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The protein encoded by PCBP2 appears to be multifunctional. Additionally we are shipping PCBP2 Antibodies (62) and PCBP2 Proteins (9) and many more products for this protein.
To promote intracellular iron flux, an iron chaperone appears to be essential for receiving iron from heme catabolism. Data suggest that PCBP2 competes with CPR (show POR ELISA Kits) for binding HO1 (show HMOX1 ELISA Kits); PCBP2 K homology 3 domain is important for HO1 (show HMOX1 ELISA Kits)/PCBP2 interaction; heme prompts HO1 (show HMOX1 ELISA Kits)/CPR (show POR ELISA Kits) multimer and decreases HO1 (show HMOX1 ELISA Kits)/PCBP2 multimer. [PCBP2 = poly(rC) binding protein 2; CPR (show POR ELISA Kits) = cytochrome P450 reductase (show POR ELISA Kits); HO1 (show HMOX1 ELISA Kits) = heme oxidase 1]
BC200 RNA interacts with hnRNP E1 (show PCBP1 ELISA Kits) and E2 mainly through its unique 3' C-rich domain.
Study determined that PCBP2 specifically associates with components of this kinase cascade and regulates the activities of its downstream transcriptional coactivators.
These results suggest that FPN1 (show SLC40A1 ELISA Kits) exports iron received from the iron chaperone PCBP2. Therefore, it was found that PCBP2 modulates cellular iron export, which is an important physiological process.
PCBP2 was overexpressed in esophageal squamous cell carcinoma tissues and cell lines. PCBP2 expression promoted proliferation of ESCC cells. We also found that reduced PCBP2 expression might induce ESCC cell apoptosis with increased cleaved caspase3 expression. Overall, our findings indicated that PCBP2 might be involved in the ESCC progression and be considered as a new treatment target in ESCC.
High expression of PCBP2 may contribute to sorafenib resistance in hepatocellular carcinoma cells.
our data indicate that miR (show MLXIP ELISA Kits)-214 may function as tumor suppressor in glioma by targeting PCBP2
beta2-adrenergic receptor (show ADRB2 ELISA Kits) signaling promotes pancreatic ductal adenocarcinoma progression by facilitating PCBP2-dependent c-myc (show MYC ELISA Kits) expression.
PCBP2 knockdown promoted angiotensin II-induced hypertrophy (increase in cell size, protein synthesis and activation of fetal genes) of cardiomyocytes, while PCBP2 overexpression obtained oppose effects.
Protein and mRNA levels of PCBP2 were down-regulated under insulin (show INS ELISA Kits)-resistant conditions. Over-expression of PCBP2 inhibits HIF1alpha (show HIF1A ELISA Kits) and STAT3 (show STAT3 ELISA Kits) pathway.
data suggest that PCBP2 regulates p73 (show ARHGAP24 ELISA Kits) expression via mRNA stability and p73 (show ARHGAP24 ELISA Kits)-dependent biological function in ROS (show ROS1 ELISA Kits) production and cellular senescence.
PCBP2 overexpression rescues the Meis1 (show MEIS1 ELISA Kits) effects of Akt (show AKT1 ELISA Kits)-mTOR (show FRAP1 ELISA Kits) pathway and hypertrophy of cardiomyocytes.
These data reveal that Pcbp1 (show PCBP1 ELISA Kits) and Pcbp2 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.
Our analysis of PCBP1 (show PCBP1 ELISA Kits) and PCBP2 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.
This study demonstrates for the first time that alpha-CP2 functions as a transcriptional activator by binding to a single-stranded poly(C) sequence.
This study provides evidence that PCBP2 and hnRNP A1 (show HNRNPA1 ELISA Kits) bind to the 5' and 3' ends of the murine norovirus 1 viral RNA and contribute to RNA circularization, playing a role in the virus life cycle.
PCBP2-AIP4 (show ITCH ELISA Kits) axis defines a new signaling cascade for MAVS (show MAVS ELISA Kits) degradation and 'fine tuning' of antiviral innate immunity.
These results indicated that Nsp1beta of porcine reproductive and respiratory syndrome virus is able to bind and interact with cellular PCBP2 strongly in both the infected cells and plasmid transfected cells.
Overall, the results presented here point toward an important role for PCBP1 (show PCBP1 ELISA Kits) and PCBP2 in regulating porcine reproductive and respiratory syndrome virus RNA synthesis via binding to viral nonstructural protein 1beta.
The protein encoded by this gene appears to be multifunctional. Along with PCBP-1 and hnRNPK, it is one of the major cellular poly(rC)-binding proteins. The encoded protein contains three K-homologous (KH) domains which may be involved in RNA binding. Together with PCBP-1, this protein also functions as a translational coactivator of poliovirus RNA via a sequence-specific interaction with stem-loop IV of the IRES, promoting 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. This multiexon structural mRNA is thought to be retrotransposed to generate PCBP-1, an intronless gene with functions similar to that of PCBP2. This gene and PCBP-1 have paralogous genes (PCBP3 and PCBP4) which are thought to have arisen as a result of duplication events of entire genes. Thsi gene also has two processed pseudogenes (PCBP2P1 and PCBP2P2). Multiple transcript variants encoding different isoforms have been found for this gene.
poly(rC) binding protein 2
, poly(rC) binding protein 3
, poly(rC)-binding protein 2
, PolyrC-binding protein 2
, poly(rc)-binding protein 2
, heterogeneous nuclear ribonucleoprotein E2
, heterogenous nuclear ribonucleoprotein E2
, hnRNP E2
, heterogeneous nuclear ribonucleoprotein X
, hnRNP X
, putative heterogeneous nuclear ribonucleoprotein X
, heterogeneous nuclear ribonucleoprotein