|Cat. No. 302 008||100 µg purified IgG, lyophilized. For reconstitution add 100 µl H2O to get a 1mg/ml solution in PBS. 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 (see remarks) gallery
IHC: 1 : 500 gallery
IHC-P/FFPE: not tested yet
|Subtype||IgG1 (κ light chain)|
|Immunogen||α-Tubulin purified from bovine brain|
Reacts with: human, rat, mouse, cow.
Other species not tested yet.
|Specificity||Specific for α-tubulin|
This antibody is a chimeric antibody based on the monoclonal mouse antibody F2C. The constant regions of the heavy and light chains have been replaced with rabbit specific sequences. The antibody can therefore be used with standard anti-rabbit secondary reagents. The antibody has been expressed in mammalian cells and carries a Strep-tag® at the C-terminus of the heavy chain.
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.