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HO-1 Protein, Human, Recombinant

(Synonyms: HO-1, HO1, HO, HMOX1, Heme Oxygenase 1) Copy Product Info

Synonyms: HO-1, HO1, HO, HMOX1, Heme Oxygenase 1

Catalog No. TMPJ-00817 Copy Product Info
Heme Oxygenase 1 (HO-1) is an enzyme in endoplasmic reticulum that belongs to the heme oxygenase family. HO-1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is subsequently converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HO-1 is found in the spleen, where senescent erythrocytes are sequestrated and destroyed. HO-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. HO-1 is involved in the regulation of cardiovascular function and response to a variety of stressors. Defects in HO-1 are the cause of Heme Oxygenase 1 deficiency, resulting in marked erythrocyte fragmentation and intravascular hemolysis, coagulation abnormalities, endothelial damage, and iron deposition in renal and hepatic tissues.
HO-1 Protein, Human, Recombinant
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Pack SizePriceUSA StockGlobal StockQuantity
5 μg$80-In Stock
10 μg$1297-10 days7-10 days
20 μg$1987-10 days7-10 days
50 μg$3907-10 days7-10 days
100 μg$6267-10 days7-10 days
200 μg$9877-10 days7-10 days
500 μg$1,9007-10 days7-10 days
1 mg$2,7307-10 days7-10 days
For In stock only · Estimated delivery: USA Stock (1-2 days) Global Stock (5-7 days)
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For research use only—not for human use. No sales to individuals. Use as intended only.
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Purity:Greater than 95% as determined by reducing SDS-PAGE.
Appearance:Solution
Color:Transparent
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Product Introduction

Bioactivity
Bioactivity
Activity has not been tested. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first.
Description
Heme Oxygenase 1 (HO-1) is an enzyme in endoplasmic reticulum that belongs to the heme oxygenase family. HO-1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is subsequently converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HO-1 is found in the spleen, where senescent erythrocytes are sequestrated and destroyed. HO-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. HO-1 is involved in the regulation of cardiovascular function and response to a variety of stressors. Defects in HO-1 are the cause of Heme Oxygenase 1 deficiency, resulting in marked erythrocyte fragmentation and intravascular hemolysis, coagulation abnormalities, endothelial damage, and iron deposition in renal and hepatic tissues.
Species
Human
Expression System
E. coli
TagTag Free
Accession NumberP09601
Amino AcidMet1-Thr261
ConstructionMet1-Thr261
Protein Purity
Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Endotoxin< 0.1 ng/µg (1 EU/µg) as determined by LAL test.
FormulationSupplied as a 0.2 μm filtered solution of 20 mM PB, 150 mM NaCl, 1 mM EDTA, pH 7.4.
Stability & StorageLyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
ShippingProteins are shipped with blue ice.
SynonymsHO-1, HO1, HO, HMOX1, Heme Oxygenase 1
Research Background
Chemical Properties
Molecular Weight30 KDa (reducing condition)
Storage & Solubility Information
StorageStore at low temperature Lyophilized powder: -20~-80°C for 1 year | Solution: -80°C for 6 months

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Keywords

Related Tags: HO-1 Protein, Human, Recombinant chemical structure | HO-1 Protein, Human, Recombinant molecular weight