p38 gamma/MAPK12 Protein, Human (sf9, His-GST)

The p38 gamma/MAPK12 protein is an important serine/threonine kinase in the MAP kinase pathway and can respond to extracellular stimuli such as pro-inflammatory cytokines or stress. p38 MAPK activates transcription factors such as ELK1 and ATF2, each of which phosphorylates approximately 200 to 300 substrates. p38 gamma/MAPK12 Protein, Human (sf9, His-GST) is the recombinant human-derived p38 gamma/MAPK12 protein, expressed by Sf9 insect cells , with N-His, N-GST labeled tag.

p38 gamma/MAPK12, a serine/threonine kinase and crucial component of the MAP kinase signal transduction pathway, is among the four p38 MAPKs playing a pivotal role in cellular responses triggered by extracellular stimuli such as pro-inflammatory cytokines or physical stress. This pathway leads to the direct activation of transcription factors like ELK1 and ATF2, with p38 MAPKs phosphorylating a diverse array of proteins, estimated to have approximately 200 to 300 substrates each. Among its downstream kinases is MAPKAPK2, activated through phosphorylation to further phosphorylate additional targets. MAPK12 contributes to myoblast differentiation and down-regulation of cyclin D1 in response to hypoxia in adrenal cells, suggesting its role in inhibiting cell proliferation while promoting differentiation. Notably, MAPK12 phosphorylates DLG1, and following osmotic shock, it increases its association with nuclear DLG1, impacting mRNA processing and/or gene transcription to aid cell adaptation to osmolarity changes. Additionally, MAPK12 regulates UV-induced checkpoint signaling and repair of UV-induced DNA damage, influences glucose uptake in muscle cells, and is essential for the normal kinetochore localization of PLK1, preventing chromosomal instability and supporting mitotic cell viability. Its signaling positively regulates the expansion of transient amplifying myogenic precursor cells during muscle growth and regeneration.

Human

Sf9 insect cells

N-His;N-GST

P53778-1 (M1-L367)

6300  [NCBI]

Approximately 65 kDa

Greater than 95% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.