Recombinant Human beta III Tubulin protein (ab125990)

Overview

Description

  • Nature
    Recombinant
  • Source
    Escherichia coli
  • Amino Acid Sequence
    • Accession
    • Species
      Human
    • Sequence
      QCGNQIGAKFWEVISDEHGIDPSGNYVGDSDLQLERISVYYNEASSHKYV PRAILVDLEPGTMDSVRSGAFGHLFRPDNFIFGQSGAGNNWAKGHYTEGA ELVDSVLDVVRKECENCDCLQGFQLTHSLGGGTGSGMGTLLISKVREEYP DRIMNTFSVVPSPKVSDTVVEPYNATLSIHQLVENTDETYCIDNEALYDI CFRTLKLATPTYGDLNHLVSATMSGVTTSLRFPGQLNADLRKLAVNMVPF PRLHFFMPG
    • Amino acids
      11 to 269

Associated products

Specifications

Our Abpromise guarantee covers the use of ab125990 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
    Lyophilised
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Store at -20°C.

    Constituents: 0.32% Tris HCl, 0.58% Sodium chloride, 28.8% Guanidine HCl

  • Reconstitution
    Reconstitute with water to desired concentration.

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

References

ab125990 has not yet been referenced specifically in any publications.

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