|Cat. No. 302 204||100 µl antiserum, lyophilized. For reconstitution add 100 µl H2O, then aliquot and store at -20°C until use.|
WB: 1 : 1000 up to 1 : 5000 (AP staining) gallery
IP: not tested yet
ICC: 1 : 500 gallery
IHC: 1 : 500 gallery
IHC-P/FFPE: not tested yet
|Immunogen||Synthetic peptide corresponding to AA 419 to 435 from human α-tubulin 4A (UniProt Id: P68366)|
Reacts with: human (P68366), rat (Q5XIF6), mouse (P68368).
Other species not tested yet.
|Specificity||Specific for α-tubulin (glu- and tyr-α-tubulin).|
|Matching control protein/peptide||302-21P|
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.