Recombinant Rat Heme oxygenase 2 (Hmox2)

Code CSB-YP010584RA
MSDS
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Source Yeast
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Code CSB-EP010584RA
MSDS
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Source E.coli
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Code CSB-EP010584RA-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-BP010584RA
MSDS
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Source Baculovirus
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Code CSB-MP010584RA
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
Hmox2Heme oxygenase 2; HO-2; EC 1.14.14.18
Species
Rattus norvegicus (Rat)
Expression Region
2-315
Target Protein Sequence
SSEVETSEG VDESENNSTA PEKENHTKMA DLSELLKEGT KEAHDRAENT QFVKDFLKGN IKKELFKLAT TALYFTYSAL EEEMDRNKDH PAFAPLYFPT ELHRKEALIK DMEYFFGENW EEQVKCSEAA QKYVDRIHYV GQNEPELLVA HAYTRYMGDL SGGQVLKKVA QRALKLPSTG EGTQFYLFEH VDNAQQFKQF YRARMNALDL SMKTKERIVE EANKAFEYNM QIFSELDQAG SMLTKETLED GLPVHDGKGD VRKCPFYAAQ PDKGTLGGSN CPFRTAMAVL RKPSLQLILA ASVALVAGLL AWYYM
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.

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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. Aorta HO-2 histological scores (HSCORE) of hypertensive rats were lower, while SBP was higher. Swimming caused enhancement of HO-2 immunostaining in aorta endothelium and adventitia of SHR. Exercise induced elevation of blood COHb index in SHR. Synchronous BP lowering effect of exercise was observed. PMID: 30132448
  2. This experiments shown here indicate that HO-2 and HO-1 are differentially regulated across sexual experience and that the two CO-producing enzymes are expressed in distinct but overlapping populations of cells in medial preoptic area. PMID: 28088559
  3. The increased HO activity and expression in females might play a role in the sexual dimorphism of cardiovascular ischemia susceptibility during the reproductive age. PMID: 24163720
  4. The distribution of neurons expressing heme oxygenase-2 (HO-2-positive neurons) in the nuclei of various parts of the brainstem was determined. PMID: 23659033
  5. HO mRNA levels display isoform-specific changes: those of HO-2 do not change appreciably, whereas those of HO-1 increase significantly in 2-h endotoxemia, with or without obstructive jaundice. PMID: 22100509
  6. Heme oxyenase-1 and -2 in the nephron inhibit tubuloglomerular feedback by releasing CO and biliverdin. CO's inhibitory effect is mediated by the soluble-guanylate-cyclase/cGMP signaling pathway, whereas biliverdin probably acts by reducing O2-. PMID: 21239629
  7. Data show that siRNA blockage of BVR protein expression in cardiomyocytes inhibits HO-2 protein induction but not vice versa. PMID: 20876213
  8. The expression and distribution of NADPH-d and HO-2 suggest that carbon monoxide and nitric oxide are likely neurotransmitters and might function in the processing orofacial signal in the spinal trigeminal nucleus together. PMID: 19821077
  9. HO-2 play a major role by sequestering NO derived radical and suppressing inflammatory response. PMID: 11950143
  10. Exposure to diesel exhaust particles elevated transcription of heme oxygenase-2 gene in rat alveolar macrophages PMID: 12011483
  11. In the uterus, HO-1 and HO-2 protein and total mRNA levels peaked on d 16 of pregnancy, whereas, in the placenta, HO-1 and HO-2 protein levels peaked on d 19 PMID: 12736392
  12. high-potassium intake increases HO-2 expression in the kidney and that HO-dependent metabolites of heme, presumably CO, play a significant role in the regulation of Na+ transport in the loop of Henle PMID: 12890663
  13. demonstrated an interaction between Hmox1 and Hmox2 at amino acids 0-45 of Hmox2 and amino acids 58-80 of Hmox1, corresponding to a highly conserved, hydrophilic, and exposed region of the protein PMID: 14514669
  14. Ho-2 level increased in cardiac myocytes one-month after diabetes mellitus. PMID: 14654370
  15. Spinal cord injury has the capacity to induce upregulation of HO-2. Endogenous serotonin is involved in HO-2 expression in spinal cord. PMID: 14753474
  16. Calmodulin binds to HO2 in a calcium-dependent manner via a canonical 1-10 motif, resulting in a 3-fold increase in catalytic activity. Mutations within this motif block calmodulin binding and calcium-dependent stimulation of enzyme activity. PMID: 15175337
  17. HO-2 is expressed by aortic endothelial cells early during hypoxic exposure and impairs ET-1-mediated potentiation of contraction to alpha-adrenoceptor stimulation. PMID: 15486027
  18. carotid body cells demonstrated HO-2-dependent hypoxic BK channel inhibition, which indicates that HO-2 is an oxygen sensor that controls channel activity during oxygen deprivation PMID: 15528406
  19. Moreover, our results showed that the combination of 2.5mg/kg of venlafaxine and 5mg/kg of quetiapine effectively prevented the HO-2 protein decrease in hippocampal neurons of stressed rats. PMID: 16115734
  20. Highly present in wildtype animals. Under modification of estrogen levels (naturally occurring, with age, or surgically) and estrogen replacement HO-1 was barely detectable, while HO-2 was consistently stably expressed at high levels. PMID: 16181109
  21. Uterine HO activity could regulate uterine quiescence in pregnancy via cGMP and it may contribute to the defense against oxidative stress. PMID: 16524721
  22. subcellular location of HO-2 is consistent with the RME hypothesis for heme uptake and suggests a role in heme degradation. PMID: 17614955
  23. NADPH-diaphorase and HO-2 positive neurons appeared the same pattern PMID: 18626777
  24. Elevations of vascular eNOS and HO-1/HO-2 may contribute to enhanced vasodilation, which can be offset by intense training and elevation in vascular iNOS. PMID: 18633193
  25. Heme oxygenase-2 is necessary for the excitatory response of cultured neonatal rat rostral ventrolateral medulla neurons to hypoxia. PMID: 18971354
  26. HO-1 and HO-2 are expressed in the vaginal smooth muscle of the female rats, and their decreased expressions are correlated with the lowered level of plasma estradiol. PMID: 19323368
  27. At least one HO product (presumably carbon monoxide) inhibits cholesterol transport to the inner mitochondrial membrane and Leydig cell steroidogenesis by binding to the heme group of the cytochrome P450 enzymes. PMID: 19648213
  28. HO-2 protein expression upregulation following hypoxia-ischemia coupled with an increase in HO-1 immunoreactivity suggests that this response may be implicated in reducing cell death or repairing damage induced by cerebral ischemia PMID: 19682508

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Subcellular Location
Microsome. Endoplasmic reticulum.
Protein Families
Heme oxygenase family
Tissue Specificity
Widely distributed in body with a high concentration in the brain.
Database Links
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