Cat. No. 302 011 |
100 µg purified IgG, lyophilized. Albumin and azide were 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. Antibodies should be stored at +4°C when still lyophilized. Do not freeze! |
Applications | |
Clone | 1D5 |
Subtype | IgG1 (κ light chain) |
Immunogen | Synthetic peptide corresponding to residues near the c-terminus of human Glu-α-tubulin. (UniProt Id: Q71U36) |
Epitop |
AA 448 to 450 from human Glu-α-tubulin (UniProt Id: Q71U36) |
Reactivity |
Reacts with: human (Q71U36), rat (P68370), mouse (P68369), zebrafish, eukaryotes, other vertebrates. Other species not tested yet. Detects also cilia of Paramecium. |
Specificity | Specific for detyrosinated α-tubulin (glu-tubulin) and polyglutamylated tubulin (also β-tubulin). No cross reaction to tyrosinated tubulin. |
Remarks |
WB: Tween 20 (other detergents not yet tested) should not be added to the blocking and washing solution. It greatly diminishes the intensity of the signal. |
Data sheet | 302_011.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. 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.