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HMOX1 Protein (AA 1-288) (His tag)

HMOX1 Origin: Human Host: Escherichia coli (E. coli) Recombinant > 95 % as determined by reducing SDS-PAGE.
Catalog No. ABIN7505108
  • Target See all HMOX1 Proteins
    HMOX1 (Heme Oxygenase (Decycling) 1 (HMOX1))
    Protein Type
    Recombinant
    Protein Characteristics
    AA 1-288
    Origin
    • 13
    • 4
    • 4
    • 4
    • 2
    • 1
    • 1
    Human
    Source
    • 16
    • 6
    • 3
    • 2
    • 2
    Escherichia coli (E. coli)
    Purification tag / Conjugate
    This HMOX1 protein is labelled with His tag.
    Sequence
    Met 1-Met 288
    Characteristics
    A DNA sequence encoding the Human HO1 protein (P09601) (Met 1-Met 288) was expressed with a N-His tag.
    Purity
    > 95 % as determined by reducing SDS-PAGE.
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    Product
    Expression System
    Conjugate
    Origin
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    Expression System HEK-293 Cells
    Conjugate His tag
    Origin Human
    Price starts at $16,231.82
    Expression System Cell-free protein synthesis (CFPS)
    Conjugate Strep Tag
    Origin Human
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  • Restrictions
    For Research Use only
  • Format
    Lyophilized
    Buffer
    Lyophilized from sterile PBS, pH 7.4.
    Normally 5 % - 8 % trehalose, mannitol and 0.01 % Tween80 are added as protectants before lyophilization.
    Storage
    4 °C,-20 °C,-80 °C
    Storage Comment
    Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
    Expiry Date
    12 months
  • Target
    HMOX1 (Heme Oxygenase (Decycling) 1 (HMOX1))
    Alternative Name
    HO1 (HMOX1 Products)
    Background

    Abbreviation: HO1

    Target Synonym: Heme Oxygenase 1,HO-1 HMOX1,HO,HO1

    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.

    Molecular Weight

    Calculated MW: 31.57 kDa

    Observed MW: 35 kDa

    UniProt
    P09601
    Pathways
    Transition Metal Ion Homeostasis, Regulation of Leukocyte Mediated Immunity, Positive Regulation of Immune Effector Process, Production of Molecular Mediator of Immune Response, SARS-CoV-2 Protein Interactome
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