Host: E. coli • AA: 1-265 (full length) • Tag: C-terminal His • MW: 31 kDa
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HO-1 (human, recombinant)

Item No. 22731

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • Heat Shock Protein 32
  • Heme Oxygenase-1
  • HMOX1
  • Hsp32
Purity
≥90% estimated by SDS-PAGE
Source
Recombinant C-terminal His-tagged expressed in E. coli
Amino Acids
1-265 (full length)
MW
31 kDa
Formulation (Request formulation change)
50 mM HEPES, pH 8.0, with 150 mM sodium chloride
UniProt Accession №
P09601
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    50 µg

    $267

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    Cayman Chemical
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    Product Description

    Heme oxygenase-1 (HO-1), also known as heat shock protein 32 (Hsp32), is an inducible heme oxygenase encoded by the HMOX1 gene.1,2,3 It is a membrane-bound enzyme that catalyzes the cleavage of heme to release carbon monoxide (CO), ferrous ions (Fe2+), and biliverdin, with biliverdin being further processed into bilirubin. HO-1 is found in human spleen, liver, and kidney where its expression is induced by the presence of heme, hormones, metals, oxidative agents, and therapeutic compounds to protect against oxidative stress and inflammatory responses. HO-1 is upregulated in a variety of cancers and siRNA knockdown of HMOX1 or inhibition of HO-1 decreases cancer cell proliferation.4,5,6 HO-1 also interacts with the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) accessory protein Orf3a that, in a similar virus, SARS-CoV, is associated with activation of the NLRP3 inflammasome.7,8,9 Cayman’s HO-1 protein can be used for ELISA and Western blot (WB) applications.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Wang, J., Lad, L., Poulos, T.L., et al. Regiospecificity determinants of human heme oxygenase. The Journal of Biological Chemisty 280(4), 2797-2806 (2005).

    2. Martasek, P., Solangi, K., Goodman, A.I., et al. Properties of human kidney heme oxygenase: Inhibition by synthetic heme analogues and metalloporphyrins. Biochem. Biophys. Res. Commun. 157(2), 480-487 (1988).

    3. Huber, W.J., III, Marohnic, C.C., Peters, M., et al. Measurement of membrane-bound human heme oxygenase-1 activity using a chemically defined assay system. Drug Metab. Dispos. 37(4), 857-864 (2009).

    4. Berberat, P.O., Dambrauskas, Z., Gulbinas, A., et al. Inhibition of heme oxygenase-1 increases responsiveness of pancreatic cancer cells to anticancer treatment. Clin. Cancer Res. 11(10), 3790-3798 (2005).

    5. Nowis, D., Legat, M., Grzela, T., et al. Heme oxygenase-1 protects tumor cells against photodynamic therapy-mediated cytotoxicity. Oncogene 25(24), 3365-3374 (2006).

    6. Fang, J., Akaike, T., and Maeda, H. Antiapoptotic role of heme oxygenase (HO) and the potential of HO as a target in anticancer treatment. Apoptosis 9(1), 27-35 (2004).

    7. Gordon, D.E., Jang, G.M., Bouhaddou, M., et al. A SARS-CoV-2 protein interaction map reveals targets for drug repurposing. Nature 583(7816), 459-468 (2020).

    8. Li, H., Liu, S.-M., Yu, X.-H., et al. Coronavirus disease 2019 (COVID-19): Current status and future perspectives. Int. J. Antimicrob. Agents (2020).

    9. Siu, K.-L., Yuen, K.-S., Castaño-Rodriguez, C., et al. Severe acute respiratory syndrome coronavirus ORF3a protein activates the NLRP3 inflammasome by promoting TRAF3-dependent ubiquitination of ASC. The FASEB Journal 33(8), 8865-8877 (2019).