Heme Oxygenase 1, Rat Recombinant Protein | Hmox1 recombinant protein

Heme Oxygenase 1, Recombinant, Rat (HO-1, HSP32, Heat Shock Protein 32)

Cat. Num. AAA637500

• Gene Names: Hmox1; Ho1; Heox; Hmox; Ho-1; HEOXG; hsp32
• Applications: Western Blot
• Purity: Highly Purified; 90% (SDS-PAGE)
• Synonyms: Heme Oxygenase 1; Rat; Recombinant; Rat (HO-1; HSP32; Heat Shock Protein 32); Hmox1 recombinant protein

• Host: E Coli
• Purity/Purification: Highly Purified; 90% (SDS-PAGE)
• Form/Format: Supplied as a liquid in Dulbecco's PBS, 0.05mM EDTA, 10% glycerol

• Applicable Applications for Hmox1 recombinant protein: Western Blot (WB)
• Application Notes: Suitable for use in Western Blot, ELISA and Immunohistochemistry.; Dilution: Western Blot (Colormetric): 50ng
• Preparation and Storage: Aliquot to avoid repeated freezing and thawing and store at -70 degree C. Aliquots are stable for 6 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

Related Product Information for Hmox1 recombinant protein

Heme oxygenase is the rate-limiting microsomal enzyme in the heme degradative pathway. Heme oxygenase catalyzes the NADPH, O2 and cytochrome P450 reductase dependent oxidation of heme to form equimolar biliverdin, carbon monoxide, a putative neurotransmitter, and iron. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. These products of the HO reaction have important physiological effects: carbon monoxide is a potent vasodilator; biliverdin and its product bilirubin are potent antioxidants; "free' iron increases oxidative stress and regulates the expression of many mRNAs (e.g., DCT-1, ferritin and transferrin receptor) by affecting the conformation of iron regulatory protein (IRP)-1 and its binding to iron regulatory elements (IREs) in the 5'- or 3'-UTRs of the mRNAs. To date, 3 forms of heme oxygenases (HO1-3) have been identified. HO-1 or Hsp-32 (EC 1.14.99.3; mouse/rat 289 aa; human 288 aa, chromosome 22; ~88% homology between the species) is an inducible enzyme. Ho-1 is expressed in most tissues with highest levels in spleen. HO-1 gene expression is inducible by heme, suggesting an important role of HO-1 in heme metabolism. Many other agents or conditions related to oxidant damage such as longer wavelength UV radiation, hyperoxia, hypoxia, hydrogen peroxide, glutathione depletion, endotoxin, and, more recently, nitric oxide (NO) have also been found to stimulate HO-1 expression. HO-1 expression has been shown to increase in benign prostatic hyperplasia (BPH) and malignant prostate tissue.

Product Categories/Family for Hmox1 recombinant protein

Molecular Biology; MB-Heat Shock Proteins

NCBI and Uniprot Product Information

• NCBI GI #: 6981032
• NCBI GeneID: 24451
• NCBI Accession #: NP_036712.1
• NCBI GenBank Nucleotide #: NM_012580.2
• UniProt Accession #: P06762; Q5BK87
• Molecular Weight: 33,006 Da
• NCBI Official Full Name: heme oxygenase 1
• NCBI Official Synonym Full Names: heme oxygenase (decycling) 1
• NCBI Official Symbol: Hmox1
• NCBI Official Synonym Symbols: Ho1; Heox; Hmox; Ho-1; HEOXG; hsp32
• NCBI Protein Information: heme oxygenase 1; heme oxygenase (decyclizing) 1
• UniProt Protein Name: Heme oxygenase 1
• UniProt Gene Name: Hmox1
• UniProt Synonym Gene Names: HO-1
• UniProt Entry Name: HMOX1_RAT

NCBI Description

catalyzes the oxidative cleavage of heme to biliverdin [RGD, Feb 2006]

Uniprot Description

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

Cellular Component: endoplasmic reticulum membrane; endoplasmic reticulum; perinuclear region of cytoplasm; plasma membrane; nucleolus; caveola; cytosol; nucleus

Molecular Function: protein binding; signal transducer activity; protein homodimerization activity; enzyme binding; metal ion binding; phospholipase D activity; heme binding; oxidoreductase activity; heme oxygenase (decyclizing) activity

Biological Process: response to nicotine; cell death; negative regulation of smooth muscle cell proliferation; negative regulation of mast cell degranulation; positive regulation of smooth muscle cell proliferation; heme metabolic process; erythrocyte homeostasis; negative regulation of cell proliferation; regulation of transcription factor activity; heme catabolic process; small GTPase mediated signal transduction; regulation of blood pressure; phospholipid 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; 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 DNA binding; iron ion homeostasis; positive regulation of angiogenesis; DNA damage response, signal transduction resulting in induction of apoptosis; response to hydrogen peroxide; response to estrogen stimulus; response to hypoxia; response to oxidative stress