Overview

Description

  • Nature

    Recombinant
  • Source

    Wheat germ
  • Amino Acid Sequence
    • Accession
    • Species

      Human
    • Sequence

      MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPSGNYVGDSDLQLERISVY YNGASSHKYVPRAILVDLEPGTMDSVRSGAFGHLFRPDNFIFGQSGAGNN WAKGHYTEGAELVDSVLDVVRKECENCDCLQGFQLTHSLGGGTGSGMGTL LISKVREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSIHQLVENTDETY CIDNEALYDICFRTLKLATPTYGDLNHLVSATMSGVTTSLRFPGQLNADL RKLAVNMVPFPRLHFFMPGFAPLTARGSQQYRALTVPELTQQMFDAKNMM AACDPRHGRYLTVATVFRGRMSMKEVDEQMLAIQSKNSSYFVEWIPNNVK VAVCDIPPRGLKMSSTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG EGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEGEMYEDDEEESEAQGPK
    • Molecular weight

      75 kDa including tags
    • Amino acids

      1 to 450
    • Tags

      GST tag N-Terminus

Associated products

Specifications

Our Abpromise guarantee covers the use of ab131995 in the following tested applications.

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

  • Applications

    ELISA

    Western blot

    SDS-PAGE

  • Form

    Liquid
  • Additional notes

    Protein concentration is above or equal to 0.05 &microg/&microl

  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.

    pH: 8.00
    Constituents: 0.31% Glutathione, 0.79% Tris HCl

General Info

  • Alternative names

    • beta 3 tubulin
    • beta-4
    • CDCBM
    • CDCBM1
    • CFEOM3
    • CFEOM3A
    • FEOM3
    • M(beta)3
    • M(beta)6
    • MC1R
    • Neuron specific beta III Tubulin
    • Neuron-specific class III beta-tubulin
    • QccE-11995
    • QccE-15186
    • TBB3_HUMAN
    • Tubb 3
    • TUBB3
    • TUBB4
    • Tubulin beta 3
    • Tubulin beta 3 chain
    • Tubulin beta 4
    • Tubulin beta III
    • Tubulin beta-3 chain
    • Tubulin beta-4 chain
    • Tubulin beta-III
    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. TUBB3 plays a critical role in proper axon guidance and mantainance.
  • Tissue specificity

    Expression is primarily restricted to central and peripheral nervous system.
  • Involvement in disease

    Defects in TUBB3 are the cause of congenital fibrosis of extraocular muscles type 3A (CFEOM3A) [MIM:600638]. A congenital ocular motility disorder marked by restrictive ophthalmoplegia affecting extraocular muscles innervated by the oculomotor and/or trochlear nerves. It is clinically characterized by anchoring of the eyes in downward gaze, ptosis, and backward tilt of the head. Congenital fibrosis of extraocular muscles type 3 presents as a non-progressive, autosomal dominant disorder with variable expression. Patients may be bilaterally or unilaterally affected, and their oculo-motility defects range from complete ophthalmoplegia (with the eyes fixed in a hypo- and exotropic position), to mild asymptomatic restrictions of ocular movement. Ptosis, refractive error, amblyopia, and compensatory head positions are associated with the more severe forms of the disorder. In some cases the ocular phenotype is accompanied by additional features including developmental delay, corpus callosum agenesis, basal ganglia dysmorphism, facial weakness, polyneuropathy.
  • 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

  • 12.5% SDS-PAGE using ab131995 stained with Coomassie Blue.

References

ab131995 has not yet been referenced specifically in any publications.

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