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Mouse Anti-HMOX1 (AA 1-266) Recombinant Antibody (CBFYH-1567) (CBMAB-H2552-FY)

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Summary

Host Animal
Mouse
Specificity
Human
Clone
CBFYH-1567
Antibody Isotype
IgG2a, κ
Application
WB, FC, ELISA, IF

Basic Information

Immunogen
Recombinant human Heme oxygenase 1 purified from E. coli
Specificity
Human
Antibody Isotype
IgG2a, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Concentration
1 mg/mL
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
AA 1-266

Target

Full Name
Heme Oxygenase 1
Introduction
Heme oxygenase, an essential enzyme in heme catabolism, cleaves heme to form biliverdin, which is subsequently converted to bilirubin by biliverdin reductase, and carbon monoxide, a putative neurotransmitter. Heme oxygenase activity is induced by its substrate heme and by various nonheme substances. Heme oxygenase occurs as 2 isozymes, an inducible heme oxygenase-1 and a constitutive heme oxygenase-2. HMOX1 and HMOX2 belong to the heme oxygenase family.
Entrez Gene ID
UniProt ID
Alternative Names
Heme Oxygenase 1; Heme Oxygenase (Decycling) 1; HO-1; Heat Shock Protein, 32-KD; EC 1.14.14.18; EC 1.14.99.
Function
Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis.
Biological Process
Angiogenesis Source: BHF-UCL
Cell death Source: BHF-UCL
Cellular iron ion homeostasis Source: CACAO
Cellular response to arsenic-containing substance Source: Ensembl
Cellular response to cadmium ion Source: Ensembl
Cellular response to cisplatin Source: Ensembl
Cellular response to heat Source: UniProtKB
Cellular response to hypoxia Source: UniProtKB
Cellular response to nutrient Source: Ensembl
Endothelial cell proliferation Source: BHF-UCL
Erythrocyte homeostasis Source: BHF-UCL
Excretion Source: BHF-UCL
Heme catabolic process Source: BHF-UCL
Heme oxidation Source: BHF-UCL
Intracellular signal transduction Source: BHF-UCL
Intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl
Iron ion homeostasis Source: BHF-UCL
Liver regeneration Source: Ensembl
Low-density lipoprotein particle clearance Source: BHF-UCL
Negative regulation of DNA binding Source: Ensembl
Negative regulation of DNA-binding transcription factor activity Source: Ensembl
Negative regulation of epithelial cell apoptotic process Source: Ensembl
Negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
Negative regulation of leukocyte migration Source: BHF-UCL
Negative regulation of macroautophagy Source: Ensembl
Negative regulation of mast cell cytokine production Source: Ensembl
Negative regulation of mast cell degranulation Source: Ensembl
Negative regulation of muscle cell apoptotic process Source: Ensembl
Negative regulation of neuron apoptotic process Source: Ensembl
Negative regulation of smooth muscle cell proliferation Source: UniProtKB
Negative regulation of vascular associated smooth muscle cell proliferation Source: Ensembl
Positive regulation of angiogenesis Source: BHF-UCL
Positive regulation of apoptotic process Source: Ensembl
Positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis Source: BHF-UCL
Positive regulation of cell migration involved in sprouting angiogenesis Source: BHF-UCL
Positive regulation of chemokine production Source: BHF-UCL
Positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
Positive regulation of macroautophagy Source: Ensembl
Positive regulation of smooth muscle cell proliferation Source: UniProtKB
Regulation of angiogenesis Source: BHF-UCL
Regulation of blood pressure Source: Ensembl
Regulation of DNA-binding transcription factor activity Source: BHF-UCL
Regulation of transcription from RNA polymerase II promoter in response to iron Source: Ensembl
Regulation of transcription from RNA polymerase II promoter in response to oxidative stress Source: BHF-UCL
Response to estrogen Source: Ensembl
Response to hydrogen peroxide Source: BHF-UCL
Response to nicotine Source: BHF-UCL
Response to oxidative stress Source: BHF-UCL
Response to xenobiotic stimulus Source: Ensembl
Small GTPase mediated signal transduction Source: Ensembl
Smooth muscle hyperplasia Source: BHF-UCL
Wound healing involved in inflammatory response Source: BHF-UCL
Cellular Location
Microsome; Endoplasmic reticulum membrane
Involvement in disease
Heme oxygenase 1 deficiency (HMOX1D):
A disease characterized by impaired stress hematopoiesis, resulting in marked erythrocyte fragmentation and intravascular hemolysis, coagulation abnormalities, endothelial damage, and iron deposition in renal and hepatic tissues. Clinical features include persistent hemolytic anemia, asplenia, nephritis, generalized erythematous rash, growth retardation and hepatomegaly.
More Infomation

Zhang, S., Wang, J., Wang, L., Aliyari, S., & Cheng, G. (2022). SARS-CoV-2 virus NSP14 Impairs NRF2/HMOX1 activation by targeting Sirtuin 1. Cellular & Molecular Immunology, 19(8), 872-882.

Liu, Y., Huang, P., Li, Z., Xu, C., Wang, H., Jia, B., ... & Xu, M. (2022). Vitamin C sensitizes pancreatic cancer cells to erastin-induced ferroptosis by activating the AMPK/Nrf2/HMOX1 pathway. Oxidative Medicine and Cellular Longevity, 2022.

Yang, C., Wang, T., Zhao, Y., Meng, X., Ding, W., Wang, Q., ... & Deng, H. (2022). Flavonoid 4, 4′-dimethoxychalcone induced ferroptosis in cancer cells by synergistically activating Keap1/Nrf2/HMOX1 pathway and inhibiting FECH. Free Radical Biology and Medicine, 188, 14-23.

Lin, H., Chen, X., Zhang, C., Yang, T., Deng, Z., Song, Y., ... & Jin, D. (2021). EF24 induces ferroptosis in osteosarcoma cells through HMOX1. Biomedicine & Pharmacotherapy, 136, 111202.

Meng, Z., Liang, H., Zhao, J., Gao, J., Liu, C., Ma, X., ... & Wang, Y. (2021). HMOX1 upregulation promotes ferroptosis in diabetic atherosclerosis. Life Sciences, 284, 119935.

Dunn, L. L., Kong, S. M., Tumanov, S., Chen, W., Cantley, J., Ayer, A., ... & Stocker, R. (2021). Hmox1 (Heme Oxygenase-1) protects against ischemia-mediated injury via stabilization of HIF-1α (Hypoxia-Inducible Factor-1α). Arteriosclerosis, thrombosis, and vascular biology, 41(1), 317-330.

Zhu, H., Klement, J. D., Lu, C., Redd, P. S., Yang, D., Smith, A. D., ... & Liu, K. (2021). Asah2 represses the p53–Hmox1 axis to protect myeloid-derived suppressor cells from ferroptosis. The Journal of Immunology, 206(6), 1395-1404.

Batra, N., De Souza, C., Batra, J., Raetz, A. G., & Yu, A. M. (2020). The HMOX1 Pathway as a Promising Target for the Treatment and Prevention of SARS-CoV-2 of 2019 (COVID-19). International journal of molecular sciences, 21(17), 6412.

Sun, J., Yu, X., Huangpu, H., & Yao, F. (2019). Ginsenoside Rb3 protects cardiomyocytes against hypoxia/reoxygenation injury via activating the antioxidation signaling pathway of PERK/Nrf2/HMOX1. Biomedicine & pharmacotherapy, 109, 254-261.

Meyer, N., Zielke, S., Michaelis, J. B., Linder, B., Warnsmann, V., Rakel, S., ... & Kögel, D. (2018). AT 101 induces early mitochondrial dysfunction and HMOX1 (heme oxygenase 1) to trigger mitophagic cell death in glioma cells. Autophagy, 14(10), 1693-1709.

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For research use only. Not intended for any clinical use.

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