protein

Heme oxygenase1,1-266aa, Human, His-tag, Recombinant, E Coli

MBS203285

0.1 mg

255 USD

Recombinant Protein

Heme oxygenase1,1-266aa, Human, His-tag, Recombinant, E Coli

Heme oxygenase1

HO-1; Heat shock protein 32; HSP32; bK286B10; D8Wsu38e; Heme oxygenase (decycling) 1; Heme oxygenase 1; Hemox; Hmox; HMOX 1; HMOX1; HO; HO 1; HO1.

heme oxygenase 1; Heme oxygenase 1; heme oxygenase 1; heat shock protein, 32-kD; heme oxygenase (decycling) 1

HMOX1; HMOX1; HO-1; HSP32; HMOX1D; bK286B10; HO; HO1; HO-1

HMOX1_HUMAN

288

MERPQPHSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALE QDLAFWYGPR WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NIASATKFKQ LYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV ETPRGKPPLN TRSQAPLEHH HHHH

> 95% by SDS - PAGE

Liquid. In 20 mM Tris-HCl buffer (pH 8.0) containing 50mM NaCl, 0.1mM PMSF, 10% glycerol

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. Tag: His-tag

Expression System: E Coli. Endotoxin: < 1.0 Eu per 1 microgram of protein (determined by LAL method)

Redox Proteins

Heme oxygenase 1 belongs to the heme oxygenase family and is an essential enzyme in heme catabolism. It cleaves heme to form biliverdin, which is subsequently converted to bilirubin by biliverdin reductase, and carbon monoxide, a putative neurotransmitter. Also this protein is known to play an important role in the regulation of cardiovascular function and its adaptive response to a variety of stressors. Recombinant human Heme oxygenase 1 protein, fused to His-tag at C-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.

Vareille M., et al. (2008). J Immunol. 180(8):5720-6. Soares MP., et al. (2001). Immunol Rev.184:275-85.

4504437

NP_002124

NM_002133.2

31.4 kDa (274 aa), confirmed by MALDI-TOF.

HIF-1 Signaling Pathway (695200); HIF-1-alpha Transcription Factor Network Pathway (138045); Heme Degradation Pathway (160971); Iron Uptake And Transport Pathway (187191); Keap1-Nrf2 Pathway (198777); Metabolism Pathway (477135); Metabolism Of Porphyrins Pathway (106325); MicroRNAs In Cancer Pathway (852705); MicroRNAs In Cancer Pathway (852928); Mineral Absorption Pathway (212237)

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. [provided by RefSeq, Jul 2008]

HMOX1: 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 1 activity is highly inducible by its substrate heme and by various non-heme substances such as heavy metals, bromobenzene, endotoxin, oxidizing agents and UVA. Expressed at higher levels in renal cancer tissue than in normal tissue. Belongs to the heme oxygenase family. Protein type: EC 1.14.99.3; Oxidoreductase; Cofactor and Vitamin Metabolism - porphyrin and chlorophyll. Chromosomal Location of Human Ortholog: 22q13.1. Cellular Component: extracellular space; endoplasmic reticulum membrane; membrane; perinuclear region of cytoplasm; endoplasmic reticulum; nucleolus; caveola; nucleus; cytosol. Molecular Function: signal transducer activity; protein binding; protein homodimerization activity; enzyme binding; metal ion binding; phospholipase D activity; heme binding; heme oxygenase (decyclizing) activity. Biological Process: cell death; response to nicotine; negative regulation of smooth muscle cell proliferation; cellular iron ion homeostasis; positive regulation of smooth muscle cell proliferation; negative regulation of mast cell degranulation; excretion; positive regulation of vasodilation; erythrocyte homeostasis; regulation of transcription factor activity; heme catabolic process; regulation of blood pressure; small GTPase mediated signal transduction; porphyrin metabolic process; negative regulation of mast cell cytokine production; angiogenesis; negative regulation of neuron apoptosis; regulation of transcription from RNA polymerase II promoter in response to oxidative stress; transmembrane transport; healing during inflammatory response; protein homooligomerization; positive regulation of I-kappaB kinase/NF-kappaB cascade; negative regulation of transcription factor activity; heme oxidation; cellular response to nutrient; negative regulation of leukocyte migration; regulation of angiogenesis; negative regulation of DNA binding; positive regulation of angiogenesis; iron ion homeostasis; positive regulation of chemokine biosynthetic process; DNA damage response, signal transduction resulting in induction of apoptosis; response to hydrogen peroxide; response to estrogen stimulus; endothelial cell proliferation; response to oxidative stress; smooth muscle hyperplasia. Disease: Heme Oxygenase 1 Deficiency; Pulmonary Disease, Chronic Obstructive

0.1 mg

255 USD

0.5 mg

535