Description

  • Product name

    Recombinant Human beta IV Tubulin protein (His tag)
    See all beta IV Tubulin proteins and peptides
  • Purity

    > 90 % SDS-PAGE.

  • Expression system

    Escherichia coli
  • Accession

  • Protein length

    Full length protein
  • Animal free

    No
  • Nature

    Recombinant
    • Species

      Human
    • Sequence

      MREIVHLQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLERINVY YNEATGGNYVPRAVLVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNN WAKGHYTEGAELVDAVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTL LISKIREEFPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADL RKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMM AACDPRHGRYLTVAAVFRGRMSMKEVDEQMLSVQSKNSSYFVEWIPNNVK TAVCDIPPRGLKMAATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG EGMDEMEFTEAESNMNDLVSEYQQYQDATAEEGEFEEEAEEEVA
    • Predicted molecular weight

      54 kDa including tags
    • Amino acids

      1 to 444
    • Tags

      His tag N-Terminus

Specifications

Our Abpromise guarantee covers the use of ab236168 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 at 4°C. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

    Constituents: Tris buffer, 50% Glycerol

General Info

  • Alternative names

    • Beta 4
    • Beta 4 tubulin
    • beta 5
    • beta four tubulin
    • Dystonia 4 torsion (autosomal dominant)
    • MC1R
    • TBB4_HUMAN
    • TUB B4
    • TUBB 4
    • tubb4
    • TUBB4A
    • TUBB5
    • Tubulin 5 beta
    • Tubulin beta 3
    • Tubulin beta 4
    • Tubulin beta 4 chain
    • Tubulin beta 4A class IVa
    • Tubulin beta 5
    • Tubulin beta IV
    • Tubulin beta-4 chain
    see all
  • Function

    Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha-chain.
  • Sequence similarities

    Belongs to the tubulin family.
  • Domain

    The highly acidic C-terminal region may bind cations such as calcium.
  • Post-translational
    modifications

    Some glutamate residues at the C-terminus are polyglutamylated. This modification occurs exclusively on glutamate residues and results in polyglutamate chains on the gamma-carboxyl group. Also monoglycylated but not polyglycylated due to the absence of functional TTLL10 in human. Monoglycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally. The precise function of such modifications is still unclear but they regulate the assembly and dynamics of axonemal microtubules.
  • Cellular localization

    Cytoplasm > cytoskeleton.
  • Information by UniProt

Images

  • Analysis of ab236168 (Tris-Glycine gel) discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

References

ab236168 has not yet been referenced specifically in any publications.

Customer reviews and Q&As

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