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Recombinant human PASK (981-end) was expressed by baculovirus in Sf9 insect cells using an N-terminal GST tag. PASK or PAS domain containing serine/threonine kinase regulates the function of many intracellular signaling pathways involved in stress. PASK is involved in sensing environmental changes in light intensity, oxygen concentration and redox potential. Through interaction with IRS-1, PASK has been proposed as a counter-regulatory mechanism in insulin and cytokine signaling (1). PASK can phosphorylate and inactivate glycogen synthase in vitro. Efficient phosphorylation requires residues 444 to 955 of PASK between the PAS and catalytic kinase domain, and this interaction is inhibited by the PAS domain. Kinase Enzyme System contains: Kinase: PASK, 10ug (Human, recombinant; amino acids 981-end). MW: ~66kDa. Substrate: ZIPtide (KKLNRTLSFAEPG). Other: Reaction Buffer, DTT. PASK NCBI Database Entry: www.ncbi.nlm.nih.gov/gene/23178/.
