Description

  • Product name

    Recombinant Human HBP protein
  • Purity

    > 90 % SDS-PAGE.
    ab139244 is purified using conventional chromatography techniques.
  • Expression system

    Escherichia coli
  • Accession

  • Protein length

    Full length protein
  • Animal free

    No
  • Nature

    Recombinant
    • Species

      Human
    • Sequence

      MGSSHHHHHHSSGLVPRGSHMGSMLGMIKNSLFGSVETWPWQVLSKGDKE EVAYEERACEGGKFATVEVTDKPVDEALREAMPKVAKYAGGTNDKGIGMG MTVPISFAVFPNEDGSLQKKLKVWFRIPNQFQSDPPAPSDKSVKIEEREG ITVYSMQFGGYAKEADYVAQATRLRAALEGTATYRGDIYFCTGYDPPMKP YGRRNEIWLLKT
    • Predicted molecular weight

      24 kDa including tags
    • Amino acids

      1 to 189
    • Tags

      His tag N-Terminus

Specifications

Our Abpromise guarantee covers the use of ab139244 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    SDS-PAGE

    Mass Spectrometry

  • Mass spectrometry

    MALDI-TOF
  • Form

    Liquid
  • Additional notes

    Product previously known as Recombinant Human HEBP1 protein.

  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

    pH: 8.00
    Constituents: 0.02% DTT, 0.32% Tris HCl, 30% Glycerol, 0.88% Sodium chloride

General Info

  • Alternative names

    • HBP
    • HEBP
    • Hebp1
    • HEBP1_HUMAN
    • Heme binding protein 1
    • Heme-binding protein 1
    • p22HBP
    see all
  • Function

    May bind free porphyrinogens that may be present in the cell and thus facilitate removal of these potentially toxic compound. Binds with a high affinity to one molecule of heme or porphyrins. It binds metalloporphyrins, free porphyrins and N-methylprotoporphyrin with similar affinities.
  • Sequence similarities

    Belongs to the HEBP family.
  • Domain

    Forms a distorted beta-barrel structure, with two helices that are packed against the outer surface of the barrel. Porphyrins are expected to bind to a hydrophobic patch on the outer surface of the beta-barrel structure.
  • Cellular localization

    Cytoplasm.
  • Information by UniProt

Images

  • 15% SDS-PAGE analysis of 3 µg ab139244.

References

ab139244 has not yet been referenced specifically in any publications.

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