protein

HMOX2, 1-264aa, Human, E Coli

MBS203726

0.1 mg

285 USD

Recombinant Protein

HMOX2, 1-264aa, Human, E Coli

HMOX2

Heme oxygenase 2 Heme oxygenase (decycling) 2; Heme oxygenase (decyclizing) 2; HMOX 2; HMOX2 protein; HO 2; HO2

heme oxygenase 2 isoform b; Heme oxygenase 2; heme oxygenase 2; heme oxygenase (decycling) 2

HMOX2

HMOX2; HMOX2; HO-2; HO2; HO-2

HMOX2_HUMAN

316

MSAEVETSEG 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 DMRK

> 90% by SDS-PAGE

Liquid. In 20mM Tris buffer(pH 8.0) containing 10% glycerol 1mM DTT.

1 mg/ml (determined by Bradford assay)

Can be stored at 4 degree C short term (1-2 weeks). For long term storage, aliquot and store at -20 degree C or -70 degree C. Avoid repeated freezing and thawing cycles.

SDS-PAGE

Antigen Species: Human

Expression System: E Coli

Redox Proteins

HMOX2 is microsomal enzyme that cleave heme ring at the alpha methane bridge to produce the antioxidant biliverdin, inorganic iron and carbon monoxide. Biliverdin is subsequently converted to bilirubin by bilibverdin reductase. This protein appears to be constitutively expressed in mammalian tissues. HMOX2 is involved in the production of carbon monoxide (CO) in brain, where CO is thought to act as a neurotransmitter. Recombinant HMOX2 protein was expressed in E.coli and purified by using conventional chromatography techniques.

Baranano DE., et al. (2001) Proc Natl Acad Sci u S A. 98(20):10996-1002. Dore S., et al. (2002) Free Radic Biol Med. 32(12):1276-82.

8051608

NP_002125

NM_002134.3

30.5 kDa (264aa), confirmed by MALDI-TOF.

Heme Degradation Pathway (160971); Iron Uptake And Transport Pathway (187191); Metabolism Pathway (477135); Metabolism Of Porphyrins Pathway (106325); Mineral Absorption Pathway (212237); Mineral Absorption Pathway (212220); Porphyrin And Chlorophyll Metabolism Pathway (83021); Porphyrin And Chlorophyll Metabolism Pathway (407); Transmembrane Transport Of Small Molecules Pathway (106572); Heme Degradation Pathway (545346)

Heme oxygenase, an essential enzyme in heme catabolism, cleaves heme to form biliverdin, which is subsequently converted to bilirubin by biliverdin reductase, and carbon monoxide, a putative neurotransmitter. Heme oxygenase activity is induced by its substrate heme and by various nonheme substances. Heme oxygenase occurs as 2 isozymes, an inducible heme oxygenase-1 and a constitutive heme oxygenase-2. HMOX1 and HMOX2 belong to the heme oxygenase family. Several alternatively spliced transcript variants encoding three different isoforms have been found for this gene. [provided by RefSeq, Oct 2013]

HMOX2: 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. Belongs to the heme oxygenase family. Protein type: EC 1.14.99.3; Cofactor and Vitamin Metabolism - porphyrin and chlorophyll; Oxidoreductase. Chromosomal Location of Human Ortholog: 16p13.3. Cellular Component: endoplasmic reticulum membrane; membrane; plasma membrane. Molecular Function: protein binding; metal ion binding; heme oxygenase (decyclizing) activity. Biological Process: cellular iron ion homeostasis; heme catabolic process; porphyrin metabolic process; response to hypoxia; heme oxidation; transmembrane transport

0.1 mg

285 USD

0.5 mg

640