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HNRNPC belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs).
Showing 10 out of 125 products:
Chicken Monoclonal HNRNPC Primary Antibody for ICC, IF - ABIN108590
Choi, Dreyfuss: Isolation of the heterogeneous nuclear RNA-ribonucleoprotein complex (hnRNP): a unique supramolecular assembly. in Proceedings of the National Academy of Sciences of the United States of America 1985
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Chicken Monoclonal HNRNPC Primary Antibody for ICC, IF - ABIN108591
Dreyfuss, Choi, Adam: Characterization of heterogeneous nuclear RNA-protein complexes in vivo with monoclonal antibodies. in Molecular and cellular biology 1984
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Dog (Canine) Polyclonal HNRNPC Primary Antibody for WB - ABIN2776586
Rual, Venkatesan, Hao, Hirozane-Kishikawa, Dricot, Li, Berriz, Gibbons, Dreze, Ayivi-Guedehoussou, Klitgord, Simon, Boxem, Milstein, Rosenberg, Goldberg, Zhang, Wong, Franklin, Li, Albala, Lim et al.: Towards a proteome-scale map of the human protein-protein interaction network. ... in Nature 2005
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APP levels then decrease progressively as a function of age in close relationship with the gradual normalization of FMRP and hnRNP C levels.
Endoplasmic reticulum resident chaperone GRP78 (show HSPA5 Antibodies), mitochondrial protein (show COX6B2 Antibodies) Prohibitin (show PHB Antibodies) and heterogeneous nuclear ribonucleoprotein (show PCBP2 Antibodies) hnRNPC (C1/C2) have been shown to interact with viral RNA. Hence it is proposed that these are the principle candidates governing endoplasmic reticulum stress-induced apoptosis in JEV infection.
Our results indicate that a balance between lncRNA SNHG1 and hnRNPC regulates p53 (show TP53 Antibodies) activity and p53 (show TP53 Antibodies)-dependent apoptosis upon doxorubicin treatment, and further indicate that a change in lncRNA subcellular localization under specific circumstances is biologically significant.
These data suggest an interplay between CELF2 (show CELF2 Antibodies) and hnRNP C as the mechanistic basis for activation-dependent alternative splicing of TRAF3 (show TRAF3 Antibodies) exon 8.
These findings suggest that hnRNP C1/C2 is involved in dengue virus replication at the stage of viral RNA synthesis.
HnRNP C, YB-1 (show YBX1 Antibodies) and hnRNP L (show HNRNPL Antibodies) coordinately enhance skipping of human MUSK (show MUSK Antibodies) exon 10 to generate a Wnt (show WNT2 Antibodies)-insensitive MuSK (show MUSK Antibodies) isoform.
Our results suggested that hnRNP C1 controls HPV16 late gene expression.
m(6)A-switch-regulated HNRNPC-binding activities affect the abundance as well as alternative splicing of target mRNAs, demonstrating the regulatory role of m(6)A-switches on gene expression and RNA maturation
PTBP1 (show PTBP1 Antibodies) and hnRNP C repress exon 3 inclusion, and that downregulation of PTBP1 (show PTBP1 Antibodies) inhibited BIM (show BCL2L11 Antibodies)-mediated apoptosis.
down-regulation of MALAT-1 expression compromised the cytoplasmic translocation of hnRNP C in the G2/M phase and resulted in G2/M arrest
hnRNP C and hnRNP H (show HNRNPH2 Antibodies) bind to the 3'-UTR (show UTS2R Antibodies) of the circadian clock gene Period 2 (mPer2 (show PER2 Antibodies)).
Neither hnRNP-C nor FMRP (show FMR1 Antibodies) is required for cyclic AMP (show TMPRSS5 Antibodies) to stimulate APP (show APP Antibodies) and Amyloid beta production.
our results reveal a new function of the splicing factor (show SLU7 Antibodies) hnRNP C in the maturation of dendritic cells that involves regulating the expression of NF-kappaB (show NFKB1 Antibodies) p65 (show NFkBP65 Antibodies) and its downstream targets CD80 (show CD80 Antibodies) and CD40 (show CD40 Antibodies).
CK1alpha-mediated phosphorylation modulates the mRNA binding ability of hnRNP-C
Data suggest that increased levels of hnRNP C1/C2 may modulate XIAP (show XIAP Antibodies) translation by interacting with the XIAP (show XIAP Antibodies)-IRES, and may foster synthesis of XIAP (show XIAP Antibodies) as a protective pathway by which neurons try to counteract the initial deleterious effects of apoptosis.
This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene can act as a tetramer and is involved in the assembly of 40S hnRNP particles. Multiple transcript variants encoding at least two different isoforms have been described for this gene.
heterogeneous nuclear ribonucleoproteins C1/C2
, hnRNP C1/C2
, nuclear ribonucleoprotein particle C1 protein
, nuclear ribonucleoprotein particle C2 protein
, heterogeneous nuclear ribonucleoprotein C (C1/C2)
, heterogeneous nuclear ribonucleoprotein C1
, heterogeneous nuclear ribonucleoprotein C2
, heterogeneous ribonucleoprotein C1/C2
, hnRNP C1 / hnRNP C2
, hnRNP C2
, snoRNA MBI-122
, heterogeneous nuclear ribonucleoprotein C
, hnRNP C protein C-terminal fragment (158 AA)
, hnRNP core protein C
, hnRNP C
, C protein