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Recombinant Human HO1 Protein(Trx Tag) (PDEH100474)

All Size Price Qty
500μg $ 1440.00
100μg $ 488.00
20μg $ 158.00
1mg $ 2340.00
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For research use only.

Synonyms HSP, heme oxygenase, heme oxygenase (decycling), bK286B, HO-1 HMOX, HMOX1, HMOX1D, HO-1, HSP32, bK286B10, 32 kD, D8Wsu38e, heat shock protein 32 kD, heat shock protein 32kD, Hemox, Hmox, HMOX 1, HO 1, HO-1 HMOX1, heme oxygenase (decycling) 1, heme oxygenase 1, heat shock protein, 32-kD, HO, HO1, bK286B10, heme oxygenase 1, HMOX1D, HO-1, HSP32
Species Human
Expression Host E.coli
Sequence Met1-Thr261
Accession P09601
Calculated Molecular Weight 48.7 kDa
Observed Molecular Weight 48 kDa
Tag N-Trx
Bio-activity Not validated for activity
Purity > 95% as determined by reducing SDS-PAGE.
Endotoxin < 10 EU/mg of the protein as determined by the LAL method
Storage Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Shipping This product is provided as lyophilized powder which is shipped with ice packs.
Formulation Lyophilized from a 0.2 μm filtered solution in PBS with 5% Trehalose and 5% Mannitol.
Reconstitution It is recommended that sterile water be added to the vial to prepare a stock solution of 0.5 mg/mL. Concentration is measured by UV-Vis
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.
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