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LSM4 encodes a member of the LSm family of RNA-binding proteins. Additionally we are shipping LSM4 Antibodies (41) and LSM4 Proteins (20) and many more products for this protein.
Results show that the RGG domain of human Lsm4 stimulates processing bodies formation. Also, a novel interaction of the Lsm4 RGG domain with HAT1 (show HAT1 ELISA Kits) and RBBP7 (show RBBP7 ELISA Kits) was discovered, leading to the possibility of a posttranslational modifications network involved in mRNP regulation.
C-terminal extension of Lsm4 interacts directly with the histone mRNP, contacting both SLBP (show SLBP ELISA Kits) and 3'hExo (show ERI1 ELISA Kits).
LSm1 (show LSM1 ELISA Kits)-7 proteins colocalize with DCP1 (show ACE ELISA Kits),DCP2 (show DCP2 ELISA Kits) and Xrn1 (show XRN1 ELISA Kits) in cytoplasmic foci
Data show that ICln159, a truncated ICln (show CLNS1A ELISA Kits) mutant, belongs to the pleckstrin (show PLEK ELISA Kits) homology (PH) domain family of proteins and interacts with LSm4, a protein involved in splicing and mRNA degradation.
LSm4 not only acts in RNA processing, but also as a co-factor in cell volume regulation.
This gene encodes a member of the LSm family of RNA-binding proteins. LSm proteins form stable heteromers that bind specifically to the 3'-terminal oligo(U) tract of U6 snRNA and may play a role in pre-mRNA splicing by mediating U4/U6 snRNP formation. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
U6 snRNA-associated Sm-like protein LSm4
, glycine-rich protein
, U6 snRNA-associated SM-like protein 4
, U6 snRNA-associated Sm-like protein 4