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anti-Human HIPK2 Antibodies:
anti-Mouse (Murine) HIPK2 Antibodies:
anti-Rat (Rattus) HIPK2 Antibodies:
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Cow (Bovine) Polyclonal HIPK2 Primary Antibody for IHC, WB - ABIN2779735
Steinmann, Schulte, Beck, Chachra, Bujnicki, Klempnauer: v-Myc inhibits C/EBPbeta activity by preventing C/EBPbeta-induced phosphorylation of the co-activator p300. in Oncogene 2009
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Human Monoclonal HIPK2 Primary Antibody for ICC, IF - ABIN2668288
Isono, Nemoto, Li, Takada, Suzuki, Katsuki, Nakagawara, Koseki: Overlapping roles for homeodomain-interacting protein kinases hipk1 and hipk2 in the mediation of cell growth in response to morphogenetic and genotoxic signals. in Molecular and cellular biology 2006
Human Polyclonal HIPK2 Primary Antibody for EIA - ABIN358542
Guha, Chaerkady, Marimuthu, Patterson, Kashyap, Harsha, Sato, Bader, Lash, Minna, Pandey, Varmus: Comparisons of tyrosine phosphorylated proteins in cells expressing lung cancer-specific alleles of EGFR and KRAS. in Proceedings of the National Academy of Sciences of the United States of America 2008
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Human Monoclonal HIPK2 Primary Antibody for ELISA, WB - ABIN565400
Esposito, Tornincasa, Chieffi, De Martino, Pierantoni, Fusco: High-mobility group A1 proteins regulate p53-mediated transcription of Bcl-2 gene. in Cancer research 2010
Hipk2 promotes PP1c-mediated Dvl dephosphorylation via its C-terminal domain and is essential Dvl stability.
Decreased HIPK2 expression indicated worse prognosis of pancreatic cancer. Overexpression of HIPK2 in pancreatic cancer cells decreased cell proliferation and attenuated aerobic glycolysis, which sustained proliferation of cancer cells. HIPK2 decreased cMyc protein levels and expression of cMyc-targeted glycolytic genes.
The data confirm a key role for HIPK2 and H2B in cytokinesis and offer the possibility of testing HIPK2 and extrachromosomal histone H2B as therapeutic targets for inhibition of cell division.
HIPK1, HIPK2 and HIPK3 interact with the components of the carbon catabolite repressor 4 (CCR4)-negative on TATA (NOT) complex, an important regulator of all the major steps in the mRNA metabolism. it has emerged that HIPKs and their related miRNAs are involved in diabetic nephropathy, gastric cancer chemoresistance, cervical cancer progression, and recombinant protein expression in cultured cells. [Review]
The downregulation of miR-197 suppresses the EMT and migration ability. HIPK2 is a direct functional target of miR-197 in LAD metastasis. In summary, miR-197 controls EMT and metastasis by directly silencing HIPK2.
Immunoprecipitation and pulldown experiments identified DCAF7 as an adaptor for the association of the adenovirus E1A protein with DYRK1A and HIPK2
HIPK2 polymorphisms rs2058265, rs6464214, and rs7456421 may have a role in kidney stone disease in Chinese males
HIPK2 overexpression may be a potential prognostic marker for predicting prognoses and a high risk of recurrence, particularly in patients with HPV-positive Tonsillar squamous cell carcinomas.
Furthermore, our results suggest that modulation of either HIPK2 levels or activity could be exploited to impair NRF2-mediated signalling in cancer cells, and thus sensitise them to chemotherapeutic drugs.
PARP1 can modulate the tumor-suppressing function of HIPK2 by regulating the protein stability of HIPK2.
Data show that HIPK2-T566 phosphorylation contributes to UV-induced HIPK2 activity but it is dispensable for doxorubicin response.
In this study, we report that the kinase HIPK2 is responsible for facilitating the Fbw7-dependent proteasomal degradation of Notch1 by phosphorylating its intracellular domain (Notch1-IC) within the Cdc4 phosphodegron motif.
the migration and invasion of hepatocellular carcinoma cells were impaired by knockdown of histone deacetylase 5 or hypoxia-inducible factor-1alpha but rescued when eliminating homeodomain-interacting protein kinase-2 in hepatocellular carcinoma cells, which suggested the critical role of histone deacetylase 5-homeodomain-interacting protein kinase-2-hypoxia-inducible factor-1alpha pathway in hypoxia-induced metastasis.
These results suggest that the HIPK2-phospho-Ser271 CREB axis is a new arsenic-responsive CREB activation mechanism in parallel with the PKA-phospho-Ser133 CREB axis.
Results demonstrated that HIPK2 may function as a novel regulator to modulate hepatic stellate cells activation, potentially by inhibiting the TGF-beta1/Smad3 signaling pathway.
Data show strong reduction of cell viability was induced in vitro and in vivo by the homeodomain interacting protein kinase 2 exon 8 spliced isoform (Hipk2-Deltae8)-specific siRNA, supporting a potential therapeutic application.
Results indicate that Hipk2 exerts a relevant role in the survival of cerebellar Purkinje cells and that Hipk2 genetic ablation generates cerebellar dysfunction compatible with an ataxic-like phenotype.
Our findings indicate that phosphorylation-dependent restriction of SIRT1 activity by HIPK2 shapes the p53 response
The findings highlight a complex regulation of CREB-binding protein activity by HIPK2, which might be relevant for the control of specific sets of target genes involved in cellular proliferation, differentiation and apoptosis.
MDM4/HIPK2/p53 cytoplasmic assembly uncovers coordinated repression of molecules with anti-apoptotic activity during early DNA damage response.
Results indicate that HIPK2 acts as a caretaker gene, whose inactivation increases tumorigenicity and causes chromosomal instability by cytokinesis failure.
Data suggest that the absence of phosphorylation at Y361 changes the HIPK2 structure, perturbs its stability, decreases its activity and affects its capability to interact with partners and with itself, increasing its tendency to form aggregates.
Protein levels of HIPK2 were increased in high glucose or TGF-beta-treated mouse glomerular mesangial cells. The HG- or TGF-beta-induced upregulation of p-MeCP2, NOX4 and primary miR-25, but downregulation of precursor and mature miR-25, were attenuated by Hipk2 siRNA. The SIAH1/HIPK2/MeCP2 axis played a novel role for in suppressing miR-25 processing and thereby upregulating NOX4 in early diabetic nephropathy.
Novel insights regarding the specific contribution of circHIPK2 to astrocyte activation in the context of drug abuse as well as for the treatment of a broad range of neuroinflammatory disorders.
reveal a previously unrecognized role of HIPK2 activation in ER-stress-mediated neurodegeneration and its potential role as a biomarker and therapeutic target for amyotrophic lateral sclerosis
HIPK2 is ubiquitinated upon heat shock.
Phosphorylation of KLF3 and CtBP2 by HIPK2 strengthens the interaction between these two factors and increases transcriptional repression by KLF3.
Homeodomain-interacting protein kinase 2, a novel autoimmune regulator interaction partner, modulates promiscuous gene expression in medullary thymic epithelial cells.
Hipk2 has an essential role in mouse white fat development
data identify Hipk2 as a novel regulator of C/EBPbeta and implicate different protein kinases in the cooperation of p300 with C/EBPbeta and C/EBPalpha
Data indicate a critical kinase HIPK2 function in cytokinesis and in the prevention of tetraploidization.
Hipk2 is a haploinsufficient tumor suppressor gene for mouse lymphoma development.
HIPK2 is an important transcriptional cofactor that regulates bone morphogenetic protein signaling in the maintenance of enteric neurons and glia.
HIPK2-mediated phosphorylation of PDX1 at Ser-269 might be a regulatory mechanism connecting signals generated by changes in extracellular glucose concentration to downstream effectors, thereby influencing islet cell differentiation and function.
Expression of Hipk2 in the mouse nucleus accumbens is modulated by a sequence variant (B2 SINE indel) in the 3' UTR of Comt (catechol-O-methyltransferase).
Hipk2 plays an important role in some but not all aspects of normal terminal erythroid differentiation.
FLT3 and CD43 signaling pathways involve STAT5A via Fiz1 and Hipk2 in B lymphoblastic lymphomas.
HIPK2 appears to function as a novel negative regulator of beta-catenin through its phosphorylation and proteasomal degradation.
activates p53 by directly phosphorylating it at Ser 46
This gene encodes a conserved serine/threonine kinase that is a member of the homeodomain-interacting protein kinase family. The encoded protein interacts with homeodomain transcription factors and many other transcription factors such as p53, and can function as both a corepressor and a coactivator depending on the transcription factor and its subcellular localization. Multiple transcript variants encoding different isoforms have been found for this gene.
homeodomain interacting protein kinase 2
, serine/threonine protein kinase
, homeodomain-interacting protein kinase 2-like
, homeodomain-interacting protein kinase 2
, homeodomain-interacting protein kinase-2
, nuclear body-associated kinase 1
, sialophorin tail-associated nuclear serine/threonine-protein kinase
, Mx-interacting protein kinase PKM