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The protein encoded by PCBP2 appears to be multifunctional. Additionally we are shipping PCBP2 Proteins (9) and and many more products for this protein.
Showing 10 out of 63 products:
Human Monoclonal PCBP2 Primary Antibody for IF, IHC (p) - ABIN562121
Fujimura, Kano, Murata: Identification of PCBP2, a facilitator of IRES-mediated translation, as a novel constituent of stress granules and processing bodies. in RNA (New York, N.Y.) 2008
Show all 9 Pubmed References
Cow (Bovine) Polyclonal PCBP2 Primary Antibody for IHC, WB - ABIN2778923
Oh, Yang, Hahn, Kim, Byun, Jeon, Kim, Song, Noh, Kim, Yoo, Kim, Kim: Transcriptome analysis of human gastric cancer. in Mammalian genome : official journal of the International Mammalian Genome Society 2005
Show all 3 Pubmed References
Human Monoclonal PCBP2 Primary Antibody for ELISA, WB - ABIN394008
Kim, Chang, Yun, Yang, Hong, Kim, Um, Lee, Lee, Hwang: Chloride intracellular channel 1 identified using proteomic analysis plays an important role in the radiosensitivity of HEp-2 cells via reactive oxygen species production. in Proteomics 2010
Human Polyclonal PCBP2 Primary Antibody for ICC, IF - ABIN4344023
Flynn, Martin, Spitale, Do, Sagan, Zarnegar, Qu, Khavari, Quake, Sarnow, Chang: Dissecting noncoding and pathogen RNA-protein interactomes. in RNA (New York, N.Y.) 2014
PCBP2 expression was markedly increased in higher stages of glioblastoma compared with those in lower stages; further research suggested that PCBP2 upregulation was connected with poorer prognosis in patients with glioblastoma
Double immunofluorescence for hnRNP E2 and TDP-43 (show TARDBP Antibodies) showed most TDP-43 (show TARDBP Antibodies) immunopositive dystrophic neuritis within frontal and temporal cortex, and the neuronal cytoplasmic inclusions seen in dentate gyrus granule cells, to contain hnRNP E2. Present findings indicate an association between TDP-43 (show TARDBP Antibodies) and hnRNP E2 which might underlie the pathogenetic mechanism of Semantic Dementia Frontotemporal Lobar Degeneration.
Data suggest that the interaction between PCBP2 and the 3'UTR (show UTS2R Antibodies) of the ARHGDIA (show ARHGDIA Antibodies) mRNA may induce a local change in RNA structure that favors subsequent binding of miR (show MLXIP Antibodies)-151-5p and miR-16 (show GDE1 Antibodies), thus leading to the suppression of ARHGDIA (show ARHGDIA Antibodies) expression.
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 Antibodies) for binding HO1 (show HMOX1 Antibodies); PCBP2 K homology 3 domain is important for HO1 (show HMOX1 Antibodies)/PCBP2 interaction; heme prompts HO1 (show HMOX1 Antibodies)/CPR (show POR Antibodies) multimer and decreases HO1 (show HMOX1 Antibodies)/PCBP2 multimer. [PCBP2 = poly(rC) binding protein 2; CPR (show POR Antibodies) = cytochrome P450 reductase (show POR Antibodies); HO1 (show HMOX1 Antibodies) = heme oxidase 1]
BC200 RNA interacts with hnRNP E1 (show PCBP1 Antibodies) 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 Antibodies) 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 Antibodies)-214 may function as tumor suppressor in glioma by targeting PCBP2
data suggest that PCBP2 regulates p73 (show ARHGAP24 Antibodies) expression via mRNA stability and p73 (show ARHGAP24 Antibodies)-dependent biological function in ROS (show ROS1 Antibodies) production and cellular senescence.
PCBP2 overexpression rescues the Meis1 (show MEIS1 Antibodies) effects of Akt (show AKT1 Antibodies)-mTOR (show FRAP1 Antibodies) pathway and hypertrophy of cardiomyocytes.
These data reveal that Pcbp1 (show PCBP1 Antibodies) 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.
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.
Our analysis of PCBP1 (show PCBP1 Antibodies) 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 Antibodies) 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 Antibodies) axis defines a new signaling cascade for MAVS (show MAVS Antibodies) 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 Antibodies) 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.
, heterogeneous nuclear ribonucleoprotein E2
, heterogenous nuclear ribonucleoprotein E2
, hnRNP E2
, poly(rC)-binding protein 2
, heterogeneous nuclear ribonucleoprotein X
, hnRNP X
, putative heterogeneous nuclear ribonucleoprotein X
, poly(rC) binding protein 2
, poly(rC) binding protein 3
, PolyrC-binding protein 2
, poly(rc)-binding protein 2
, heterogeneous nuclear ribonucleoprotein