Anti-SFRS4/SRSF4 antibody

Supplementary info

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

Activity summary

SFRS4 also known as SRSF4 or splicing factor SRp75 is a serine/arginine-rich splicing factor that plays a central role in pre-mRNA splicing. It has a molecular mass of approximately 75 kDa. SRSF4 contributes to the accurate assembly of spliceosomes by binding to specific RNA sequences through its RNA recognition motifs. This protein is expressed ubiquitously with higher expression levels observed in tissues like the brain and heart indicating its importance for proper cellular functions in these areas.

Biological function summary

Splicing is an important process in the regulation of gene expression and SRSF4 actively participates in this essential function by guiding the splicing machinery to the appropriate splice sites. SRSF4 is part of the highly conserved SR protein family which functions collectively as a complex to regulate alternative splicing events. Alternative splicing allows for the generation of multiple protein isoforms from a single gene significantly expanding the proteomic diversity.

Pathways

Alternative splicing regulated by SRSF4 integrates into the larger RNA processing and post-transcriptional modification network. SRSF4 is involved in the mRNA splicing pathway and interacts with various other splicing factors such as SRSF1 and U2AF. These interactions allow precise execution of splicing and efficient production of mature messenger RNA preparatory for translation processes downstream.

Associated diseases and disorders

Mutations or dysregulation of SRSF4 have connections with several conditions including cancer and neurodegenerative diseases. Abnormal splicing patterns regulated by SRSF4 can lead to the production of oncogenic isoforms in various cancers. In neurodegenerative diseases its altered function might disturb neuronal alternative splicing patterns impacting protein diversity vital for neuronal functions. SRSF4 interacts with proteins like SRSF2 and hnRNPs in these pathological contexts influencing the disease progression through defective splicing mechanisms.