protein

Recombinant Mus musculus Heme oxygenase 1

MBS9422322

0.01 mg

230 USD

Recombinant Protein

Recombinant Mus musculus Heme oxygenase 1

[Heme oxygenase 1]

[P32 protein]

[heme oxygenase 1; Heme oxygenase 1; heme oxygenase 1; heme oxygenase 1; P32 protein]

[HMOX1]

[Hmox1; Hmox1; HO1; HO-1; Hmox; Hemox; Hsp32; D8Wsu38e; HO-1]

Yeast

[Full Length, 1-289aa]

Greater than 90% as determined by SDS-PAGE.

20mM Tris-HCl based buffer, pH8.0

Store at -20°C, for extended storage, conserve at -20°C or -80° C. Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Calculated MW: 34.93 kD. Target Species: Mouse

Tag Info: His-tag

He oxygenase cleaves the he ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of he oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free he sensitizes cells to undergo apoptosis.

6754212

NP_034572.1

NM_010442.2

P14901

HIF-1 Signaling Pathway (695223); Heme Degradation Pathway (1367853); Iron Uptake And Transport Pathway (1368042); Keap1-Nrf2 Pathway (198378); Lung Fibrosis Pathway (1458483); Metabolism Pathway (1367614); Metabolism Of Porphyrins Pathway (1367851); Mineral Absorption Pathway (212238); Mineral Absorption Pathway (212220); Oxidative Stress Pathway (198384)

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: Cofactor and Vitamin Metabolism - porphyrin and chlorophyll; EC 1.14.99.3; Oxidoreductase. Chromosomal Location of Human Ortholog: 8 35.59 cM 8 C1. Cellular Component: caveola; cytosol; endoplasmic reticulum; membrane; nucleolus; nucleus; perinuclear region of cytoplasm. Molecular Function: enzyme binding; heme binding; heme oxygenase (decyclizing) activity; phospholipase D activity; protein homodimerization activity; signal transducer activity. Biological Process: angiogenesis; cell death; cellular iron ion homeostasis; DNA damage response, signal transduction resulting in induction of apoptosis; erythrocyte homeostasis; healing during inflammatory response; heme catabolic process; heme metabolic process; heme oxidation; iron ion homeostasis; negative regulation of cell proliferation; negative regulation of DNA binding; negative regulation of macroautophagy; negative regulation of mast cell cytokine production; negative regulation of mast cell degranulation; negative regulation of neuron apoptosis; negative regulation of smooth muscle cell proliferation; negative regulation of transcription factor activity; positive regulation of angiogenesis; positive regulation of apoptosis; positive regulation of I-kappaB kinase/NF-kappaB cascade; positive regulation of macroautophagy; positive regulation of smooth muscle cell proliferation; protein homooligomerization; regulation of blood pressure; regulation of transcription factor activity; regulation of transcription from RNA polymerase II promoter in response to oxidative stress; response to estrogen stimulus; response to hydrogen peroxide; response to hypoxia; response to nicotine; response to oxidative stress; small GTPase mediated signal transduction

0.01 mg

230 USD

0.05 mg

290

0.1 mg

455

0.2 mg

705

0.5 mg

1145

1 mg

1800