Pig HMOX1 ELISA Kit (V2LY-0626-LY972)

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Tested Data
Request for COA
Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Sensitivity
0.152 ng/mL
Detection Range
0.3-90 ng/mL
Sample Type
Serum, Plasma, cell culture supernates
Specificity
Pig
Assay Type
Sandwich
Reactivity
Pig
Assay Time
1.5 h
Molecule Mass
33.1 kDa
Components
  • Pre-coated ELISA Plate: 12 wells * 8 detachable strips
  • Standard solution: 0.5ml x1
  • Standard diluent: 3ml x1
  • Streptavidin-HRP: 6ml x1
  • Stop solution: 6ml x1
  • Substrate solution A: 6ml x1
  • Substrate solution B: 6ml x1
  • Wash buffer concentrate (25x): 20ml x1
  • Biotinylated antibody: 1ml x1

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

Storage
Store at 2-8°C
More Infomation

Target

Full Name
Heme Oxygenase 1
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.

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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