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LSM4 encodes a member of the LSm family of RNA-binding proteins. Additionally we are shipping LSM4 Antibodies (41) and many more products for this protein.
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Human LSM4 Protein expressed in Escherichia coli (E. coli) - ABIN667317
Brahms, Meheus, de Brabandere, Fischer, Lührmann: Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B' and the Sm-like protein LSm4, and their interaction with the SMN protein. in RNA (New York, N.Y.) 2001
Show all 2 references for 667317
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 Proteins) and RBBP7 (show RBBP7 Proteins) 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 Proteins) and 3'hExo (show ERI1 Proteins).
LSm1 (show LSM1 Proteins)-7 proteins colocalize with DCP1 (show ACE Proteins),DCP2 (show DCP2 Proteins) and Xrn1 (show XRN1 Proteins) in cytoplasmic foci
Data show that ICln159, a truncated ICln (show CLNS1A Proteins) mutant, belongs to the pleckstrin (show PLEK Proteins) 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