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HNRNPLL is a master regulator of activation-induced alternative splicing in T cells. Additionally we are shipping Heterogeneous Nuclear Ribonucleoprotein L-Like Antibodies (43) and Heterogeneous Nuclear Ribonucleoprotein L-Like Kits (21) and many more products for this protein.
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Loss-of-function mutati (show PTPRC Proteins)on of hnRNPLL disrupts peripheral T cell accumulation even in the absence of CD45 protein, indicating that hnRNPLL acts through an independent mechanism to promote (show PTPRC Proteins)peripheral T cell longevity.
Participation of SRRF (Stromal RNA Regulating Factor) isoforms in post-transcriptional events in bone marrow stromal cells; an important role in regulation of the RNA expression that directs the bone marrow stromal cells differentiation pathway
identification of heterogeneous ribonucleoprotein L-like (hnRNPLL) as a critical inducible regulator of CD45 (show PTPRC Proteins) alternative splicing
These data establish that hnRNP (show HNRNPC Proteins) LL plays a critical and unique role in the signal-induced regulation of CD45 (show PTPRC Proteins) and demonstrate the utility of cell-based screens for the identification of novel splicing regulatory factors.
We identify similar patterns of hnRNPLL-induced differential intron retention flanking alternative exons in 14 other genes, representing novel elements of the hnRNPLL-induced splicing program in T cells.
Data indicate that the RNA-binding protein hnRNPLL has a critical role in tuning transcriptomes of terminally differentiating B lymphocytes.
The splicing factor hnRNPLL and the transcription elongation factor ELL2 modulate the ratio of secred versus membrane-encoding Ighg2b transcripts at the expense of the secreted isoform.
results highlight both overlapping and divergent roles for hnRNPLL between conventional T cells and NKT (show CTSL1 Proteins) cells
In T cells with no CD45 (show PTPRC Proteins) protein, hnRNPLL mutation diminishes peripheral T cell accumulation and demonstrates that hnRNPLL regulates T cell longevity independently from its effects on CD45 (show PTPRC Proteins) splicing.
A single substitution in a memory-induced RNA-binding protein, hnRNPLL, destabilized an RNA-recognition domain that bound with micromolar affinity to RNA containing the Ptprc (show PTPRC Proteins) exon-silencing sequence.
HNRNPLL is a master regulator of activation-induced alternative splicing in T cells. In particular, it alters splicing of CD45 (PTPRC\; MIM 151460), a tyrosine phosphatase essential for T-cell development and activation (Oberdoerffer et al., 2008
heterogeneous nuclear ribonucleoprotein L-like
, Heterogeneous nuclear ribonucleoprotein L-like
, stromal RNA regulating factor
, stromal RNA-regulating factor