Cat. No. 302 308 |
50 µg purified recombinant IgG, lyophilized. Albumin and azide were added for stabilization. For reconstitution add 50 µl H2O to get a 1mg/ml solution in PBS. Then aliquot and store at -20°C to -80°C until use. Antibodies should be stored at +4°C when still lyophilized. Do not freeze! |
Applications | |
Clone | Gp3A2 |
Subtype | IgG2 (κ light chain) |
Immunogen | Synthetic peptide corresponding to residues near the carboxy terminus of human α-Tubulin 4A. (UniProt Id: P68366) |
Reactivity |
Reacts with: human (P68366), rat (Q5XIF6), mouse (P68368), vertebrates, invertebrates, yeast. Other species not tested yet. |
Specificity | Specific for α-tubulin (glu- and tyr-α-tubulin) |
Matching control protein/peptide | 302-21P |
Remarks |
This antibody is a chimeric antibody based on the well known monoclonal mouse antibody clone 3A2. The constant regions of the heavy and light chains have been replaced by Guinea pig specific sequences. Therefore, the antibody can be used with standard anti-Guinea pig secondary reagents. The antibody has been expressed in mammalian cells. |
Data sheet | 302_308.pdf |
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.
Assembled microtubules can be detyrosinated by a carboxypeptidaseS called vasohibins / SVBPs. Detyrosinated α-tubulin is referred to as Glu-α-tubulin and occurs for exemple in neurons. This reaction can be reverted by Tubulin tyrosine ligase (TTL) that ads a C-terminal tyrosin to Glu α-tubulin.
Another post-translational modification of α-tubulin is C-terminal polyglutamylation which is also 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 TTL and is one of the dominant α-tubulin isoforms in neurons.