Over the past nineteen years, GloboZymes has established itself as a leading provider of top quality protein kinases, protein kinase substrates, protein phosphatases, modulator proteins, protein synthesis initiation factors and antibodies. As a worldwide provider of purified signal transduction enzymes, regulatory proteins and antibodies, we assure quality above all. Below are just a few examples of the top quality protein kinase preparations we supply.
Purified GST-tagged PAK1
PAK1 is a 65-68 kDa Group I member of a protein serine/threonine kinase family whose activity is stimulated by the Rho family small GTPases Rac and Cdc42. PAKs regulate numerous cellular processes. These include cell morphology and cytoskeleton organization, cell motility, apoptosis, neuronal functions, cell cycle progression and viral replication. GST-PAK1 exhibits an apparent Mr ~ 100 kDa on SDS-PAGE.
An extract (30 ug) of HEK293 cells was subjected to Western blotting with GloboZymes affinity-purified Anti-PAK polyclonal antibody. The arrow denotes the position of PAK1 (65 kDa). The affinity-purified polyclonal antibody was produced in rabbits to a synthetic peptide corresponding to residues 484-502 of human PAK1. It reacts with PAK from diverse tissues (not shown).
Purified Preparations of Auto-Activated Protein Kinase (AK)
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.
AK is PAK2 Catalytic Domain
N-terminal and internal amino acid sequencing of GloboZymes purified preparations of AK demonstrated that this enzyme represents the catalytic domain of the PAK2 enzymes. AK is physiologically relevant as it is produced in cells during apoptosis. It does not require G-proteins cdc42 or Rac for activation.
cPK, Cytosolic Protamine Kinase
GloboZymes provides purified preparations of cPK from bovine kidney. These preparations phosphorylate eIF4E at Ser209 and Thr210. Interestingly, Thr210 is rapidly and preferentially dephosphorylated by PP2A. This may, in part, confer the site specificty of the phosphorylation of eIF4E at Ser209 in vivo.