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Delta2-tubulin antibody - 302 213

Delta2-tubulin is a major cytoskeleton protein mainly occuring in neurons
Rabbit polyclonal purified antibody
Cat. No.: 302 213
Amount: 50 µg
Price: $375.00
Cat. No. 302 213 50 µg specific antibody, lyophilized. Affinity purified with the immunogen. Albumin was 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
 
WB: 1 : 1000 (AP staining) gallery  
IP: not tested yet
ICC: 1 : 200 up to 1 : 500 (see remarks) gallery  
IHC: yes gallery  
IHC-P: 1 : 500 gallery  
Immunogen Synthetic peptide corresponding to AA 443 to 449 from rat Δ2-tubulin (UniProt Id: P68370)
Reactivity Reacts with: human, rat (P68370), mouse, mammals.
Other species not tested yet.
Specificity Specific for Δ2-tubulin.
Remarks

This antibody has been cross-adsorbed against peptides corresponding to the C-termini of glu- and tyr-tubulin.
ICC: Requires long permeabilization with 0.3% Triton X 100 for 30 min.

Data sheet 302_213.pdf
Cat. No.: 302 213
Amount: 50 µg
Price: $375.00
Background

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.