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This intronless gene is thought to have been generated by retrotransposition of a fully processed PCBP-2 mRNA. Additionally we are shipping PCBP1 Antibodies (117) and PCBP1 Kits (4) and many more products for this protein.
Showing 8 out of 9 products:
Study report a novel interaction between mutant HSPB1 (show HSPB1 Proteins)-P182L and the RNA binding protein (show PTBP1 Proteins) PCBP1, leading to a reduction in its translational repression activity. Identifying PCBP1 mRNA targets revealed a marked prevalence for an RNA recognition motif, preferably seen in their 5' and 3'UTRs. Findings further support a role for mutant HSPB1 (show HSPB1 Proteins) in neurodegenerative diseases.
It is reported here that TGF-beta (show TGFB1 Proteins) directly regulates alternative splicing of cancer stem cell marker CD44 (show CD44 Proteins) through a phosphorylated threonine179 of SMAD3 (show SMAD3 Proteins)-mediated interaction with RNA-binding protein (show PTBP1 Proteins) PCBP1.
our findings suggest that PCBP1 is a molecular marker of oxaliplatin resistance in colorectal cancer
Data suggest a 216-nucleotide proximal cis (show CISH Proteins)-element in LIF (show LIF Proteins) mRNA exhibits mRNA destabilizing potential; on exposure to carcinogen PMA (phorbol-12-myristate-13-acetate), this cis (show CISH Proteins)-element exhibits mRNA stabilizing activity. PMA induces nucleo-cytoplasmic translocation of both nucleolin (show NCL Proteins) and PCBP1, 2 trans-acting factors that bind to and stabilize LIF (show LIF Proteins) mRNA. [LIF (show LIF Proteins) = leukemia inhibitory factor (show LIF Proteins); PCBP1 = poly(rC) binding protein 1]
It was concluded that a novel positive feedback loop amplifies hnRNP-E1 during prolonged folate deficiency and thereby maximizes upregulation of folate receptors in order to restore folate homeostasis toward normalcy in placental cells.
TGF-beta (show TGFB1 Proteins) signaling through Akt2 (show AKT2 Proteins) induces phosphorylation of heterogeneous nuclear ribonucleoprotein E1 (hnRNP E1) at serine-43 (p-hnRNP E1), driving epithelial to mesenchymal transition and metastasis.
These results establish the role of hnRNP K and PCPB1 in the translational control of morphine-induced MOR expression in human neuroblastoma (NMB) cells as well as cells stably expressing MOR (NMB1).
The results provide a mechanism for exon 16 3' splice site activation in which a coordinated effort among TIA1 (show TIA1 Proteins), Pcbp1, and RBM39 (show RBM39 Proteins) stabilizes or increases U2 snRNP (show LSM2 Proteins) recruitment, enhances spliceosome A complex formation, and facilitates exon definition through RBM39 (show RBM39 Proteins)-mediated splicing regulation.
BC200 RNA interacts with hnRNP E1 and E2 mainly through its unique 3' C-rich domain.
Low expression of PCBP1 is associated with lung cancer metastasis.
Study report a novel interaction between mutant HSPB1 (show HSPB1 Proteins)-P182L and the RNA binding protein PCBP1, leading to a reduction in its translational repression activity. Identifying PCBP1 mRNA targets revealed a marked prevalence for an RNA recognition motif, preferably seen in their 5' and 3'UTRs. Findings further support a role for mutant HSPB1 (show HSPB1 Proteins) in neurodegenerative diseases.
These studies demonstrate the importance of ferritin (show FTL Proteins) for the vectorial transfer of imported iron to mitochondria in developing red cells and of PCBP1 and NCOA4 (show NCOA4 Proteins) in mediating iron flux through ferritin (show FTL Proteins).
Pcbp1 modulated the processing of muscle-enriched miR-1, miR (show MLXIP Proteins)-133, and miR (show MLXIP Proteins)-206 by physically interacting with argonaute 2 (AGO2 (show EIF2C2 Proteins)) and other miRNA pathway components.
These data reveal that Pcbp1 and Pcbp2 (show PCBP2 Proteins) are individually essential for mouse embryonic development and have distinct impacts on embryonic viability and that Pcpb2 has a nonredundant in vivo role in hematopoiesis.
PCBP1 may serve as a novel maternal factor (show ZAR1 Proteins).
Our analysis of PCBP1 and PCBP2 (show PCBP2 Proteins) expression demonstrates robust expression of these two proteins within the gastric epithelium with high concordance for both proteins in their cell-type specificities and intracellular distributions.
knockdown of PCBP1 led to a reversal effect on the transcriptional inactivation during oocyte growth, which highlights the important role of PCBP1 in maintaining the gobal transcriptional silencing when the growth phase is completed
TGF-beta (show TGFB1 Proteins) modulates the expression of Dab2 (show DAB2 Proteins) and ILEI (show FAM3C Proteins) mRNA required for epithelial-mesenchymal transdifferentiation by inducing phosphorylation of hnRNP E1, resulting in its release from a structural, 33-nucleotide BAT (show BAAT Proteins) element in the 3'UTR of Dab2 (show DAB2 Proteins) and ILEI (show FAM3C Proteins).
To define the mechanism of STAT3C suppression of transcript. and/or translational activity of NF-kappaB (show NFKB1 Proteins) we found that a alphaCP-1 interacted with STAT3C. alphaCP-1 is a K-homol. domain-containing RNA-binding prot (show SLC6A7 Proteins) with specific for C-rich pyrimidine tracts
This intronless gene is thought to have been generated by retrotransposition of a fully processed PCBP-2 mRNA. This gene and PCBP-2 have paralogues (PCBP3 and PCBP4) which are thought to have arisen as a result of duplication events of entire genes. The protein encoded by this gene appears to be multifunctional. It along with PCBP-2 and hnRNPK corresponds to the major cellular poly(rC)-binding protein. It contains three K-homologous (KH) domains which may be involved in RNA binding. This encoded protein together with PCBP-2 also functions as translational coactivators of poliovirus RNA via a sequence-specific interaction with stem-loop IV of the IRES and promote poliovirus RNA replication by binding to its 5'-terminal cloverleaf structure. It has also been implicated in translational control of the 15-lipoxygenase mRNA, human Papillomavirus type 16 L2 mRNA, and hepatitis A virus RNA. The encoded protein is also suggested to play a part in formation of a sequence-specific alpha-globin mRNP complex which is associated with alpha-globin mRNA stability.
poly(rC) binding protein 1
, poly(rC)-binding protein 1-like
, heterogeneous nuclear ribonucleoprotein E1
, heterogenous nuclear ribonucleoprotein E1
, heterogenous nuclear ribonucleoprotein X
, nucleic acid-binding protein SUB2.3
, poly(rC)-binding protein 1
, hnRNP-E1 protein
, hnRNP E1