|Cat. No. 302 117||100 µg purified IgG, lyophilized. Azide was added before lyophilization. For reconstitution add 100 µl H2O to get a 1mg/ml solution in PBS. Then aliquot and store at -20°C to -80°C until use.|
WB: 1 : 1000 up to 1 : 5000 (AP staining) gallery
ICC: 1 : 500 gallery
IHC: 1 : 500 gallery
IHC-P/FFPE: 1 : 200 up to 1 : 1000 gallery
|Immunogen||Recombinant protein corresponding to AA 1 to 447 from yeast Tyr-α-tubulin|
|Epitop||maps to the last 8 residues (GEEEGEEY) at thecarboxy terminus of alpha tubulin when tyrosinated|
Reacts with: human, rat (P68370), mouse, vertebrates, invertebrates, yeast.
Other species not tested yet.
|Specificity||Specific for tyrosinated α-tubulin (tyr-tubulin). No cross reaction to glu-α-tubulin.|
Microtubules are involved in a wide variety of cellular activities ranging from mitosis and transport events to cell movement and the maintainance of cell shape.
Tubulin itself is a globular protein which consists of two polypeptides, α-tubulin and β-tubulin. α- and β-tubulin dimers are assembled to 13 protofilaments that form a microtubule of 22 nm diameter. Tyrosine ligase ads a C-terminal tyrosin to monomeric α-tubulin.
Assembled microtubules can again be detyrosinated by a cytoskeleton associated carboxypeptidase. Detyrosinated α-tubulin is referred to as Glu-α-tubulin. Another post-translational modification of detyrosinated α-tubulin is C-terminal polyglutamylation which is characteristic for microtubules in neuronal cells and the mitotic spindle. A third variant of detyrosinated α-tubulin is Δ2-tubulin which lacks the C-terminal glutamic acid. It cannot be tyrosinated by tyrosine ligase and is one of the dominant α-tubulin isoforms in neurons.