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HNRNPK belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). Additionally we are shipping Heterogeneous Nuclear Ribonucleoprotein K Antibodies (161) and Heterogeneous Nuclear Ribonucleoprotein K Kits (36) and many more products for this protein.
Showing 10 out of 16 products:
Human HNRNPK Protein expressed in Escherichia coli (E. coli) - ABIN1047168
Matunis, Michael, Dreyfuss: Characterization and primary structure of the poly(C)-binding heterogeneous nuclear ribonucleoprotein complex K protein. in Molecular and cellular biology 1992
Show all 2 references for ABIN1047168
Human HNRNPK Protein expressed in Wheat germ - ABIN1306879
Li, Liu: Identification of heterogeneous nuclear ribonucleoprotein K as a transactivator for human low density lipoprotein receptor gene transcription. in The Journal of biological chemistry 2010
Show all 2 references for ABIN1306879
hnRNP K binds miR (show MLXIP Proteins)-122, a mature liver-specific microRNA required for Hepatitis C virus replication.
The authors identified two new human proteins that interact with Ehrlichia chaffeensis EtpE-C: CD147 (show BSG Proteins) and heterogeneous nuclear ribonucleoprotein K (hnRNP-K).
Data show that proto-oncogene (show RAB1A Proteins) protein c-myc (show MYC Proteins) is upregulated by sumoylated heterogeneous nuclear ribonucleoprotein K (hnRNP K) at the translational level in Burkitt's lymphoma cells.
hnRNP K may be a key molecule involved in cell motility in RCC (show XRCC1 Proteins) cells
It describes the identification of heterogeneous nuclear ribonucleoprotein K (hnRNPK) as one of the composite element binding factors(CEBF) that acts as transactivator of PXR (show NR1I2 Proteins) promoter.
RTVP-1 (show GLIPR1 Proteins) regulates glioma cell spreading, migration and invasion and that these effects are mediated via interaction with N-WASP (show WASL Proteins) and by interfering with the inhibitory effect of hnRNPK on the function of this protein.
we investigate the role of hnRNP K in the radioresistance of malignant melanoma cells
These results indicate that dengue virus type 2 and Junin virus induce hnRNP K cytoplasmic translocation to favor viral multiplication.
Data implicate hnRNPK in the development of hematological disorders and suggest hnRNPK acts as a tumor suppressor.
Inhibition of CDK2 (show CDK2 Proteins) phosphorylation blocked phosphorylation of hnRNP K, preventing its incorporation into stress granules (SGs (show FBN1 Proteins)). Due to interaction between hnRNP K with TDP-43 (show TARDBP Proteins), the loss of hnRNP K from SGs (show FBN1 Proteins) prevented accumulation of TDP-43 (show TARDBP Proteins).
a previously unidentified function of phosphorylation at this phylogenetically conserved site and implicates hnRNPK as an intracellular molecular target of ERK (show MAPK1 Proteins)-mediated signaling in axon outgrowth.
hnRNP K is essential for successful optic axon regeneration via a novel post-transcriptional regulatory pathway.
A crucial role is reported for hnrpk in axon development in Xenoops laevis.
the cytoplasmic hnRNPK interacts with GSK3beta and regulates its function.
These findings functionally integrate K17 (show KRT17 Proteins), hnRNP K, and gene expression along with RSK (show RPS6KA1 Proteins) and CXCR3 (show CXCR3 Proteins) signaling in a keratinocyte-autonomous axis and provide a potential basis for their implication in tumorigenesis
Nova haploinsufficient mice had spontaneous epilepsy
HnRNP K-3' UTR complex inhibits TAK1 (show NR2C2 Proteins) mRNA translation.
hnRNP-K regulates extracellular matrix, cell motility, and angiogenesis pathways. Involvement of the selected genes (Cck (show CCK Proteins), Mmp-3 (show MMP3 Proteins), Ptgs2 (show PTGS2 Proteins), and Ctgf (show CTGF Proteins)) and pathways was validated by gene-specific expression analysis
HNRNPK affects production of the essential NEAT1_2 isoform by negatively regulating its 3'-end polyadenylation by arresting CFIm (show CPSF6 Proteins) complex binding near NEAT1_1's alternative polyadenylation site.
Mitochondrial superoxide production stimulated by adiponectin (show ADIPOQ Proteins) serves as a trigger to initiate the translocation of hnRNP K, which in turn promotes UCP2 (show UCP2 Proteins) expressions in liver.
the mutually antagonistic action of two RNA-binding proteins, Hu and hnRNP K, control the timing of the switch from proliferation to neuronal differentiation through the post-transcriptional regulation of p21 mRNA
insulin (show INS Proteins) activates the import of hnRNP K protein into mitochondria; overexpression of hnRNP K protein modulates insulin (show INS Proteins)-activated mitochondrial gene expression; and insulin (show INS Proteins) treatment stimulates binding of hnRNP K protein to mitochondrial DNA
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 is located in the nucleoplasm and has three repeats of KH domains that binds to RNAs. It is distinct among other hnRNP proteins in its binding preference\; it binds tenaciously to poly(C). This protein is also thought to have a role during cell cycle progession. Several alternatively spliced transcript variants have been described for this gene, however, not all of them are fully characterized.
heterogeneous nuclear ribonucleoprotein K
, heterogeneous nuclear ribonucleoprotein k
, heterogenous nuclear ribonucleoprotein K
, heterogeneous nuclear ribonucleoprotein K-like
, dC-stretch binding protein
, transformation upregulated nuclear protein
, hnRNP K
, dC stretch-binding protein
, hnRNP-K protein