Recombinant Human Heme oxygenase 2 (HMOX2)

Code CSB-YP010584HU
MSDS
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Source Yeast
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Code CSB-EP010584HU
MSDS
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Source E.coli
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Code CSB-EP010584HU-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP010584HU
MSDS
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Source Baculovirus
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Code CSB-MP010584HU
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
HMOX2
Uniprot No.
Alternative Names
Heme oxygenase (decycling) 2; Heme oxygenase (decyclizing) 2; Heme oxygenase 2; HMOX 2; Hmox2; HMOX2 protein; HMOX2_HUMAN; HO 2; HO-2; HO2; OTTHUMP00000159847
Species
Homo sapiens (Human)
Expression Region
2-316
Target Protein Sequence
SAEVETSEG VDESEKKNSG ALEKENQMRM ADLSELLKEG TKEAHDRAEN TQFVKDFLKG NIKKELFKLA TTALYFTYSA LEEEMERNKD HPAFAPLYFP MELHRKEALT KDMEYFFGEN WEEQVQCPKA AQKYVERIHY IGQNEPELLV AHAYTRYMGD LSGGQVLKKV AQRALKLPST GEGTQFYLFE NVDNAQQFKQ LYRARMNALD LNMKTKERIV EEANKAFEYN MQIFNELDQA GSTLARETLE DGFPVHDGKG DMRKCPFYAA EQDKGALEGS SCPFRTAMAV LRKPSLQFIL AAGVALAAGL LAWYYM
Protein Length
Full Length of Mature Protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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Target Background

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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