polymerase chain reaction pcr fragment  (Millipore)


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    Structured Review

    Millipore polymerase chain reaction pcr fragment
    Polymerase Chain Reaction Pcr Fragment, supplied by Millipore, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/polymerase chain reaction pcr fragment/product/Millipore
    Average 91 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    polymerase chain reaction pcr fragment - by Bioz Stars, 2020-07
    91/100 stars

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    Polymerase Chain Reaction:

    Article Title: Cancer testis antigen Sperm Protein 17 as a new target for triple negative breast cancer immunotherapy
    Article Snippet: .. 1/20 of retro-transcription reaction volume was PCR-amplified in 20 μL reaction with PCR Core kit with Taq DNA polymerase (Sigma-Aldrich, Saint Louis, MO). .. Primers sequences were: SP17 left 5’-GCTCGGAGAGAAAGGAGGTTC-3’, SP17 right 5’-TACTCCCCCATTCTGCTGGA-3’, Human β-actin Real-Time Primer Mix (1 nmol/200 μL, Origene cat. # HP204660).

    Article Title: Mycobacterium avium subspecies hominissuis in Crohn’s disease: a case report
    Article Snippet: .. The PCR amplification was performed in 50 μl volume using 94°C for 30 seconds, 55°C for 30 seconds and 72°C for 45 seconds for 40 cycles using the PCR Core-kit (Sigma Aldrich). .. The PCR amplicon was visualized on 1.2% agarose gel electrophoresis.

    Article Title: Nitrite Reductase NirBD Is Induced and Plays an Important Role during In Vitro Dormancy of Mycobacterium tuberculosis
    Article Snippet: .. PCR was carried out by using Taq DNA polymerase provided in the PCR core kit (Sigma) in a total volume of 50 μl. .. The amplification PCR product was first analyzed on a 2% agarose gel containing 1% (vol/vol) SafeView dye followed by nucleotide sequencing to verify the fragment.

    Amplification:

    Article Title: Mycobacterium avium subspecies hominissuis in Crohn’s disease: a case report
    Article Snippet: .. The PCR amplification was performed in 50 μl volume using 94°C for 30 seconds, 55°C for 30 seconds and 72°C for 45 seconds for 40 cycles using the PCR Core-kit (Sigma Aldrich). .. The PCR amplicon was visualized on 1.2% agarose gel electrophoresis.

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    Millipore genomic dna fragments encoding prkg2 exon iii
    NO-Cbi stimulates Wnt signaling and mPOB proliferation via PKG II (A) POBs isolated from mice homozygous for <t>prkg2</t> alleles flanked by LoxP sites (“floxed” PRKG2 f/f ) were infected with adenovirus expressing β-galactosidase (LacZ, control) or CRE recombinase (CRE). Forty-eight h later, relative amounts of prkg2 mRNA were determined by qRT-PCR, and knockdown efficiency of PKG II protein was analyzed by Western blotting, with caveolin-1 serving as a loading control. (B) Cells were infected as in A, but 30 h later were transferred to medium containing 0.1% FBS, and 18 h later were treated with 10 μM NO-Cbi or vehicle for 10 min. Akt and GSK-3β phosphorylation were assessed using antibodies specific for Akt(pSer 473 ) and GSK-3β(pSer 9 ), with total GSK-3β serving as a loading control; densitometric quantification is shown on the right, with relative amounts of pAkt and pGSK-3β found in vehicle-treated, control virus-infected cells assigned a value of 1. (C) PRKG2 f/f POBs were infected with control or Cre virus and transferred to 0.1% FBS as in B; they were treated with NO-Cbi or vehicle for 6 h, prior to detecting β-catenin by immunofluorescence staining. The bottom panel shows nuclei counterstained with Hoechst 33342. Numbers below indicate the percentage of cells showing nuclear β-catenin. (D) Cells were infected and cultured as in B; they were treated with NO-Cbi or vehicle for 1 h prior to measuring 3 H-thymidine incorporation into <t>DNA</t> for 24 h. (E) Cells were infected with control or CRE virus as described in A, and treated with 10 μM NO-Cbi or vehicle for 24 h. Expression of Wingless type MMTV-integration site family-1a (Wnt1a), low-density lipoprotein receptor- related protein-5 (Lrp5), β-catenin (βCat), cyclin D (CycD), alkaline phosphatase (ALP), osteocalcin (OCN), and tubulin (Tuba1) mRNA was measured by qRT-PCR and normalized to 18S rRNA; normalized mRNA in untreated cells was assigned a value of 1 . (F) POBs cultured in 10 % FBS were treated with 10 μM NO-Cbi for the indicated times, and Lrp5 protein (open circles) and mRNA (filled squares) were assessed by Western blotting (a representative blot is shown) and qRT-PCR, respectively. Panels A–F show means ± SEM of 3–5 independent experiments in osteoblasts isolated from PRKG2 f/f ). *p
    Genomic Dna Fragments Encoding Prkg2 Exon Iii, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Millipore transgene fragment
    Generation of Fshb-Cre deleter mice is achieved by pronuclear microinjection of the <t>transgene</t> DNA (A). The transgene is stably transmitted to F2 progeny as demonstrated by tail DNA genomic PCR (B) using specific primers indicated by blue arrows (A) that
    Transgene Fragment, supplied by Millipore, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore tbca
    CX-4945 affects alternative splicing in a <t>CK2-independent</t> manner. (A) Two other inhibitors of CK2, TBB and <t>TBCA,</t> were also tested to determine whether splicing regulation by CX-4945 is related to CK2 activity. 293T cells were treated with 10 µM CX-4945 or 100 µM TBB or and TBCA for 12 hours. Inhibitory activities of CX-4945, TBB, and TBCA on CK2 were assessed by examination of phosphorylation of AKT(S129), the major substrate of CK2. Total levels of AKT were also monitored as a control. hnRNP A1 was used as a loading control. (B) Alternatively spliced CK2 α′, ELL2, CPEB1, PRPSAP2, and QRSL1 mRNAs were examined by RT-PCR. PCR products of normal and alternatively spliced isoforms are denoted by black arrowheads. An extra PCR product of the QRSL1 gene appeared in TBB-treated samples and is denoted by an asterisk. All experiments were performed twice, and representative data for each are presented.
    Tbca, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    NO-Cbi stimulates Wnt signaling and mPOB proliferation via PKG II (A) POBs isolated from mice homozygous for prkg2 alleles flanked by LoxP sites (“floxed” PRKG2 f/f ) were infected with adenovirus expressing β-galactosidase (LacZ, control) or CRE recombinase (CRE). Forty-eight h later, relative amounts of prkg2 mRNA were determined by qRT-PCR, and knockdown efficiency of PKG II protein was analyzed by Western blotting, with caveolin-1 serving as a loading control. (B) Cells were infected as in A, but 30 h later were transferred to medium containing 0.1% FBS, and 18 h later were treated with 10 μM NO-Cbi or vehicle for 10 min. Akt and GSK-3β phosphorylation were assessed using antibodies specific for Akt(pSer 473 ) and GSK-3β(pSer 9 ), with total GSK-3β serving as a loading control; densitometric quantification is shown on the right, with relative amounts of pAkt and pGSK-3β found in vehicle-treated, control virus-infected cells assigned a value of 1. (C) PRKG2 f/f POBs were infected with control or Cre virus and transferred to 0.1% FBS as in B; they were treated with NO-Cbi or vehicle for 6 h, prior to detecting β-catenin by immunofluorescence staining. The bottom panel shows nuclei counterstained with Hoechst 33342. Numbers below indicate the percentage of cells showing nuclear β-catenin. (D) Cells were infected and cultured as in B; they were treated with NO-Cbi or vehicle for 1 h prior to measuring 3 H-thymidine incorporation into DNA for 24 h. (E) Cells were infected with control or CRE virus as described in A, and treated with 10 μM NO-Cbi or vehicle for 24 h. Expression of Wingless type MMTV-integration site family-1a (Wnt1a), low-density lipoprotein receptor- related protein-5 (Lrp5), β-catenin (βCat), cyclin D (CycD), alkaline phosphatase (ALP), osteocalcin (OCN), and tubulin (Tuba1) mRNA was measured by qRT-PCR and normalized to 18S rRNA; normalized mRNA in untreated cells was assigned a value of 1 . (F) POBs cultured in 10 % FBS were treated with 10 μM NO-Cbi for the indicated times, and Lrp5 protein (open circles) and mRNA (filled squares) were assessed by Western blotting (a representative blot is shown) and qRT-PCR, respectively. Panels A–F show means ± SEM of 3–5 independent experiments in osteoblasts isolated from PRKG2 f/f ). *p

    Journal: Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research

    Article Title: A NOVEL, DIRECT NO DONOR REGULATES OSTEOBLAST AND OSTEOCLAST FUNCTIONS AND INCREASES BONE MASS IN OVARIECTOMIZED MICE

    doi: 10.1002/jbmr.2909

    Figure Lengend Snippet: NO-Cbi stimulates Wnt signaling and mPOB proliferation via PKG II (A) POBs isolated from mice homozygous for prkg2 alleles flanked by LoxP sites (“floxed” PRKG2 f/f ) were infected with adenovirus expressing β-galactosidase (LacZ, control) or CRE recombinase (CRE). Forty-eight h later, relative amounts of prkg2 mRNA were determined by qRT-PCR, and knockdown efficiency of PKG II protein was analyzed by Western blotting, with caveolin-1 serving as a loading control. (B) Cells were infected as in A, but 30 h later were transferred to medium containing 0.1% FBS, and 18 h later were treated with 10 μM NO-Cbi or vehicle for 10 min. Akt and GSK-3β phosphorylation were assessed using antibodies specific for Akt(pSer 473 ) and GSK-3β(pSer 9 ), with total GSK-3β serving as a loading control; densitometric quantification is shown on the right, with relative amounts of pAkt and pGSK-3β found in vehicle-treated, control virus-infected cells assigned a value of 1. (C) PRKG2 f/f POBs were infected with control or Cre virus and transferred to 0.1% FBS as in B; they were treated with NO-Cbi or vehicle for 6 h, prior to detecting β-catenin by immunofluorescence staining. The bottom panel shows nuclei counterstained with Hoechst 33342. Numbers below indicate the percentage of cells showing nuclear β-catenin. (D) Cells were infected and cultured as in B; they were treated with NO-Cbi or vehicle for 1 h prior to measuring 3 H-thymidine incorporation into DNA for 24 h. (E) Cells were infected with control or CRE virus as described in A, and treated with 10 μM NO-Cbi or vehicle for 24 h. Expression of Wingless type MMTV-integration site family-1a (Wnt1a), low-density lipoprotein receptor- related protein-5 (Lrp5), β-catenin (βCat), cyclin D (CycD), alkaline phosphatase (ALP), osteocalcin (OCN), and tubulin (Tuba1) mRNA was measured by qRT-PCR and normalized to 18S rRNA; normalized mRNA in untreated cells was assigned a value of 1 . (F) POBs cultured in 10 % FBS were treated with 10 μM NO-Cbi for the indicated times, and Lrp5 protein (open circles) and mRNA (filled squares) were assessed by Western blotting (a representative blot is shown) and qRT-PCR, respectively. Panels A–F show means ± SEM of 3–5 independent experiments in osteoblasts isolated from PRKG2 f/f ). *p

    Article Snippet: To generate PRKG2f/f mice, we PCR-amplified genomic DNA fragments encoding prkg2 exon III with flanking sequences from 129/SvJ ES cells using KOD polymerase (EMD Millipore Corporation).

    Techniques: Isolation, Mouse Assay, Infection, Expressing, Quantitative RT-PCR, Western Blot, Immunofluorescence, Staining, Cell Culture, ALP Assay

    NO-Cbi inhibits osteoclast differentiation (A,B) Murine bone marrow mono-nuclear cells were cultured in the presence of M-CSF; after 3 d, RANKL was added, with or without NO-Cbi at the indicated concentrations. Tartrate-resistant acid phosphatase (TRAP)-positive cells (red) were counted on day 8. (C) Cells were cultured as in A, but some cultures received 10 μM NO-Cbi, 5 μM DETA-NONOate (Deta-NO, which releases two moles of NO per mole of drug), or 100 μM 8-pCPT-cGMP together with RANKL. (D) Expression of TRAP, cathepsin K (Ctsk), and calcitonin receptor (CalcR) mRNA was determined by qRT-PCR and normalized to 18S rRNA; normalized mRNA in vehicle-treated cells was assigned a value of 1. (E–G) Bone marrow mononuclear cells isolated from PRKG2 f/f mice were cultured with M-CSF and RANKL as described in panel A, but 24 h after plating, cells were infected with adenovirus expressing either green fluorescent protein (GFP, control) or CRE. Relative amounts of prkg2 mRNA were determined by qRT-PCR (E), and TRAP-positive cells were counted on day 8 (F,G). Panels B–F show means ± SEM of at least three independent experiments; *p

    Journal: Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research

    Article Title: A NOVEL, DIRECT NO DONOR REGULATES OSTEOBLAST AND OSTEOCLAST FUNCTIONS AND INCREASES BONE MASS IN OVARIECTOMIZED MICE

    doi: 10.1002/jbmr.2909

    Figure Lengend Snippet: NO-Cbi inhibits osteoclast differentiation (A,B) Murine bone marrow mono-nuclear cells were cultured in the presence of M-CSF; after 3 d, RANKL was added, with or without NO-Cbi at the indicated concentrations. Tartrate-resistant acid phosphatase (TRAP)-positive cells (red) were counted on day 8. (C) Cells were cultured as in A, but some cultures received 10 μM NO-Cbi, 5 μM DETA-NONOate (Deta-NO, which releases two moles of NO per mole of drug), or 100 μM 8-pCPT-cGMP together with RANKL. (D) Expression of TRAP, cathepsin K (Ctsk), and calcitonin receptor (CalcR) mRNA was determined by qRT-PCR and normalized to 18S rRNA; normalized mRNA in vehicle-treated cells was assigned a value of 1. (E–G) Bone marrow mononuclear cells isolated from PRKG2 f/f mice were cultured with M-CSF and RANKL as described in panel A, but 24 h after plating, cells were infected with adenovirus expressing either green fluorescent protein (GFP, control) or CRE. Relative amounts of prkg2 mRNA were determined by qRT-PCR (E), and TRAP-positive cells were counted on day 8 (F,G). Panels B–F show means ± SEM of at least three independent experiments; *p

    Article Snippet: To generate PRKG2f/f mice, we PCR-amplified genomic DNA fragments encoding prkg2 exon III with flanking sequences from 129/SvJ ES cells using KOD polymerase (EMD Millipore Corporation).

    Techniques: Cell Culture, Expressing, Quantitative RT-PCR, Isolation, Mouse Assay, Infection

    NO-Cbi enhances cGMP/PKG and Erk/Akt signaling, gene expression, proliferation, and survival in POBs (A) POBs isolated from intact C57Bl6 mice were incubated in medium with 0.1% FBS (3 × 10 5 cells/ml) for 2 h prior to receiving vehicle or 10 μM NO-Cbi (NOCbi) for the indicated times. Stable NO oxidation products (nitrite plus nitrate, NO x ) were measured in the medium by the Griess reaction (NO x present in medium without cells was subtracted). (B,C) POBs were treated with vehicle or NO-Cbi at the indicated concentrations for 30 min. The intracellular cGMP concentration was measured by ELISA (B), and VASP phosphorylation was analyzed by Western blot using a phospho-Ser 259 -specific antibody, with bar graph showing densitometric quantification of pVASP normalized to β-actin (C). (D,E) Serum-deprived POBs were treated with vehicle or 10 μM NO-Cbi for 10 min and ERK ( D ) and Akt ( E ) activation were assessed by blotting with phospho-specific antibodies. Densitometric quantification of pErk and pAkt normalized to total Erk and Akt, respectively, is shown in the bar graphs. (F) POBs were serum-starved for 36 h in medium containing 1% BSA with 10 μM NO-Cbi or vehicle; apoptosis was assessed by immunofluorescence staining with antibodies specific for cleaved caspase-3 and FITC-coupled secondary antibodies (green); nuclei were counterstained with Hoechst 33342 (blue). (G) POBs were cultured in medium with 0.1% FBS for 18 h, and treated with 10 μM NO-Cbi or vehicle for 1 h; they were transferred to fresh medium containing 3 H-thymidine for 24 h, and thymidine incorporation into DNA was measured. ( H,I ) Confluent POBs were differentiated in ascorbate-containing medium for 14 d, with some cells receiving 10 μM NO-Cbi (filled bars) or vehicle (open bars) during the last 24 h. Expression of osteocalcin (OCN), osteopontin (Spp1), collagen 1-A1 (Col1a1), alkaline phosphatase (ALP), low-density lipoprotein receptor-related protein-5 (Lrp5), tubulin (Tuba1), receptor activator of nuclear factor kappa-B ligand (RANKL), and osteoprotegerin (OPG) mRNA was determined by qRT-PCR and normalized to 18S rRNA; normalized mRNA in vehicle-treated cells was assigned a value of 1. Panels A–I show means ± SEM of at least three independent experiments; *p

    Journal: Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research

    Article Title: A NOVEL, DIRECT NO DONOR REGULATES OSTEOBLAST AND OSTEOCLAST FUNCTIONS AND INCREASES BONE MASS IN OVARIECTOMIZED MICE

    doi: 10.1002/jbmr.2909

    Figure Lengend Snippet: NO-Cbi enhances cGMP/PKG and Erk/Akt signaling, gene expression, proliferation, and survival in POBs (A) POBs isolated from intact C57Bl6 mice were incubated in medium with 0.1% FBS (3 × 10 5 cells/ml) for 2 h prior to receiving vehicle or 10 μM NO-Cbi (NOCbi) for the indicated times. Stable NO oxidation products (nitrite plus nitrate, NO x ) were measured in the medium by the Griess reaction (NO x present in medium without cells was subtracted). (B,C) POBs were treated with vehicle or NO-Cbi at the indicated concentrations for 30 min. The intracellular cGMP concentration was measured by ELISA (B), and VASP phosphorylation was analyzed by Western blot using a phospho-Ser 259 -specific antibody, with bar graph showing densitometric quantification of pVASP normalized to β-actin (C). (D,E) Serum-deprived POBs were treated with vehicle or 10 μM NO-Cbi for 10 min and ERK ( D ) and Akt ( E ) activation were assessed by blotting with phospho-specific antibodies. Densitometric quantification of pErk and pAkt normalized to total Erk and Akt, respectively, is shown in the bar graphs. (F) POBs were serum-starved for 36 h in medium containing 1% BSA with 10 μM NO-Cbi or vehicle; apoptosis was assessed by immunofluorescence staining with antibodies specific for cleaved caspase-3 and FITC-coupled secondary antibodies (green); nuclei were counterstained with Hoechst 33342 (blue). (G) POBs were cultured in medium with 0.1% FBS for 18 h, and treated with 10 μM NO-Cbi or vehicle for 1 h; they were transferred to fresh medium containing 3 H-thymidine for 24 h, and thymidine incorporation into DNA was measured. ( H,I ) Confluent POBs were differentiated in ascorbate-containing medium for 14 d, with some cells receiving 10 μM NO-Cbi (filled bars) or vehicle (open bars) during the last 24 h. Expression of osteocalcin (OCN), osteopontin (Spp1), collagen 1-A1 (Col1a1), alkaline phosphatase (ALP), low-density lipoprotein receptor-related protein-5 (Lrp5), tubulin (Tuba1), receptor activator of nuclear factor kappa-B ligand (RANKL), and osteoprotegerin (OPG) mRNA was determined by qRT-PCR and normalized to 18S rRNA; normalized mRNA in vehicle-treated cells was assigned a value of 1. Panels A–I show means ± SEM of at least three independent experiments; *p

    Article Snippet: To generate PRKG2f/f mice, we PCR-amplified genomic DNA fragments encoding prkg2 exon III with flanking sequences from 129/SvJ ES cells using KOD polymerase (EMD Millipore Corporation).

    Techniques: Expressing, Isolation, Mouse Assay, Incubation, Concentration Assay, Enzyme-linked Immunosorbent Assay, Western Blot, Activation Assay, Immunofluorescence, Staining, Cell Culture, ALP Assay, Quantitative RT-PCR

    Generation of Fshb-Cre deleter mice is achieved by pronuclear microinjection of the transgene DNA (A). The transgene is stably transmitted to F2 progeny as demonstrated by tail DNA genomic PCR (B) using specific primers indicated by blue arrows (A) that

    Journal: Molecular and cellular endocrinology

    Article Title: Fshb-iCre mice are efficient and specific Cre deleters for the gonadotrope lineage

    doi: 10.1016/j.mce.2015.10.006

    Figure Lengend Snippet: Generation of Fshb-Cre deleter mice is achieved by pronuclear microinjection of the transgene DNA (A). The transgene is stably transmitted to F2 progeny as demonstrated by tail DNA genomic PCR (B) using specific primers indicated by blue arrows (A) that

    Article Snippet: The transgene fragment was further purified on Millipore Montage DNA columns, and microinjected into one-cell FVB mouse embryos as described ( ).

    Techniques: Mouse Assay, Stable Transfection, Polymerase Chain Reaction

    CX-4945 affects alternative splicing in a CK2-independent manner. (A) Two other inhibitors of CK2, TBB and TBCA, were also tested to determine whether splicing regulation by CX-4945 is related to CK2 activity. 293T cells were treated with 10 µM CX-4945 or 100 µM TBB or and TBCA for 12 hours. Inhibitory activities of CX-4945, TBB, and TBCA on CK2 were assessed by examination of phosphorylation of AKT(S129), the major substrate of CK2. Total levels of AKT were also monitored as a control. hnRNP A1 was used as a loading control. (B) Alternatively spliced CK2 α′, ELL2, CPEB1, PRPSAP2, and QRSL1 mRNAs were examined by RT-PCR. PCR products of normal and alternatively spliced isoforms are denoted by black arrowheads. An extra PCR product of the QRSL1 gene appeared in TBB-treated samples and is denoted by an asterisk. All experiments were performed twice, and representative data for each are presented.

    Journal: PLoS ONE

    Article Title: Identification of a Novel Function of CX-4945 as a Splicing Regulator

    doi: 10.1371/journal.pone.0094978

    Figure Lengend Snippet: CX-4945 affects alternative splicing in a CK2-independent manner. (A) Two other inhibitors of CK2, TBB and TBCA, were also tested to determine whether splicing regulation by CX-4945 is related to CK2 activity. 293T cells were treated with 10 µM CX-4945 or 100 µM TBB or and TBCA for 12 hours. Inhibitory activities of CX-4945, TBB, and TBCA on CK2 were assessed by examination of phosphorylation of AKT(S129), the major substrate of CK2. Total levels of AKT were also monitored as a control. hnRNP A1 was used as a loading control. (B) Alternatively spliced CK2 α′, ELL2, CPEB1, PRPSAP2, and QRSL1 mRNAs were examined by RT-PCR. PCR products of normal and alternatively spliced isoforms are denoted by black arrowheads. An extra PCR product of the QRSL1 gene appeared in TBB-treated samples and is denoted by an asterisk. All experiments were performed twice, and representative data for each are presented.

    Article Snippet: The CK2 inhibitors CX-4945 (Selleck), TBB (Sigma), TBCA (Calbiochem), and Clk inhibitor TG-003 (Sigma) were dissolved in DMSO before incubation with the cells.

    Techniques: Activity Assay, Reverse Transcription Polymerase Chain Reaction, Polymerase Chain Reaction