You Searched For: heme

Catalog Number: (BOSSBS-2075R-A680)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl

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Catalog Number: (APOSBITP1611-1MG)

Supplier: Apollo Scientific

Description: Human recombinant myoglobin (heme free)

UOM: 1 * 1 mg

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Catalog Number: (BOSSBS-2075R-A750)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl

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Catalog Number: (CAYM700543-1)

Supplier: Cayman Chemical

Description: Ready for use with colorimetric assay kit. This vial contains solution of 500 µM heme.

UOM: 1 * 1 mL

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Catalog Number: (BOSSBS-2075R-CY3)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-1238R-CY3)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-2075R-A555)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-2075R-A647)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-2075R-A488)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-2075R-FITC)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl

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Catalog Number: (ENZOBMLHP93010100)

Supplier: ENZO LIFE SCIENCES

Description: Synthetic peptide corresponding to amino acid residues [12-25] + Cys-NH2 of human heme oxygenase-1.

UOM: 1 * 100 µG

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Supplier: ENZO LIFE SCIENCES

Description: Heme Oxygenase-1 (HO-1) also known as Hsp32, is the inducible isoform of Heme oxygenase that catalyzes the NADPH, oxygen, and cytochrome P450 reductase dependent oxidation of Heme to carbon monoxide, ferrous iron and biliverdin which is rapidly reduced to bilirubin. These products of the HO reaction have important physiological effects: carbon monoxide is a potent vasodilator and has been implicated to be a physiological regulator of cGMP and vascular tone; 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 transferring 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, three identified Heme oxygenase isoforms are part of the HO system that catalyze Heme into biliverdin and carbon monoxide. These are inducible HO-1 or Hsp32, constitutive HO-2 that is abundant in the brain and testis, and HO-3 which is related to HO-2 but is the product of a different gene. The HO system is the rate-limiting step in Heme degradation and HO activity decreases the levels of Heme which is a well known potent catalyst of lipid peroxidation and oxygen radical formation.

New Product

Catalog Number: (USBIH1847-69E-200)

Supplier: US Biological

Description: Anti-Heme Oxygenase 1 Mouse Monoclonal Antibody (Biotin) [clone: 4E136]

UOM: 1 * 200 µG

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Supplier: ENZO LIFE SCIENCES

Description: Heme Oxygenase-1 (HO-1) also known as Hsp32, is the inducible isoform of Heme oxygenase that catalyzes the NADPH, oxygen, and cytochrome P450 reductase dependent oxidation of Heme to carbon monoxide, ferrous iron and biliverdin which is rapidly reduced to bilirubin. These products of the HO reaction have important physiological effects: carbon monoxide is a potent vasodilator and has been implicated to be a physiological regulator of cGMP and vascular tone; 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 transferring 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, three identified Heme oxygenase isoforms are part of the HO system that catalyze Heme into biliverdin and carbon monoxide. These are inducible HO-1 or Hsp32, constitutive HO-2 that is abundant in the brain and testis, and HO-3 which is related to HO-2 but is the product of a different gene. The HO system is the rate-limiting step in Heme degradation and HO activity decreases the levels of Heme which is a well known potent catalyst of lipid peroxidation and oxygen radical formation.

New Product

Catalog Number: (BOSSBS-2075R-CY5)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl

Sale

Catalog Number: (BOSSBS-1238R-A488)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl

Sale