Description

  • Product name

    Recombinant Human hHR23b protein
  • Purity

    > 90 % SDS-PAGE.

  • Expression system

    Escherichia coli
  • Accession

  • Protein length

    Full length protein
  • Animal free

    No
  • Nature

    Recombinant
    • Species

      Human
    • Sequence

      MQVTLKTLQQQTFKIDIDPEETVKALKEKIESEKGKDAFPVAGQKLIYAG KILNDDTALKEYKIDEKNFVVVMVTKPKAVSTPAPATTQQSAPASTTAVT SSTTTTVAQAPTPVPALAPTSTPASITPASATASSEPAPASAAKQEKPAE KPAETPVATSPTATDSTSGDSSRSNLFEDATSALVTGQSYENMVTEIMSM GYEREQVIAALRASFNNPDRAVEYLLMGIPGDRESQAVVDPPQAASTGAP QSSAVAAAAATTTATTTTTSSGGHPLEFLRNQPQFQQMRQIIQQNPSLLP ALLQQIGRENPQLLQQISQHQEHFIQMLNEPVQEAGGQGGGGGGGSGGIA EAGSGHMNYIQVTPQEKEAIERLKALGFPEGLVIQAYFACEKNENLAANF LLQQNFDED
    • Predicted molecular weight

      43 kDa including tags
    • Amino acids

      1 to 409
    • Tags

      GST tag N-Terminus

Associated products

Specifications

Our Abpromise guarantee covers the use of ab205997 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

  • Form

    Liquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on Dry Ice. Store at -80°C. Avoid freeze / thaw cycle.

    Constituents: 0.24% Tris, 0.87% Sodium chloride, 0.2% Beta mercaptoethanol, 10% Glycerol

General Info

  • Alternative names

    • hHR 23b
    • hHR23B
    • HR 23B
    • HR23B
    • mHR 23B
    • mHR23B
    • p58
    • RAD 23B
    • RAD23 (S. cerevisiae) homolog B
    • RAD23 homolog B
    • RAD23 homolog B (S. cerevisiae)
    • RAD23 yeast homolog of B
    • Rad23b
    • RD23B_HUMAN
    • UV excision repair protein RAD23 homolog B
    • XP C repair complementing complex 58 kDa
    • XP C repair complementing complex 58 kDa protein
    • XP C repair complementing protein
    • XP-C repair-complementing complex 58 kDa protein
    • XPC repair complementing complex 58 kDa
    • XPC repair complementing complex 58 kDa protein
    • XPC repair complementing protein
    see all
  • Function

    Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome. May play a role in endoplasmatic reticulum-associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome.
    Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with CETN2 appears to stabilize XPC. May protect XPC from proteasomal degradation.
    The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts. XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1.
  • Sequence similarities

    Belongs to the RAD23 family.
    Contains 1 STI1 domain.
    Contains 2 UBA domains.
    Contains 1 ubiquitin-like domain.
  • Domain

    The ubiquitin-like domain mediates interaction with ATXN3.
  • Cellular localization

    Nucleus. Cytoplasm. The intracellular distribution is cell cycle dependent. Localized to the nucleus and the cytoplasm during G1 phase. Nuclear levels decrease during S-phase; upon entering mitosis, relocalizes in the cytoplasm without association with chromatin.
  • Information by UniProt

Images

  • SDS-PAGE analysis of ab205997 (5µg).

References

ab205997 has not yet been referenced specifically in any publications.

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