Western blot analysis of Lane 1: Untreated 293 cell lysates, Lane 2: Synthesized peptide treated 293 cell lysates reacted with STK4/STK3 (phospho T183) polyclonal antibody (Cat # PAB29650) at 1:500-1:3000 dilution.
Immunohistochemical staining of paraffin-embedded human brain tissue reacted with STK4/STK3 (phospho T183) polyclonal antibody (Cat # PAB29650) at 1:50-1:100 dilution. The picture on the right is treated with the synthesized peptide.
The protein encoded by this gene is a cytoplasmic kinase that is structurally similar to the yeast Ste20p kinase, which acts upstream of the stress-induced mitogen-activated protein kinase cascade. The encoded protein can phosphorylate myelin basic protein and undergoes autophosphorylation. A caspase-cleaved fragment of the encoded protein has been shown to be capable of phosphorylating histone H2B. The particular phosphorylation catalyzed by this protein has been correlated with apoptosis, and it's possible that this protein induces the chromatin condensation observed in this process. [provided by RefSeq
Protein kinase activation is a frequent response of cells to treatment with growth factors, chemicals, heat shock, or apoptosis-inducing agents. This protein kinase activation presumably allows cells to resist unfavorable environmental conditions. The yeast 'sterile 20' (Ste20) kinase acts upstream of the mitogen-activated protein kinase (MAPK) cascade that is activated under a variety of stress conditions. MST2 was identified as a kinase that is activated by the proapoptotic agents straurosporine and FAS ligand (MIM 134638) (Taylor et al., 1996 [PubMed 8816758]; Lee et al., 2001 [PubMed 11278283]).[supplied by OMIM