Recombinant Pig Heme oxygenase 1 (HMOX1)

Product Details

Purity
>85% (SDS-PAGE)
Target Names
HMOX1
Uniprot NO.
Alternative Names
HMOX1; Heme oxygenase 1; HO-1; EC 1.14.14.18
Species
Sus scrofa (Pig)
Source
Yeast
Expression Region
1-288
Target Protein Sequence
MEHSQPNSMP QDLSEALKEA TKEVHVQAEN AEFMKNFQKG EVTREGFKLV MASLYHIYDA LEEEIEHNKE NPVYTPLYFP EELHRRAALE QDMAFWYGPR WQEAIPYTQA TKRYVRRLQQ VGRFEPELLV AHAYTRYMGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NVANATKFKQ LYRSRMNTLE MTPEVKQRVL EEAKTAFLLN IQLFEEVQEL LTQDTKDQRP SQASDIRKRA GSRVQDSTPV TTPRGKPQLS VLSQVPLIRW VLTLSFLVAT VAMGLYAM
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.
Protein Length
Full length protein
Tag Info
N-terminal His-tagged/Tag-Free
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.
Storage Condition
Store at -20°C, for extended storage, conserve at -20°C or -80°C.
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.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Customer Reviews and Q&A

 Customer Reviews

Target Background

Function(From Uniprot)
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.
Gene References into Functions
  1. These results provide a unique insight into the molecular mechanisms underlying the antiviral effects of the stress-responsive protein HO-1 during Porcine reproductive and respiratory syndrome virus infection. PMID:27908781
  2. findings collectively suggest that miR-506 acts as a tumor suppressor via regulation of ROCK1 expression and may thus be a promising therapeutic target for HCC PMID:26471299
  3. Exogenous administration of CO exacerbated allergic symptoms, resulting in higher levels of both CO and heme oxygenase-1 expression, and a further reduction in H2S levels and CSE expression. PMID:25583855
  4. Down-regulation of HO-1 is associated with pulmonary arterial hypertension and right ventricular failure. PMID:23936023
  5. The study revealed the involvement of HO-1 in classical swine fever virus proliferation. PMID:23357296
  6. The protective properties of flavonoids, such as EGCG, against endothelial inflammation may be regulated in part though induction of HO-1 and subsequent activator protein-1 signaling. PMID:20580034
  7. Glutamate regulates Ca2+ signals in smooth muscle cells of newborn piglet brain slice arterioles through astrocyte- and heme oxygenase-dependent mechanisms. PMID:19966053
  8. obalt protoporphyrin prevents postictal cerebral vascular dysfunction by upregulating HO-1. PMID:15681702
  9. Data demonstrate that lipopolysaccharides evoke a heat shock response, with an increase heat shock proteins 70 and Hsp32) and of VEGF, a specific endothelial cell growth factor. PMID:16333987
  10. Interaction of soluble factors in plasma possibly generated during PICSO are not responsible for upregulation of HO-1 and VEGF mRNA. PMID:19618599

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Subcellular Location
Microsome. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side.
Protein Families
Heme oxygenase family
Database Links

UNIGENE: Ssc.115

KEGG: ssc:445512

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