AK, Auto-Activated Protein Kinase

Source: Bovine kidney

Purity: > 90% by SDS-PAGE, apparent Mr ~ 36-kDa

Supplied: 50 ng (~ 1 units) 100 ng (~ 2 units) supplied in 10 μl or 20 μl, respectively of 50 mM Tris-HCl pH 7.0 buffer containing 14 mM β-mercaptoethanol, 0.03% Brij-35. 1 mM benzamidine, 0.1 mM phenylmethanesulfonyl fluoride, 1 mM EDTA and 65% ethyleneglycol.

Activity: ~ 17,000 units/mg with myelin basic protein (MBP) as substrate. One unit of AK is the amount of the enzyme that incorporates 1 nmol of phosphate into MBP per min. Maintain preparations in aliquots at -70° C. Avoid repeated thawing.

Synonyms: Auto-Activated Protein Kinase; Autophosphorylation-Activated Protein Kinase; Catalytic Domain of PAK2; Catalytic Domain of p21-Activated Protein Kinase.

Gel filtration Chromatography of Purified Auto-activated Protein Kinase



Figure: Sephacryl S-200 profile of the purified preparations of AK; Activity (●—●);  Protein (○—○) . Insert shows the SDS-PAGE pattern of the purified preparation. The gel was stained with silver.



Background: The catalytic domain of PAK2 was originally isolated as an Auto-activated Protein Kinase (AK). It was so termed because the purified enzyme underwent rapid autophosphorylation and concomitant 15-30-fold activation. Subsequent identification of PAK’s and amino sequencing of AK revealed that it was equivalent to the catalytic domain of PAK2*. Unlike native PAK2, AK does not require the p21-GTPases Cdc42 and Rac for activity. AK is a physiologically relevant form of PAK2. It is produced from the native enzyme via a caspase-dependent pathway in cells undergoing apoptosis.

References: Proc Natl Acad Sci USA 90: 2500   J Biol Chem 268: 11193   J Cell Physiol 178: 397   J Biol Chem 276: 14909 * Damuni Z. unpublished observations



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