Facebook

All categories

  • All categories
  • Flow Cytometry Antibodies
  • Immunoassays
  • Cell Isolation and Identification
  • Cell Health and Metabolism Assay Kits
  • Cell Culture
  • Antibodies and Reagents
  • Proteins and Peptides
Please enter the item number/product keyword!
Keyword cannot be empty !
INSERT SYMBOLS:
  • α
  • β
  • γ
  • δ
  • ε
  • ζ
  • η
  • θ
  • κ
  • μ
  • ω
  • σ
  • τ
  • λ
  • Ⅰ
  • Ⅱ
  • Ⅲ
  • Ⅳ
  • Ⅴ
  • Ⅵ
  • Ⅶ
  • Ⅷ
  • Ⅸ
  • Ⅹ
  • Ⅺ
  • Ⅻ
  • ⅩⅢ
  • ⅩⅢ
  • ⅩⅣ
  • ⅩⅤ
  • ⅩⅦ
  • ⅩⅧ
  • UP ↑

Recombinant Human HO1 Protein(Trx Tag) (PDEH100474)

All Size Price Qty
500μg $ 1440.00
- +
100μg $ 488.00
- +
20μg $ 158.00
- +
1mg $ 2340.00
- +
Add to cart

For research use only.

Synonyms 32 kD, 32-kD, bK286B, bK286B10, D8Wsu38e, heat shock protein, heat shock protein 32 kD, heat shock protein 32kD, heme oxygenase, heme oxygenase (decycling), heme oxygenase (decycling) 1, heme oxygenase 1, Hemox, Hmox, HMOX 1, HMOX1, HMOX1D, HO, HO 1, HO-1, HO-1 HMOX, HO-1 HMOX1, HO1, HSP, 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
Form Lyophilized powder
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.
  • IF:{{item.impact}}

    Journal:{{item.journal}} ({{item.year}})

    DOI:{{item.doi}}

    Reactivity:{{item.species}}

    Sample Type:{{item.sample_type}}

  • Q{{(FAQpage.currentPage - 1)*pageSize+index+1}}:{{item.name}}

No files available. Please enter the correct identification code in the search area to query the relevant documents.

empty
Product Information
Title Status Valid until Action
{{v.文件名}} {{v.status_str}} {{v.timestamp_str}} Download /

*Note:Please download the relevant files within the validity period. After expiration, file preview and download will not be available on the page.

确定