Mitogen- and stress-activated protein kinases (MSK2) is nuclear kinase that act downstream of mitogen-activated protein/extracellular signal-regulated kinase pathways. It contains two kinase domains in the N-terminal and C-terminal region, respectively. MSK2 is activated in response to mitogenic stimuli via Erk1/2MAPK pathway and also by stress stimuli via p38MAPK pathway. Signals from mitogens and cellular stresses are involved in many functions including cell proliferation, differentiation, and survival through the phosphorylation of cyclic AMP response element-binding protein (CREB) at Ser133 which is catalyzed by MSK2. Recently, MSK2 has been shown to be required for stress-induced phosphorylation of histone H3-Ser and transcriptional activation of several immediate early genes.

Western Blot: 1:2,000; Immunohistochemistry: Paraffin-embedded sections;

Type: Primary
Antigen: RPS6KA4 (ribosomal protein S6 kinase, 90kDa, polypeptide 4)
Clonality: Polyclonal
Clone:
Conjugation: Unconjugated
Epitope:
Host: Rabbit
Isotype: IgG
Reactivity: Human