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SLU7 knockdown in liver cells resulted in profound changes in pre-mRNA splicing and gene expression, leading to impaired glucose and lipid metabolism, refractoriness to key metabolic hormones, and reversion to a fetal-like gene expression pattern.
These observations together point to an altered recruitment and dependence on SLU7, suggesting its role in facilitating transitions that promote catalysis, and highlight the diversity in spliceosome assembly.
RBM22 and hSlu7 differ significantly in their subcellular distributions under stress conditions, and RBM22 enhances the cytoplasmic translocation of hSlu7 under stress.
The zinc-knuckle motif of hSlu7 determines the cellular localization of the protein through a nucleocytoplasmic-sensitive shuttling balance.
hSlu7 has a broad effect on alternative splicing
Regulation of transcription of the RNA splicing factor hSlu7 by Elk-1 (show ELK1 Proteins) and Sp1 (show PSG1 Proteins) affects alternative splicing
SLU7 knockdown in liver resulted in profound changes in pre-mRNA splicing and gene expression, leading to impaired glucose and lipid metabolism, refractoriness to key metabolic hormones, and reversion to a fetal-like gene expression pattern.
Pre-mRNA splicing occurs in two sequential transesterification steps. The protein encoded by this gene is a splicing factor that has been found to be essential during the second catalytic step in the pre-mRNA splicing process. It associates with the spliceosome and contains a zinc knuckle motif that is found in other splicing factors and is involved in protein-nucleic acid and protein-protein interactions.
, Pre-mRNA-splicing factor SLU7
, pre-mRNA-splicing factor SLU7
, splicing factor
, step II splicing factor SLU7
, zinc knuckle motif containing