Heme oxygenase 1 (HO-1) is an endoplasmic reticulum heme oxygenase enzyme in the heme oxygenase family. HO-1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is subsequently broken down to Bilirubin by Biliverdin reductase. The highest HO-1 activity is in the spleen, where senescent erythrocytes are sequestrated and destroyed in the physiological state. The induction of HO-1 activity by its substrate heme and various non-heme chemicals including heavy metals, bromobenzene, endotoxin, oxidizing agents, and UVA is well documented. HO-1 is important in the regulation of cardiac 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. Human HO/HMOX1 Recombinant Protein is a highly pure recombinant protein developed by Assay Genie for use in a range of applications.
Product Name:
Human HO/HMOX1 Recombinant Protein (RPES0471)
Product Code:
RPES0471
Size:
10µg
Species:
Human
Expressed Host:
E.coli
Synonyms:
Heme Oxygenase 1, HO-1, HMOX1, HO, HO1
Accession:
P09601
Sequence:
Met 1-Thr 261
Fusion tag:
Endotoxin:
<1.0 EU per µg as determined by the LAL method.
Protein Construction:
Recombinant Human Heme Oxygenase 1 is produced by our E.coli expression system and the target gene encoding Met1-Thr261 is expressed.
Purity:
> 95 % as determined by reducing SDS-PAGE.
Mol Mass:
29.9 kDa
AP Mol Mass:
30 kDa
Formulation:
Supplied as a 0.2 µm filtered solution of 20mM PB, 150mM NaCl, 1mM EDTA, pH 7.4.
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.
Stability and Storage:
Store at < -20°C, stable for 6 months. Please minimize freeze-thaw cycles.
Human HO-1 / HMOX1 / HSP32 ELISAHMOX1 (Heme Oxygenase 1) is a Protein Coding gene and is 96 amino acids long and weighs 10 kDa. HMOX1 has an interesting ortholog in the dolphin and Danio rerio...