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Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and t. Additionally we are shipping SFRS Protein Kinase 2 Proteins (14) and many more products for this protein.
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Human Polyclonal SRPK2 Primary Antibody for EIA, IHC (p) - ABIN359708
Cantrell: Phosphoinositide 3-kinase signalling pathways. in Journal of cell science 2001
Dog (Canine) Monoclonal SRPK2 Primary Antibody for IF, WB - ABIN968376
Wang, Lin, Dyck, Yeakley, Songyang, Cantley, Fu: SRPK2: a differentially expressed SR protein-specific kinase involved in mediating the interaction and localization of pre-mRNA splicing factors in mammalian cells. in The Journal of cell biology 1998
SRPK2 may contribute to the formation of hyperphosphorylated tau and the pathogenesis of Alzheimer disease.
Interaction of Akt (show AKT1 Antibodies)-phosphorylated SRPK2 with 14-3-3 (show YWHAQ Antibodies) mediates cell cycle and cell death in neurons.
Data indicate serine/arginine-rich protein (show MANF Antibodies) kinases SRPK1 (show SRPK1 Antibodies)/2/SRPIN340 complexes by molecular docking and molecular dynamics.
A conserved electronegative docking groove in SRPK2 is responsible for substrate binding.
the BLRF2 RS motif is phosphorylated by SRPK2 and is important for viral replication.
Our results demonstrate that SRPK1 (show SRPK1 Antibodies) and SRPK2 are host factors essential for Hepatitis C virus replication.
Short-term exercise resulted in a significant increase of mRNA expression of genes encoding proteins involved in the formation of precatalytic splisosome: SRPK2.
Both SRPK1 and SRPK2 are most likely the cellular protein kinases mediating HBV core protein phosphorylation during viral infection and therefore represent important host cell targets for therapeutic intervention in HBV infection.
negative role of SRPK1 and SRPK2 in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein
SRPK2 knock down results in hypophosphorylation of the arginine-serine (RS) domain-containing human PRP28 (show DDX23 Antibodies) protein (PRP28 (show DDX23 Antibodies), also known as DDX23 (show DDX23 Antibodies)), and destabilizes PRP28 (show DDX23 Antibodies) association with the tri (show VANGL2 Antibodies)-snRNP (show LSM2 Antibodies).
overexpression of SRPK2 is associated with phosphorylating acinus (show ACIN1 Antibodies) and regulating its stimulatory effects on cyclin A1 (show CCNA1 Antibodies) expression, contributing to leukemia cell proliferation
Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Promotes neuronal apoptosis by up-regulating cyclin-D1 (CCND1) expression. This is done by the phosphorylation of SRSF2, leading to the suppression of p53/TP53 phosphorylation thereby relieving the repressive effect of p53/TP53 on cyclin-D1 (CCND1) expression. Phosphorylates ACIN1, and redistributes it from the nuclear speckles to the nucleoplasm, resulting in cyclin A1 but not cyclin A2 up- regulation. Plays an essential role in splicesomal B complex formation via the phosphorylation of DDX23/PRP28.
SFRS protein kinase 2
, SFRS protein kinase 3
, serine/threonine-protein kinase SRPK2-like
, SR-protein-specific kinase 2
, SRSF protein kinase 2
, WW domain binding protein 6
, serine/arginine-rich protein-specific kinase 2
, serine/threonine-protein kinase SRPK2
, SR protein kinase 2
, serine kinase SRPK2
, serine/arginine-rich splicing factor kinase 2
, serine/arginine-rich protein specific kinase 2