.T., Naowarojna, N., et al. PALP: A rapid imaging technique for stratifying ferroptosis sensitivity in normal and tumor tissues in situ. Cell Chem. Bio. 29, 157-170 (2022).

    Li, Z., Ferguson, L., Deol, K.K., et al. Ribosome stalling during selenoprotein translation exposes a ferroptosis vulnerability. Nat. Chem. Biol. (2022).

    Armenta, D.A., Laqtom, N.N., Alchemy, G., et al. Ferroptosis inhibition by lysosome-dependent catabolism of extracellular protein. Cell Chem. Biol. 29(11), 1588-1600 (2022).

    Beatty, A., Singh, T., Tyurina, Y.Y., et al. Ferroptotic cell death triggered by conjugated linolenic acids is mediated by ACSL1. Nat. Commun. 12(1), 2244 (2021).

    Du, W., Gu, M., Hu, M., et al. Lysosomal Zn2+ release triggers rapid, mitochondria-mediated, non-apoptotic cell death in metastatic melanoma. Cell Rep. 37(3), 109848 (2021).

    Nagakannan, P., Islam, M.I., Conrad, M., et al. Cathepsin B is an excutioner of ferroptosis. Biochim. Biophys. Acta Mol. Cell Res. 1868(3), 118928 (2021).

    Kremer, D.M., Nelson, B.S., Lin, L., et al. GOT1 inhibition primes pancreatic cancer for ferroptosis through the autophagic release of labile iron. bioRxiv (2020).

    Bersuker, K., Hendricks, J., Li, Z., et al. The CoQ oxidoreductase FSP1 acts parallel to GPX4 to inhibit ferroptosis. Nature 575(7784), 688-692 (2019).

    Cao, J.Y., Poddar, A., Magtanong, L., et al. A genome-wide haploid genetic screen identifies regulators of glutathione abundance and ferroptosis sensitivity. Cell Rep. 26(6), 1544-1556 (2019).

    Magtanong, L., Ko, P.-J., To, M., et al. Exogenous monounsaturated fatty acids promote a ferroptosis-resistant cell state. Cell Chem. Biol. 26(3), 420-432 (2019).

    Sen, A., Ren, S., Lerchenmüller, C., et al. MicroRNA-138 regulates hypoxia-induced endothelial cell dysfunction by targeting S100A1. PLoS One 8(11), e78684 (2013).