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Recombinant Mouse Heme oxygenase 1(Hmox1)

Recombinant Mouse Heme oxygenase 1(Hmox1)

Hersteller	Cusabio
Kategorie	Oncology Neuroscience Molecular Targets for Neuroscience Peptides & Proteins Recombinant Proteins By Organ Heart & Blood Cancer
Typ	Proteins Recombinant
Specific against	other
Format	Liquid or Lyophilized powder
Menge	500ug
ArtNr	CSB-EP010583MO-500
eClass 6.1	34160400
eClass 9.0	42020190
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Research Topic	Cell Biology
Uniprot ID	P14901
Gene Names	Hmox1
Organism	Mus musculus (Mouse)
AA Sequence	MERPQPDSMPQDLSEALKEATKEVHIQAENAEFMK NFQKGQVSREGFKLVMASLYHIYTALEEEIERNKQ NPVYAPLYFPEELHRRAALEQDMAFWYGPHWQEII PCTPATQHYVKRLHEVGRTHPELLVAHAYTRYLGD LSGGQVLKKIAQKAMALPSSGEGLAFFTFPNIDSP TKFKQLYRARMNTLEMTPEVKHRVTEEAKTAFLLN IELFEELQVMLTEEHKDQSPSQMASLRQRPASLVQ DTAPAETPRGKPQISTSSSQTPLLQWVLTLSFLLA TVAVGIYAM
Expression Region	1-289aa
Sequence Info	Full Length
Source	E.coli
Tag Info	N-terminal 6xHis-B2M-tagged
MW	46.9 kDa
Alternative Name(s)	P32 protein
Relevance	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.
Reference	"Isolation and characterization of a complementary DNA clone for a Mr 32, 000 protein which is induced with tumor promoters in BALB/c 3T3 cells." Kageyama H., Hiwasa T., Tokunaga K., Sakiyama S. Cancer Res. 48:4795-4798(1988)
Purity	Greater than 85% as determined by SDS-PAGE.
Storage Buffer	Tris-based buffer, 50% glycerol
Storage	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 -20C/-80C. The shelf life of lyophilized form is 12 months at -20C/-80C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4C for up to one week.
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.
Subcellular Location	Microsome, Endoplasmic reticulum membrane, Peripheral membrane protein, Cytoplasmic side
Protein Families	Heme oxygenase family
Tag Information	N-terminal 6xHis-B2M-tagged

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