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HMOX1 Protein (AA 1-261)

Recombinant HMOX1 protein expressed in Escherichia coli (E. coli).
Catalog No. ABIN1096831

Quick Overview for HMOX1 Protein (AA 1-261) (ABIN1096831)

Target

See all HMOX1 Proteins
HMOX1 (Heme Oxygenase (Decycling) 1 (HMOX1))

Protein Type

Recombinant

Origin

  • 12
  • 4
  • 4
  • 4
  • 2
  • 1
  • 1
Human

Source

  • 16
  • 6
  • 3
  • 2
  • 1
Escherichia coli (E. coli)

Purity

> 95 % as determined by reducing SDS-PAGE.
  • Protein Characteristics

    AA 1-261

    Purpose

    Recombinant Human Heme Oxygenase 1/HO-1

    Sequence

    MERPQPDSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALE QDLAFWYGPR WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NIASATKFKQ LYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV ETPRGKPPLN T

    Characteristics

    Recombinant Human Heme Oxygenase 1/HO-1 is produced with our E. coli expression system. The target protein is expressed with sequence (Met1-Thr261) of Human HO-1.

    Sterility

    0.2 μm filtered

    Endotoxin Level

    Less than 0.1 ng/μg (1 IEU/μg) as determined by LAL test
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  • Restrictions

    For Research Use only
  • Format

    Liquid

    Reconstitution

    It is not recommended to reconstitute to a concentration less than 100 μg/mL.
    Dissolve the lyophilized protein in ddH2O.
    Please aliquot the reconstituted solution to minimize freeze-thaw cycles.

    Buffer

    Supplied as a 0.2 μm filtered solution of 20 mM PB, 150 mM NaCl, 1 mM EDTA, pH 7.4.

    Handling Advice

    Always centrifuge tubes before opening. Do not mix by vortex or pipetting.

    Storage

    -80 °C

    Storage Comment

    Store at < -20°C, stable for 6 months after receipt.
    Please minimize freeze-thaw cycles.

    Expiry Date

    6 months
  • Target

    HMOX1 (Heme Oxygenase (Decycling) 1 (HMOX1))

    Alternative Name

    hmox1

    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.
    Alternative Names: Heme Oxygenase 1, HO-1, HMOX1, HO, HO1

    Molecular Weight

    29.86 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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