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AGC group

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Recombinant protein kinases of the AGC family

The AGC kinase group defines the subgroup of Ser/Thr protein kinases named after 3 representative families, the cAMP-dependent protein kinase (PKA), the cGMP-dependent protein kinase (PKG) and the protein kinase C (PKC) families. The AGC family contains more than 60 human protein kinases which have been highly conserved throughout eukaryotic evolution and can be classified into 14 subfamilies. A unique feature of AGC kinases is the presence of a C-terminal segment containing a hydrophobic motif within the catalytic domain whereas the selectivity and specificity in the regulation of AGC kinases is predominantly derived from the regions located N- and C-terminal to the catalytic core.

  • PKC
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  • cGMP-dependent protein kinase, PKG

    cGMP-dependent protein kinases (PKG)

    cGMP-dependent protein kinases (PKG) are a group of Ser/Thr protein kinases containing two isoforms, type 1 and type 2, that are regulated by the second messenger cGMP. In contrast to PKA, the cGMP binding and catalytic domains are located on the same polypeptide. Binding of the second messenger cGMP induces a conformational change that relieves the inhibitory effect of a pseudosubstrate domain. PKG mediates many of the smooth muscle relaxation effects triggered by nitric oxide.


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  • cAMP-dependent protein kinase, PKA

    cAMP-dependent protein kinase (PKA)

    cAMP-dependent protein kinase - PKA is an ubiquitous serine-theonine protein kinase present in a variety of tissues. The intracellular cAMP level regulates cellular responses by altering the interaction between the catatytic C and regulatory R subunits of PKA. The inactive PKA holoenzyme is activated when cAMP binds to the regulatory subunits which induces the release of two active catalytic subunits.

    cAMP-dependent protein kinase - PKA - catalytic and regulatory subunits - holo enzyme


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  • Akt/PKB

    Protein kinase B or Akt (PKB/Akt)

    Protein kinase B or Akt (PKB/Akt)is a serine/threonine kinase, which in mammals comprises three highly homologous members known as PKB alpha (Akt1), PKB beta (Akt2) and PKB gamma (Akt3). PKB/Akt is a growth-factor-regulated protein kinase which contains a pleckstrin homology (PH) domain. Binding of phosphoinositide 3-OH kinase products to the pleckstrin homology domain results in translocation of PKB/Akt to the plasma membrane where it is activated by phosphorylation by upstream kinases including the phosphoinoside-dependent kinase 1 (PDK1). Key roles for this enzyme can be found in cellular processes such as glucose metabolism, cell proliferation, apoptosis, transcription and cell migration.


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