Recombinant Human MED30 / TRAP25 protein (GST tag N-Terminus)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

MED30 also known as TRAP25 is a component of the Mediator complex which functions as a coactivator in transcription. It possesses a molecular mass of approximately 21 kDa. This protein is expressed in a broad range of tissues indicating its ubiquitous role across different biological systems. MED30 forms part of the complex machinery that regulates transcription by serving as a bridge between gene-specific transcription factors and RNA polymerase II.

Biological function summary

MED30 participates in essential processes by integrating signals that are required for the initiation and regulation of transcription. It is a part of the larger Mediator complex which is important for the transcription of nearly all protein-coding genes. The Mediator complex consists of several subunits and MED30 helps in maintaining the structural stability and functional modulation of this assembly contributing to transcription regulation at various levels.

Pathways

MED30 integrates signal transduction pathways with transcriptional regulation. It plays a significant role within the MAPK/ERK and Wnt signaling pathways. In the MAPK/ERK pathway MED30 interacts with key proteins such as ERK1/2 to mediate responses to external stimuli affecting gene expression. Regarding the Wnt pathway it collaborates with beta-catenin linking signaling alterations to changes in transcriptional activity.

MED30 has shown associations with certain cancers and developmental disorders. Abnormalities in the Mediator complex including MED30 have been linked to oncogenesis where irregular expression or mutations could lead to tumor progression. Additionally the dysregulation of Mediator subunits including MED30 connects to developmental syndromes where altered gene expression patterns impair normal developmental processes. Connections between MED30 and other proteins such as beta-catenin in Wnt-related cancers highlight its importance in disease mechanisms.