HMOX2 Antibody

Code CSB-PA010584HA01HU
Size US$299
  • Immunofluorescence staining of Hela cells with CSB-PA010584HA01HU at 1:100, counter-stained with DAPI. The cells were fixed in 4% formaldehyde, permeabilized using 0.2% Triton X-100 and blocked in 10% normal Goat Serum. The cells were then incubated with the antibody overnight at 4°C. The secondary antibody was Alexa Fluor 488-congugated AffiniPure Goat Anti-Rabbit IgG(H+L).
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Product Details

Full Product Name Rabbit anti-Homo sapiens (Human) HMOX2 Polyclonal antibody
Uniprot No. P30519
Target Names HMOX2
Alternative Names Heme oxygenase (decycling) 2 antibody; Heme oxygenase (decyclizing) 2 antibody; Heme oxygenase 2 antibody; HMOX 2 antibody; Hmox2 antibody; HMOX2 protein antibody; HMOX2_HUMAN antibody; HO 2 antibody; HO-2 antibody; HO2 antibody; OTTHUMP00000159847 antibody
Raised in Rabbit
Species Reactivity Human
Immunogen Recombinant Human Heme oxygenase 2 protein (2-293AA)
Immunogen Species Homo sapiens (Human)
Conjugate Non-conjugated
Clonality Polyclonal
Isotype IgG
Purification Method >95%, Protein G purified
Concentration It differs from different batches. Please contact us to confirm it.
Buffer Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form Liquid
Tested Applications ELISA, IF
Recommended Dilution
Application Recommended Dilution
IF 1:50-1:200
Protocols ELISA Protocol
Immunofluorescence (IF) Protocol
Troubleshooting and FAQs Antibody FAQs
Storage Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

Target Data

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. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter.
Gene References into Functions
  1. The frequencies of genotype and allelic variants of ALAD rs1800435 did not differ significantly between patients with essential tremor (ET) and controls, and were not influenced by gender. Subjects carrying the ALAD rs1800435CC genotype (wild-type) and the HMOX2 rs1051308GG genotype or the HMOX2 rs1051308G allele had significantly decreased risk for ET. PMID: 28276576
  2. HO-2 is a cellular myristate-binding protein that negatively regulates both virus replication and host inflammatory responses. PMID: 28132836
  3. Our results suggest that rs1051308 is associated with risk of developing Parkinson disease in Han Chinese, and further studies involving various ethnicities are needed to validate the association. PMID: 28179208
  4. High HMOX2 expression is associated with bladder cancer. PMID: 28320388
  5. HMOX2 contributes to high-altitude adaptation in Tibetans by functioning as a modifier in the regulation of hemoglobin metabolism. PMID: 26781569
  6. a weak association between HMOX2 rs1051308 polymorphisms and the risk to develop essential tremor in the Spanish population. PMID: 26091465
  7. Taken together with EPR measurements, which show the appearance of a new low-spin heme signal in reduced HO2, it appears that a cysteine residue(s) in the HRMs directly interacts with a second bound heme PMID: 25849895
  8. HO-2 protein is expressed in the cytosols of skin cancer cells. PMID: 25864768
  9. Interactions of HO-2 with CPR and BVR, were evaluated. PMID: 25196843
  10. increased expression of nucleated RBC, HSP90alpha and corresponding decreased expression of HO-2 in such hypoxic condition may play a protective role; to prevent cord blood RBC against stress induced damage during preeclampsia. PMID: 22935040
  11. PFKFB4 and HO-2 are expressed in a coordinated manner to maintain glucose homeostasis. PMID: 22892400
  12. Role of cysteine residues in heme binding to human heme oxygenase-2 elucidated by two-dimensional NMR spectroscopy. PMID: 22923613
  13. Although the carboxy-terminal deletion mutant of HO-2 is found in the nucleus, translocation of HO-2 to the nucleus does not occur under conditions of hypoxia. PMID: 22545110
  14. for the first time, copy number variations in the HMOX2 gene and an association of the SNP rs2270363 with Parkinson's disease risk. PMID: 21709601
  15. Results suggest that the c.544G>A polymorphism of the heme oxygenase-2 gene is not associated with age-related macular degeneration in this population. PMID: 21804464
  16. HO-2, which is highly expressed in the corneal epithelium, appears to be critical for the wound healing process in the cornea. PMID: 21506105
  17. These findings are consistent with the presence of a hydrogen-bonding network at the heme's distal side within the active site of HO-2 with potentially significant differences from that observed in HO-1. PMID: 20502928
  18. There was positive correlation between seminal plasma HO enzyme activity and sperm concentration, per cent of motile spermatozoa, number of motile spermatozoas ml(-1) and significant negative correlation with per cent of sperm abnormal forms. PMID: 20629646
  19. high expression in keratinocytes prevents basal and radiation-induced gene expression of heme oxygenase 1 PMID: 19874887
  20. HO-2 is important in maintaining endothelial viability and may preserve local regulation of vascular tone, thrombosis, and inflammatory responses during reductions in systemic oxygen delivery PMID: 20118244
  21. HO-2 protein content was decreased by 17% and 5% in human trophoblast cells after 24-h exposure to 1% and 5% O(2), respectively, versus 20% O(2) but unchanged in chorionic villi PMID: 12578814
  22. Low expression of HO-2 may lead to enhanced levels of free heme at the feto-maternal interface, with subsequent upregulation of adhesion molecules, allowing enhanced inflammatory cells migration to the feto-maternal interface. PMID: 14506930
  23. HO-2 is part of the BK channel complex and enhances channel activity in normoxia PMID: 15528406
  24. Catalytically inactive mutant, HO-2H45A, overexpressed in HEK293 cell lines was more sensitive to hemin as compared to control. HO-2H45A was also able to protect cells against oxidative stress injury. PMID: 16043027
  25. Review summarizes function of hemoxygenase-2 as an oxygen sensor of native and recombinant large conductance, voltage- and calcium-dependent potassium BK(Ca) channels expressed in carotid body glomus cells. PMID: 16137652
  26. These results suggest that HO-2 may down-regulate the expression of HO-1, thereby directing the co-ordinated expression of HO-1 and HO-2. PMID: 17064313
  27. Suggest membrane potential gradient in small intestine is dependent on carbon monoxide generated by HO-2 in interstital cells of Cajal. PMID: 17510199
  28. the heme regulatory motifs in HO-2 constitute a thiol/disulfide redox switch that regulates the myriad physiological functions of HO-2, including its involvement in the hypoxic response in the carotid body PMID: 17540772
  29. analysis of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2 PMID: 17965015
  30. HO-2 may be important in controlling trophoblast invasion. PMID: 19345412
  31. The thiol/disulfide switch in HO-2 responds to cellular oxidative stress and reductive conditions, representing a paradigm for how heme regulatory motifs can integrate heme homeostasis with carbon monoxide signaling and redox regulation. PMID: 19473966

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Subcellular Location Microsome, Endoplasmic reticulum
Protein Families Heme oxygenase family
Database Links

HGNC: 5014

OMIM: 141251

KEGG: hsa:3163

STRING: 9606.ENSP00000219700

UniGene: Hs.284279

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