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electromechanical responses of cardiomyocytes to individual and combined components of ischemia. Can. J. Physiol. Pharmacol, 80: 1145-1157 2003.- Schaeffer, C., D. Vandroux, L. Thomassin, P. Athias, L. Rochette and J. L. Connat. Calcitonin gene-related peptide partly protects cultured smooth muscle cells from apoptosis induced by an oxidative stress via activation of ERK1/2 MAPK. Biochim Biophys Acta 1643(1-3): 65-73. 2004.- Chantome, A., A. Pance, N. Gauthier, D. Vandroux, J. Chenu, E. Solary, J. F. Jeannin and S. Reveneau. Casein kinase II-mediated phosphorylation of NF-kB p65 subunit enhances inducible nitric oxide synthase gene transcription in vivo. J Biol Chem. 279(23): 23953-60. 2004.- Gambert, S., S. Bes-Houtmann, D. Vandroux, C. Tissier, C. Vergely-Vandriesse, L. Rochette and P. Athias. Deep hypothermia during ischemia improves functional recovery and reduces free-radical generation in isolated reperfused rat heart. J Heart Lung Transplant 23(4): 487-91. 2004.- Vandroux, D., C. ...
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TY - JOUR. T1 - Epigenetic regulation of gene expression by Ikaros, HDAC1 and Casein Kinase II in leukemia. AU - Song, Chunhua. AU - Pan, X.. AU - Ge, Z.. AU - Gowda, Chandrika. AU - Ding, Y.. AU - Li, H.. AU - Li, Z.. AU - Yochum, Gregory. AU - Muschen, M.. AU - Li, Q.. AU - Payne, K. J.. AU - Dovat, Sinisa. PY - 2016/6/1. Y1 - 2016/6/1. UR - http://www.scopus.com/inward/record.url?scp=84955311527&partnerID=8YFLogxK. UR - http://www.scopus.com/inward/citedby.url?scp=84955311527&partnerID=8YFLogxK. U2 - 10.1038/leu.2015.331. DO - 10.1038/leu.2015.331. M3 - Letter. VL - 30. SP - 1436. EP - 1440. JO - Leukemia. JF - Leukemia. SN - 0887-6924. IS - 6. ER - ...
The IUPHAR/BPS Guide to Pharmacology. casein kinase II inhibitor III ligand page. Quantitative data and detailed annnotation of the targets of licensed and experimental drugs.
This gene encodes a member of the potassium channel, voltage-gated, shaker-related subfamily. The encoded protein is one of the beta subunits, which are auxiliary proteins associating with functional Kv-alpha subunits. The encoded protein forms a heterodimer with the potassium voltage-gated channel, shaker-related subfamily, member 5 gene product and regulates the activity of the alpha subunit. [provided by RefSeq, May 2012 ...
CK2 is an extremely pleiotropic Ser/Thr protein kinase, responsible for the generation of a large proportion of the human phosphoproteome and implicated in a wide variety of biological functions. CK2 plays a global role as an anti-apoptotic agent, a property which is believed to partially account for the addiction of many cancer cells to high CK2 levels. To gain information about the CK2 targets whose phosphorylation is primarily implicated in its pro-survival signaling advantage has been taken of quinalizarin (QZ) a cell permeable fairly specific CK2 inhibitor, previously shown to be able to block endogenous CK2 triggering an apoptotic response. HEK-293T cells either treated or not for 3h with 50μM QZ were exploited to perform a quantitative SILAC phosphoproteomic analysis of phosphosites readily responsive to QZ treatment. Our analysis led to the identification of 4883 phosphosites, belonging to 1693 phosphoproteins. 71 phosphosites (belonging to 47 proteins) underwent a 50% or more decreased ...
Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Phosphorylates casein in vitro (PubMed:7678767). The alpha chain contains the catalytic site. The tetrameric holoenzyme CK2, composed of two alpha and two beta subunits, phosphorylates the transcription factor GBFl, resulting in stimulation of its DNA binding activity (PubMed:7696877). CK2 phosphorylates the transcription factor PIF1 after an exposure to light, resulting in a proteasome-dependent degradation of PIF1 and promotion of photomorphogenesis (PubMed:21330376). CK2 phosphorylates translation initiation factors. May participate in the regulation of the initiation of translation (PubMed:19509278, PubMed:19509420). Acts as circadian clock component that maintains the correct period length through phosphorylation of CCA1 (PubMed:21900482). Required for the maintenance and control of genomic stability and chromatin structure (PubMed:22487192). May act as an ectokinase that
Buy our Recombinant human CKII alpha prime polypeptide protein. Ab105125 is an active full length protein produced in Baculovirus infected Sf9 cells and has…
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BioAssay record AID 712789 submitted by ChEMBL: Inhibition of human CK1-gamma2 in HEK293 cells assessed as inhibition of doxcycline-induced LRP6 phosphorylation after 2 hrs by electrochemiluminescence analysis.
Protein kinase CK2 (CK2) is a ubiquitous serine/threonine kinase with multiple cellular functions in vertebrates including apoptosis, differentiation, proliferation, survival, tumorigenesis, signal transduction, immune regulation and inflammation. In the current study, the catalytic and regulatory subunit homologs of Litopenaeus vannamei protein kinase CK2 (LvCK2α and LvCK2ß) were cloned and characterized. LvCK2α has a full-length cDNA sequence of 1764 bp with a 1053 bp open reading frame (ORF) encoding a putative protein of 351 amino acids, which contains a typical serine/threonine kinase domain. On the other hand, LvCK2ß has a 1394 bp full-length cDNA with an ORF of 663 bp encoding a protein with 221 amino acids, which contains a Casein kinase II regulatory subunit domain. Sequence and phylogenetic analysis revealed that LvCK2 was evolutionary related with the CK2 of invertebrates. Quantitative reverse transcription PCR (RT-qPCR) analysis showed that LvCK2α and LvCK2ß transcripts were ...
Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating Ser-392 of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8.
The National Institute of Standards and Technology (NIST) uses its best efforts to deliver a high quality copy of the Database and to verify that the data contained therein have been selected on the basis of sound scientific judgment. However, NIST makes no warranties to that effect, and NIST shall not be liable for any damage that may result from errors or omissions in the Database ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Induction of the generation of endoplasmic reticulum (ER) calcium (Ca(++))-mediated reactive oxygen species (ROS) by gallic acid (GA) has been implicated in the mitochondrial apoptotic death of human oral cancer (OC) cells, but the molecular mechanism by which GA causes ER Ca(++) release of OC cells to undergo cell death remains unclear. Here, we report that GA-induced phosphorylation of B-cell lymphoma 2 (BCL-2)-interacting killer (BIK) (threonine (Thr) 33/Serine (Ser) 35) and p53 (Ser 15 and Ser 392), Bcl-2-associated x protein (BAX)/BCL-2 antagonist killer 1 (BAK) oligomerization on the ER and mitochondria, rising of cytosolic Ca(+)(+) and ROS, cytochrome c (Cyt c) release from the mitochondria, Ψm loss, and apoptosis were suppressed in cells co-treated with a specific inhibitor of casein kinase II (CK II) (4,5,6,7-tetrabromobenzotriazole ...
CK2 is a pleiotropic and constitutively active serine/threonine protein kinase composed of two catalytic (α and/or α′) and two regulatory β-subunits, whose mechanism of modulation is still obscure. Here we show that CK2 α/α′ subunits undergo intermolecular (trans) tyrosine-autophosphorylation, which is dependent on intrinsic catalytic activity and is suppressed by the individual mutation of Tyr182, a crucial residue of the activation loop, to phenylalanine. At variance with serine-autophosphorylation, tyrosine-autophosphorylation of CK2α is reversed by ADP and GDP and is counteracted by the β-subunit and by a peptide reproducing the activation loop of CK2α/α′ (amino acids 175-201). These results disclose new perspectives about the mode of regulation of CK2 catalytic subunits.. ...
The acronym CK2 (derived from the misnomer casein kinase 2) denotes one of the most pleiotropic members of the eukaryotic protein kinase superfamily, characterized by an acidic consensus sequence in which a carboxylic acid (or pre-phosphorylated) side chain at position n+3 relative to the target serine/threonine residue plays a crucial role. The latest repertoire of CK2 substrates includes approx. 300 proteins, but the analysis of available phosphopeptide databases from different sources suggests that CK2 alone may be responsible for the generation of a much larger proportion (10-20%) of the eukaryotic phosphoproteome. Although for the time being CK2 is not included among protein kinases whose inhibitors are in clinical practice or in advanced clinical trials, evidence is accumulating that elevated CK2 constitutive activity co-operates to induce a number of pathological conditions, including cancer, infectious diseases, neurodegeneration and cardiovascular pathologies. The development and ...
It is now generally recognized that protein kinase signaling is involved in virtually every aspect of cell function, including growth and proliferation. The field of protein phosphorylation, including
1LR4: Inclining the purine base binding plane in protein kinase CK2 by exchanging the flanking side-chains generates a preference for ATP as a cosubstrate.
PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.
Data Availability StatementAll components and data can be accessible on demand. avoid artefactual results caused by pre-senescent adjustments. Since these cells ought to be researched within a firmly controlled pre-senescent division count ( 21 divisions), and yields of myoblasts per muscle biopsy are low, it is difficult or impossible to amplify sufficiently large cell numbers (some 250 106 myoblasts) to obtain sufficient conditioned medium for the standard ultracentrifugation approach to exosome isolation. Thus, an optimized strategy to extract and study secretory muscle vesicles is needed. In this study, conditions are optimized for the in vitro cultivation of human myoblasts, and the quality and yield of exosomes extracted using an ultracentrifugation protocol are compared with a modified polymer-based precipitation strategy combined with extra washing steps. Both vesicle extraction methods successfully enriched exosomes, as vesicles were positive for CD63, CD82, CD81, floated at identical ...
Rabbit Polyclonal Anti-CKII alpha prime polypeptide Antibody. Validated: WB, IP. Tested Reactivity: Human, Mouse. 100% Guaranteed.
CKII, CK2, CkII-beta, CK2beta, DmCKIIbeta, dCKII, DmCK2beta, CKIIbeta, CkIIbeta1, betaCK2, DmCkIIbeta, CKIIb, CG15224, CK II, CKII-beta1, mbu, CkII, And, CCK2, CK-IIbeta, CK-II beta, CK-2, Ds cas kin, CkIIbeta, Cask-II-b, dCK2beta ...
CKII, CK2, CkII-beta, CK2beta, DmCKIIbeta, dCKII, DmCK2beta, CKIIbeta, CkIIbeta1, betaCK2, DmCkIIbeta, CKIIb, CG15224, CK II, CKII-beta1, mbu, CkII, And, CCK2, CK-IIbeta, CK-II beta, CK-2, Ds cas kin, CkIIbeta, Cask-II-b, dCK2beta ...
CKII alpha antibody [N1C3] (casein kinase 2, alpha prime polypeptide) for ICC/IF, IHC-P, WB. Anti-CKII alpha pAb (GTX110726) is tested in Human samples. 100% Ab-Assurance.
RefSeq Summary (NM_001320): This gene encodes the beta subunit of casein kinase II, a ubiquitous protein kinase which regulates metabolic pathways, signal transduction, transcription, translation, and replication. The enzyme is composed of three subunits, alpha, alpha prime and beta, which form a tetrameric holoenzyme. The alpha and alpha prime subunits are catalytic, while the beta subunit serves regulatory functions. The enzyme localizes to the endoplasmic reticulum and the Golgi apparatus. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2013 ...
Full-length recombinant human CK1δ was expressed by baculovirus in Sf9 insect cells using an N-terminal GST tag. CK1δ is a member of the CK1 family of serine/threonine protein kinases which play an important role in diverse cell processes, including DNA replication and repair.
1DS5: The crystal structure of the complex of Zea mays alpha subunit with a fragment of human beta subunit provides the clue to the architecture of protein kinase CK2 holoenzyme.
Protein kinase casein kinase II (CK2) is a heterotetrameric serine/threonine kinase involved in proliferation, apoptosis and embryonic development. It is expressed at elevated levels in proliferating tissue, human cancer cell lines and virtually all forms of solid cancers. Recently it has been shown that CK2 inhibition induces apoptosis in cell models of acquired anti-estrogen resistance. These findings suggest that there may be tumor phenotype specific effects of CK2 in breast cancer and consequently phenotype specific sensitivity to CK2 inhibition. As such we sought to determine if luminal and basal cell types display differential sensitivity to selective CK2 inhibitors. Utilizing crystal violet and alamar blue assays, it was found that CK2 inhibition decreased viability of both luminal and basal breast cancer cell lines, with basal-like ER(−) MDA MB 231 cells showing notable sensitivity. Hypertrophic morphologic changes consistent with cellular senescence were noted upon inhibition of CK2. ...
TY - JOUR. T1 - Protein kinase CK2 localizes to sites of DNA double-strand break regulating the cellular response to DNA damage. AU - Olsen, Birgitte B.. AU - Wang, Shih Ya. AU - Svenstrup, Tina H.. AU - Chen, Benjamin P C. AU - Guerra, Barbara. PY - 2012/3/9. Y1 - 2012/3/9. N2 - Background: The DNA-dependent protein kinase (DNA-PK) is a nuclear complex composed of a large catalytic subunit (DNA-PKcs) and a heterodimeric DNA-targeting subunit Ku. DNA-PK is a major component of the non-homologous end-joining (NHEJ) repair mechanism, which is activated in the presence of DNA double-strand breaks induced by ionizing radiation, reactive oxygen species and radiomimetic drugs. We have recently reported that down-regulation of protein kinase CK2 by siRNA interference results in enhanced cell death specifically in DNA-PKcs-proficient human glioblastoma cells, and this event is accompanied by decreased autophosphorylation of DNA-PKcs at S2056 and delayed repair of DNA double-strand breaks.Results: In the ...
Kinson, P. L. and Orlando, C. M. (1979), 2,2′,6,6′-Tetrabromo-3,3′,5,5′-tetramethyl-4,4′-biphenol (TTB)-flame retardant copolycarbonates and copolyesters. J. Appl. Polym. Sci., 23: 155-162. doi: 10.1002/app.1979.070230114 ...
Nucleolin is a ubiquitous multifunctional protein involved in preribosome assembly and associated with both nucleolar chromatin in interphase and nucleolar organizer regions on metaphasic chromosomes in mitosis. Extensive nucleolin phosphorylation by a casein kinase (CKII) occurs on serine in growing cells. Here we report that while CKII phosphorylation is achieved in interphase, threonine phosphorylation occurs during mitosis. We provide evidence that this type of in vivo phosphorylation involves a mammalian homolog of the cell cycle control Cdc2 kinase. In vitro M-phase H1 kinase from starfish oocytes phosphorylated threonines in a TPXK motif present nine times in the amino-terminal part of the protein. The same sites which matched the p34cdc2 consensus phosphorylation sequence were used in vivo during mitosis. We propose that successive Cdc2 and CKII phosphorylation could modulate nucleolin function in controlling cell cycle-dependent nucleolar function and organization. Our results, along ...
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Protein phosphorylation is an important biological process associated with elicitor-induced defense responses in plants. In a previous report, we described how plant ferredoxin-like protein (PFLP) in transgenic plants enhances resistance to bacterial pathogens associated with the hypersensitive response (HR). PFLP possesses a putative casein kinase II phosphorylation (CK2P) site at the C-terminal in which phosphorylation occurs rapidly during defense response. However, the contribution of this site to the enhancement of disease resistance and the intensity of HR has not been clearly demonstrated. In this study, we generated two versions of truncated PFLP, PEC (extant CK2P site) and PDC (deleted CK2P site), and assessed their ability to trigger HR through harpin (HrpZ) derived from Pseudomonas syringae as well as their resistance to Ralstonia solanacearum. In an infiltration assay of HrpZ, PEC intensified harpin-mediated HR; however, PDC negated this effect. Transgenic plants expressing these ...
anti-CK2beta | casein kinase 2 subunit beta antibodies, UniProt: P40228, P40229, O81275, O80507, At5g47080, At4g17640, At3g60250, At2g44680, anti-CKB, CKB, CK2 beta, AS16 3213
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anti-CK2alpha | casein kinase 2 subunit alpha antibodies, UniProt: Q08467, Q08466, O64817, O64816, At5g67380, At3g50000, At2g23080, At2g23070, anti-CKA, CKA, CK2 alpha, AS16 3212
5 products from 4 suppliers. Compare and order Casein Kinase 1 delta ELISA Kits. View citations, images, detection ranges, sensitivity, prices and more. Recommended products for the most popular species. Our scientists will help you find the right ELISA kit for your needs.
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Casein kinase II is a protein serinethreonine kinase that is thought to be present in all eukarotic cells, implying that it has fundamental cellular functions. The holoenzyme is a tetramer containing 2 alpha or alpha-prime subunits (or one of each) and 2 beta subunits. The function of beta subunit
Protein kinase CK2 is a tetrameric holoenzyme composed of two catalytic (α and/or α) subunits and two regulatory (β) subunits. Crystallographic data paired with fluorescence imaging techniques have suggested that the formation of the CK2 holoenzyme complex within cells is a dynamic process. Although the monomeric CK2α subunit is endowed with a constitutive catalytic activity, many of the plethora of CK2 substrates are exclusively phosphorylated by the CK2 holoenzyme. This means that the spatial and high affinity interaction between CK2α and CK2β subunits is critically important and that its disruption may provide a powerful and selective way to block the phosphorylation of substrates requiring the presence of CK2β. In search of compounds inhibiting this critical protein-protein interaction, we previously designed an active cyclic peptide (Pc) derived from the CK2β carboxy-terminal domain that can efficiently antagonize the CK2 subunit interaction. To understand the functional significance of
Multiple myeloma cells survival and proliferation rely on high levels and activity of the serine-threonine kinase CK2. Conference Proceeding ...
Csnk1g3 - Csnk1g3 (untagged) - Mouse casein kinase 1, gamma 3 (cDNA clone MGC:40777 IMAGE:5366964), (10ug) available for purchase from OriGene - Your Gene Company.
1lr4: Inclining the purine base binding plane in protein kinase CK2 by exchanging the flanking side-chains generates a preference for ATP as a cosubstrate.
CK2 is a constitutively active, ubiquitously expressed and pleiotropic serine/threonine protein kinase that is implicated in many cellular functions including tumorigenesis. CK2 has two catalytic subunits, CK2a and CK2a, that carry out its function in the cell. Previous studies have indicated that inhibitor-refractory mutants have been effective in recovering residual CK2 activity, in the presence of inhibitors, when compared to wild type CK2. Based on these observations, inhibitor-refractory mutants were created for both CK2a and CK2a and tested with various concentrations with two CK2-specific inhibitors, CX-4945 and inhibitor VIII. The CK2a triple mutant (V66A/I174A/H160D) was tested in inducible U2OS Flp-In cell lines with inhibitor VIII and CX-4945 inhibitors and was found to recover residual CK2 activity 5-fold greater than previously established CK2a-(V66A/I174A) inhibitor-refractory mutants. Seven novel mutations were made to CK2a in vitro and tested with CK2 inhibitor CX-4945. The mutants
The synthetic peptide RRKDLHDDEEDEAMSITA can be used as a substrate for casein kinase 1 (CK1) in in vitro kinase assays. It is phosphorylated by CK1 with a Km of 172 �M
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What do most of you out there use for a CK7 control?......CK20 control?.... We currently are using an adenocarcinoma of the lung for our CK7 and an adenocarcinoma of the colon for the CK20. We have been having problems and need some help. Thanks Amy Johnson _______________________________________________ Histonet mailing list [email protected] http://lists.utsouthwestern.edu/mailman/listinfo/histonet ...
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