HO-1 (human recombinant)

Heme oxygenase-1 (HO-1), also known as heat shock protein 32 (Hsp32), is an inducible heme oxygenase encoded by the HMOX1 gene. 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. 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. Cayman’s HO-1 protein can be used for ELISA and Western blot (WB) applications.

[1] JINLING WANG. Regiospecificity determinants of human heme oxygenase: differential NADPH- and ascorbate-dependent heme cleavage by the R183E mutant.[J]. The Journal of Biological Chemistry, 2005, 280 4: 2797-2806. DOI: 10.1074/jbc.m411229200
[2] PAVEL MARTASEK. Properties of human kidney heme oxygenase: Inhibition by synthetic heme analogues and metalloporphyrins[J]. Biochemical and biophysical research communications, 1988, 157 2: Pages 480-487. DOI: 10.1016/s0006-291x(88)80274-2
[3] WARREN J HUBER. Measurement of membrane-bound human heme oxygenase-1 activity using a chemically defined assay system.[J]. Drug Metabolism and Disposition, 2009, 37 1: 857-864. DOI: 10.1124/dmd.108.025023
[4] PASCAL O BERBERAT. Inhibition of heme oxygenase-1 increases responsiveness of pancreatic cancer cells to anticancer treatment.[J]. Clinical Cancer Research, 2005, 11 10: 3790-3798. DOI: 10.1158/1078-0432.ccr-04-2159
[5] D NOWIS. Heme oxygenase-1 protects tumor cells against photodynamic therapy-mediated cytotoxicity[J]. Oncogene, 2006, 25 24: 3365-3374. DOI: 10.1038/sj.onc.1209378
[6] J. FANG  H. M  T Akaike. Antiapoptotic role of heme oxygenase (HO) and the potential of HO as a target in anticancer treatment[J]. Apoptosis, 2004, 9 1: 27-35. DOI: 10.1023/b:appt.0000012119.83734.4e
[7] DAVID E. GORDON. A SARS-CoV-2 protein interaction map reveals targets for drug repurposing[J]. Nature, 2020, 583 7816: 459-468. DOI: 10.1038/s41586-020-2286-9
[8] HENG LI . Coronavirus disease 2019 (COVID-19): current status and future perspectives[J]. International Journal of Antimicrobial Agents, 2020, 55 5: Article 105951. DOI: 10.1016/j.ijantimicag.2020.105951
[9] KAM-LEUNG SIU. Severe acute respiratory syndrome Coronavirus ORF3a protein activates the NLRP3 inflammasome by promoting TRAF3-dependent ubiquitination of ASC[J]. FASEB Journal, 2019, 33 8: 8865-8877. DOI: 10.1096/fj.201802418r