Description
Recombinant Human HO-1/HMOX1 Protein | PKSH032529 | Gentaur US, UK & Europe Disrtribition
Synonyms: Heme Oxygenase 1; HO-1; HMOX1; HO; HO1
Active Protein: N/A
Activity: Recombinant Human Heme Oxygenase 1 is produced by our E.coli expression system and the target gene encoding Met1-Thr261 is expressed.
Protein Construction: Recombinant Human Heme Oxygenase 1 is produced by our E.coli expression system and the target gene encoding Met1-Thr261 is expressed.
Fusion Tag:
Species: Human
Expressed Host: E.coli
Shipping: This product is provided as liquid. It is shipped at frozen temperature with blue ice/gel packs. Upon receipt, store it immediately at<-20°C.
Purity: > 95 % as determined by reducing SDS-PAGE.
Endotoxin: < 1.0 EU per µg as determined by the LAL method.
Stability and Storage: Store at < -20°C, stable for 6 months. Please minimize freeze-thaw cycles.
Molecular Mass: 29.9 kDa
Formulation: Supplied as a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, 1mM EDTA, pH 7.4.
Reconstitution: Not Applicable
Background: 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.
Research Area: Signal Transduction, Cardiovascular, Neuroscience, Cancer, epigenetics and nuclear signal, metabolism,