Anti-SLU7 antibody [EPR11111]

Supplementary info

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

Activity summary

SLU7 also known as Splicing Factor SLU7 is an essential component of the pre-mRNA splicing process. Weighing approximately 65 kDa SLU7 is mainly found in the nucleus of cells where splicing occurs. It plays an important role in the second catalytic step of alternative splicing by ensuring accurate 3' splice site selection. SLU7 assists in proper intron removal and exon joining during mRNA processing ensuring the production of mature mRNA. Expression of SLU7 is observed in various tissues but high levels are noted in the brain and liver.

Biological function summary

SLU7 influences the regulation of gene expression by participating in mRNA splicing. As part of the larger spliceosome complex SLU7 helps with the recognition of splice sites addressing both simple and more complex pre-mRNA structures. Its function impacts various cellular processes by modulating the diversity of protein products through alternative splicing. This diversity is important for cells to adapt to developmental cues and environmental changes impacting cell differentiation and the response to stress.

Pathways

SLU7 functions significantly in mRNA processing and RNA transport pathways. It interacts with other splicing factors such as U2AF35 and U2AF65 forming a network important for the precise removal of introns from pre-mRNA. SLU7's involvement in these pathways affects numerous cellular transcription-related processes and connects with gene regulatory networks influencing the broader system of gene expression.

Associated diseases and disorders

Errors in SLU7 function have links to neurodegenerative diseases and certain cancers. In neurodegenerative conditions such as Alzheimer's disease altered splicing patterns due to SLU7 malfunction may contribute to the pathology. In cancer aberrant expression or mutations in SLU7 could disrupt normal splicing affecting cellular growth and tumor progression. Connections are seen with RBM17 and other spliceosomal proteins where deregulation can exacerbate disease development and progression.