|Cat. No. 302 203||100 µg specific antibody, lyophilized. Affinity purified with the immunogen. Albumin was added for stabilization. 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
IP: not recommended
ICC: 1 : 100 up to 1 : 1000 gallery
IHC: 1 : 400 gallery
IHC-P/FFPE: not tested yet
ELISA: yes (see remarks)
|Immunogen||Synthetic peptide corresponding to AA 443 to 449 from rat α-tubulin (UniProt Id: P68370)|
Reacts with: human, rat (P68370-1), mouse, mammals, chicken.
Other species not tested yet.
|Specificity||Recognizes glu- and tyr-α-tubulin and Δ2-tubulin with a preference for glu- and Δ2-tubulin.|
ELISA: Suitable as detector antibody for sandwich-ELISA with cat. no. 302 211 as capture antibodies.
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.