dnase i rnase free Thermo Fisher Search Results


  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 99
    Thermo Fisher thermo fisher rnase free
    Northern analysis and <t>RNase</t> H and <t>DNase</t> I sensitivity of R-loops within mtDNA coding regions. Mitochondrial RNA remains bound to CsCl-purified mtDNA. Samples were prepared as described in the legend for Fig. 2 and treated with nucleases as indicated by (+) and (-). pA is poly(A)+-purified RNA. Gene-specific riboprobes were generated from PCR products as described under “Experimental Procedures.”
    Thermo Fisher Rnase Free, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 783 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/thermo fisher rnase free/product/Thermo Fisher
    Average 99 stars, based on 783 article reviews
    Price from $9.99 to $1999.99
    thermo fisher rnase free - by Bioz Stars, 2020-05
    99/100 stars
      Buy from Supplier

    99
    Thermo Fisher dnase i
    NPM1 dissociates from rRNA/rDNA following S -glutathionylation. ( a ) Nucleoplasmic dispersion of endogenous NPM1 (left) or FLAG-NPM1 C275S (right) after RNase A (1 mg ml −1 ) and <t>DNase</t> I (0.5 U ml −1 ) digestions in HeLa cells with or without H 2 O 2 (500 μM) treatment. ( b , c ) Equal quantities of FLAG-NPM1 immunoprecipitated by anti-FLAG M2 gel in RIP ( b ) and ChIP ( c ) assays in HEK293T cells treated with H 2 O 2 (500 μM)±NAC pretreatment, blotted by anti-NPM1 antibody (upper). The relative quantities of rRNA and rDNA bound with these FLAG-NPM1 were assessed (bottom). Unpaired t- test, ** P
    Dnase I, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 56236 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dnase i/product/Thermo Fisher
    Average 99 stars, based on 56236 article reviews
    Price from $9.99 to $1999.99
    dnase i - by Bioz Stars, 2020-05
    99/100 stars
      Buy from Supplier

    99
    Thermo Fisher ambion dnase i rnase free
    NPM1 dissociates from rRNA/rDNA following S -glutathionylation. ( a ) Nucleoplasmic dispersion of endogenous NPM1 (left) or FLAG-NPM1 C275S (right) after RNase A (1 mg ml −1 ) and <t>DNase</t> I (0.5 U ml −1 ) digestions in HeLa cells with or without H 2 O 2 (500 μM) treatment. ( b , c ) Equal quantities of FLAG-NPM1 immunoprecipitated by anti-FLAG M2 gel in RIP ( b ) and ChIP ( c ) assays in HEK293T cells treated with H 2 O 2 (500 μM)±NAC pretreatment, blotted by anti-NPM1 antibody (upper). The relative quantities of rRNA and rDNA bound with these FLAG-NPM1 were assessed (bottom). Unpaired t- test, ** P
    Ambion Dnase I Rnase Free, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ambion dnase i rnase free/product/Thermo Fisher
    Average 99 stars, based on 13 article reviews
    Price from $9.99 to $1999.99
    ambion dnase i rnase free - by Bioz Stars, 2020-05
    99/100 stars
      Buy from Supplier

    98
    Thermo Fisher ribonuclease free dnase i complementary dna
    NPM1 dissociates from rRNA/rDNA following S -glutathionylation. ( a ) Nucleoplasmic dispersion of endogenous NPM1 (left) or FLAG-NPM1 C275S (right) after RNase A (1 mg ml −1 ) and <t>DNase</t> I (0.5 U ml −1 ) digestions in HeLa cells with or without H 2 O 2 (500 μM) treatment. ( b , c ) Equal quantities of FLAG-NPM1 immunoprecipitated by anti-FLAG M2 gel in RIP ( b ) and ChIP ( c ) assays in HEK293T cells treated with H 2 O 2 (500 μM)±NAC pretreatment, blotted by anti-NPM1 antibody (upper). The relative quantities of rRNA and rDNA bound with these FLAG-NPM1 were assessed (bottom). Unpaired t- test, ** P
    Ribonuclease Free Dnase I Complementary Dna, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 98/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ribonuclease free dnase i complementary dna/product/Thermo Fisher
    Average 98 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    ribonuclease free dnase i complementary dna - by Bioz Stars, 2020-05
    98/100 stars
      Buy from Supplier

    Image Search Results


    Northern analysis and RNase H and DNase I sensitivity of R-loops within mtDNA coding regions. Mitochondrial RNA remains bound to CsCl-purified mtDNA. Samples were prepared as described in the legend for Fig. 2 and treated with nucleases as indicated by (+) and (-). pA is poly(A)+-purified RNA. Gene-specific riboprobes were generated from PCR products as described under “Experimental Procedures.”

    Journal: The Journal of Biological Chemistry

    Article Title: Native R-loops Persist throughout the Mouse Mitochondrial DNA Genome *Native R-loops Persist throughout the Mouse Mitochondrial DNA Genome * S⃞

    doi: 10.1074/jbc.M806174200

    Figure Lengend Snippet: Northern analysis and RNase H and DNase I sensitivity of R-loops within mtDNA coding regions. Mitochondrial RNA remains bound to CsCl-purified mtDNA. Samples were prepared as described in the legend for Fig. 2 and treated with nucleases as indicated by (+) and (-). pA is poly(A)+-purified RNA. Gene-specific riboprobes were generated from PCR products as described under “Experimental Procedures.”

    Article Snippet: 500 ng of LA9 mtDNA-mtRNA were treated with 1.4 units of RNase-free DNase I (Ambion) or RNase H (Stratagene), denatured with glyoxal/DMSO, and separated on a 1% agarose gel using the NorthernMax-Gly kit (Ambion).

    Techniques: Northern Blot, Purification, Generated, Polymerase Chain Reaction

    Northern analysis and DNase and RNase sensitivity of mtDNA-bound nascent H-strand RNA and DNA at O H . EtBr-CsCl-purified closed circular mtDNA was analyzed by Northern analysis to detect stable R-loops. RNA size markers are in lane 1 . Poly(A)+-purified RNA is in the lane denoted by pA +. DNase I and RNase H sample treatments are indicated above the panels. A , probing for CSB-proximal RNA with T3#4 riboprobe (shown in D ). B , less exposed film of view shown in A , revealing the increased intensity of ∼150-nt species in lane 3 after DNase treatment. C , probing for CSB-distal RNA with T3#1 riboprobe as shown in D. D , reference diagram showing the major noncoding region of mtDNA. This region is identified in Fig. 1 as the area encompassing O H . The transcription start site is shown with a bent arrow followed by several relevant DNA sequence features, including CSBs III, II, and I. The termination-associated sequences ( TAS ) region is shown at the promoter distal end of the DNA. T3#4 and T#31 riboprobe positions are shown above. Below the DNA map are nucleic acids identified in the Northern blots shown in A-C . RNA is shown by thick black lines , and RNA primers in transition with DNA are shown in gray . DNA alone is in shown by thin black lines . The lines are to scale, with size interruptions shown by breaks .

    Journal: The Journal of Biological Chemistry

    Article Title: Native R-loops Persist throughout the Mouse Mitochondrial DNA Genome *Native R-loops Persist throughout the Mouse Mitochondrial DNA Genome * S⃞

    doi: 10.1074/jbc.M806174200

    Figure Lengend Snippet: Northern analysis and DNase and RNase sensitivity of mtDNA-bound nascent H-strand RNA and DNA at O H . EtBr-CsCl-purified closed circular mtDNA was analyzed by Northern analysis to detect stable R-loops. RNA size markers are in lane 1 . Poly(A)+-purified RNA is in the lane denoted by pA +. DNase I and RNase H sample treatments are indicated above the panels. A , probing for CSB-proximal RNA with T3#4 riboprobe (shown in D ). B , less exposed film of view shown in A , revealing the increased intensity of ∼150-nt species in lane 3 after DNase treatment. C , probing for CSB-distal RNA with T3#1 riboprobe as shown in D. D , reference diagram showing the major noncoding region of mtDNA. This region is identified in Fig. 1 as the area encompassing O H . The transcription start site is shown with a bent arrow followed by several relevant DNA sequence features, including CSBs III, II, and I. The termination-associated sequences ( TAS ) region is shown at the promoter distal end of the DNA. T3#4 and T#31 riboprobe positions are shown above. Below the DNA map are nucleic acids identified in the Northern blots shown in A-C . RNA is shown by thick black lines , and RNA primers in transition with DNA are shown in gray . DNA alone is in shown by thin black lines . The lines are to scale, with size interruptions shown by breaks .

    Article Snippet: 500 ng of LA9 mtDNA-mtRNA were treated with 1.4 units of RNase-free DNase I (Ambion) or RNase H (Stratagene), denatured with glyoxal/DMSO, and separated on a 1% agarose gel using the NorthernMax-Gly kit (Ambion).

    Techniques: Northern Blot, Purification, Sequencing

    miC Variants Inhibit RNA Foci Formation in (G 4 C 2 ) 44 -Expressing Cells (A) RNA foci detected in HEK293T cells expressing (G 4 C 2 ) 44 . Cells were transfected with 250 ng (G 4 C 2 ) 44 and (G 4 C 2 ) 3 plasmid and fixed 2 days post-transfection after treatment with DNase or RNase. RNA FISH was performed using a TYE563-(CCCCGG) 3 LNA probe (red), and nuclei were stained with DAPI (blue). Nuclear foci were resistant to DNase but degraded by RNase indicating RNA foci. (B) Reduction of RNA foci by miC4_101 and miC32_101. Cells were co-transfected with 250 ng (G 4 C 2 ) 44 and 100 ng miC4_101, miC32_101, or miScr plasmid. Cells were fixed 2 days post-transfection, and RNA FISH was performed as described in (A). (C) Quantification of RNA foci in miC4_101- and miC32_101-transfected cells. A series of five images was made using 10× magnification to quantify the number of cells containing nuclear foci using ImageJ (mean ± SD, one-way ANOVA, multiple-comparison test, ***p

    Journal: Molecular Therapy. Nucleic Acids

    Article Title: Artificial MicroRNAs Targeting C9orf72 Can Reduce Accumulation of Intra-nuclear Transcripts in ALS and FTD Patients

    doi: 10.1016/j.omtn.2019.01.010

    Figure Lengend Snippet: miC Variants Inhibit RNA Foci Formation in (G 4 C 2 ) 44 -Expressing Cells (A) RNA foci detected in HEK293T cells expressing (G 4 C 2 ) 44 . Cells were transfected with 250 ng (G 4 C 2 ) 44 and (G 4 C 2 ) 3 plasmid and fixed 2 days post-transfection after treatment with DNase or RNase. RNA FISH was performed using a TYE563-(CCCCGG) 3 LNA probe (red), and nuclei were stained with DAPI (blue). Nuclear foci were resistant to DNase but degraded by RNase indicating RNA foci. (B) Reduction of RNA foci by miC4_101 and miC32_101. Cells were co-transfected with 250 ng (G 4 C 2 ) 44 and 100 ng miC4_101, miC32_101, or miScr plasmid. Cells were fixed 2 days post-transfection, and RNA FISH was performed as described in (A). (C) Quantification of RNA foci in miC4_101- and miC32_101-transfected cells. A series of five images was made using 10× magnification to quantify the number of cells containing nuclear foci using ImageJ (mean ± SD, one-way ANOVA, multiple-comparison test, ***p

    Article Snippet: Optionally, cells were treated for 30 min with 5 mg/mL RNase A (QIAGEN) or 100 U RNase-free DNase (Invitrogen).

    Techniques: Expressing, Transfection, Plasmid Preparation, Fluorescence In Situ Hybridization, Staining

    NPM1 dissociates from rRNA/rDNA following S -glutathionylation. ( a ) Nucleoplasmic dispersion of endogenous NPM1 (left) or FLAG-NPM1 C275S (right) after RNase A (1 mg ml −1 ) and DNase I (0.5 U ml −1 ) digestions in HeLa cells with or without H 2 O 2 (500 μM) treatment. ( b , c ) Equal quantities of FLAG-NPM1 immunoprecipitated by anti-FLAG M2 gel in RIP ( b ) and ChIP ( c ) assays in HEK293T cells treated with H 2 O 2 (500 μM)±NAC pretreatment, blotted by anti-NPM1 antibody (upper). The relative quantities of rRNA and rDNA bound with these FLAG-NPM1 were assessed (bottom). Unpaired t- test, ** P

    Journal: Nature Communications

    Article Title: A redox mechanism underlying nucleolar stress sensing by nucleophosmin

    doi: 10.1038/ncomms13599

    Figure Lengend Snippet: NPM1 dissociates from rRNA/rDNA following S -glutathionylation. ( a ) Nucleoplasmic dispersion of endogenous NPM1 (left) or FLAG-NPM1 C275S (right) after RNase A (1 mg ml −1 ) and DNase I (0.5 U ml −1 ) digestions in HeLa cells with or without H 2 O 2 (500 μM) treatment. ( b , c ) Equal quantities of FLAG-NPM1 immunoprecipitated by anti-FLAG M2 gel in RIP ( b ) and ChIP ( c ) assays in HEK293T cells treated with H 2 O 2 (500 μM)±NAC pretreatment, blotted by anti-NPM1 antibody (upper). The relative quantities of rRNA and rDNA bound with these FLAG-NPM1 were assessed (bottom). Unpaired t- test, ** P

    Article Snippet: RNase A and DNase I digestion HeLa cells grown on coverslips were permeabilized with 0.1% Triton X-100 in PBS for 2 min, washed immediately and treated with RNase A (EN0531, 1 mg ml−1 , Fermentas, Thermo) or DNase I (EN0523, 0.5 U μl−1 , Fermentas, Thermo) in solution buffer for 10 min at 37 °C and cells were then fixed with 4% paraformaldehyde for 10 min and analysed by immunofluorescence.

    Techniques: Immunoprecipitation, Chromatin Immunoprecipitation

    Mutational analysis of the predicted stem-loop structure in the N-SL2 . (A) Strategic representation of RT-PCR used to detect (-) gRNA, (+) sg mRNA7 and (-) sg mRNA7. The positions are according to APRRSV stain (GenBank: GQ330474 ) and all primer sequences are listed in Table 1. pAS was a non-replicative control which was absence of gene ORF1a and ORF1b (1688-13118) in full-length cDNA clone. (B) Schematic representation of the mutations introduced into the N-SL2 structure. The loop was enlarged as described in Figure 1, and mutants L-LL and L-RR were generated by overlapping PCR mutagenesis. L-RL was generated by combining the right and left arm sequences of the L-LL and L-RR, respectively, such that the overall structure of N-SL2 was restored. All the mutated nucleotides (lowercase) are highlighted in gray shading. The stem mutants, S-LL and S-RR, were generated by overlapping PCR such that one arm sequence was replaced with that of the opposite arm. The double mutant, S-RL, was generated by combining the mutations in the left and right arms such that the overall structure was restored. All mutant sequences are shown as lowercase. (C) RT-PCR of RNAs extracted from pAS and WT transfected cells at 24 hours after transfection. DNase I and RNase A were used to omit template DNA and the reverse transcriptase. The primers were nested RT-PCR primers as same as (-) gRNA detection. A 2-kbp ladder was used as a molecular size marker. The numbers indicated the lane No. (D) RT-PCR analysis of the mutants. Total cellular RNAs were extracted from mutant plasmids-transfected from BHK-21 cells at 24 hours post-transfection. β-actin is a marker for the level of intracellular RNA isolation, and pAS is a non-replicative control.

    Journal: Virology Journal

    Article Title: A 5'-proximal Stem-loop Structure of 5' Untranslated Region of Porcine Reproductive and Respiratory Syndrome Virus Genome Is Key for Virus Replication

    doi: 10.1186/1743-422X-8-172

    Figure Lengend Snippet: Mutational analysis of the predicted stem-loop structure in the N-SL2 . (A) Strategic representation of RT-PCR used to detect (-) gRNA, (+) sg mRNA7 and (-) sg mRNA7. The positions are according to APRRSV stain (GenBank: GQ330474 ) and all primer sequences are listed in Table 1. pAS was a non-replicative control which was absence of gene ORF1a and ORF1b (1688-13118) in full-length cDNA clone. (B) Schematic representation of the mutations introduced into the N-SL2 structure. The loop was enlarged as described in Figure 1, and mutants L-LL and L-RR were generated by overlapping PCR mutagenesis. L-RL was generated by combining the right and left arm sequences of the L-LL and L-RR, respectively, such that the overall structure of N-SL2 was restored. All the mutated nucleotides (lowercase) are highlighted in gray shading. The stem mutants, S-LL and S-RR, were generated by overlapping PCR such that one arm sequence was replaced with that of the opposite arm. The double mutant, S-RL, was generated by combining the mutations in the left and right arms such that the overall structure was restored. All mutant sequences are shown as lowercase. (C) RT-PCR of RNAs extracted from pAS and WT transfected cells at 24 hours after transfection. DNase I and RNase A were used to omit template DNA and the reverse transcriptase. The primers were nested RT-PCR primers as same as (-) gRNA detection. A 2-kbp ladder was used as a molecular size marker. The numbers indicated the lane No. (D) RT-PCR analysis of the mutants. Total cellular RNAs were extracted from mutant plasmids-transfected from BHK-21 cells at 24 hours post-transfection. β-actin is a marker for the level of intracellular RNA isolation, and pAS is a non-replicative control.

    Article Snippet: To eliminate the transfected input DNA, the RNA preparation was further treated with 2 U RNase-free recombinant DNase I for 30 minutes at 37°C by using the DNA-free Kit (Ambion), followed by re-suspension in RNase-free H2 O. RT-PCR was employed to detect the (-) gRNAs and sg mRNAs using specific primers.

    Techniques: Reverse Transcription Polymerase Chain Reaction, Staining, Generated, Polymerase Chain Reaction, Mutagenesis, Sequencing, Transfection, Marker, Isolation

    IR induces RIG-I binding to endogenous double-stranded RNAs A. HEK293 reporter cells were irradiated after transfection with either an empty vector, a full length human RIG-I, a RIG-I lacking CARD domains (RIG-I helicase/CTD), or a RIG-I harboring K858A and K861A mutations in the C-terminal domain (RIG-I K858A-K861A), in addition to an IFN-beta promoter-driven luciferase construct. A Renilla reporter construct served as a transfection control. Data are presented as mean fold-change relative to the non-irradiated empty vector control. B. Donor HEK293 cells were either unirradiated or treated with IR (3 or 6 Gy). Total RNA was purified and transferred to independent batches of HEK293 reporter cells transfected by RIG-I constructs as described in (A). A synthetic double-stranded RNA construct comprised of 5′-triphosphorylated dsRNA and an unphosphorylated counterpart served as positive and negative controls, respectively (inset). C. Experimental design for isolation and purification of RNA bound to RIG-I after exposure to IR. *To validate RNA sequencing data by qPCR experiments, UV crosslinking was performed prior to cell lysis and immunoprecipitation of RIG-I. See methods for further details. D. Purified RNA from total cellular extracts (Lanes 2 and 3) and complexes with RIG-I (Lanes 4 and 5). Lane 1 is the marker. Data are representative of at least 3 independent experiments. E. HEK293 cells over-expressing the HA-tagged full length RIG-I (Lanes 2 and 3), the RIG-I helicase-CTD mutant (Lanes 4 and 5) and the RIG-I K858A-K861A CTD mutant (Lanes 6 and 7) were either un-irradiated or exposed to IR (6 Gy), lysed and incubated with anti-HA monoclonal antibody to pulldown the respective WT and mutant RIG-I proteins. RIG-I diagrams illustrate the mechanism of RIG-I activation (adapted from [ 57 ]). In the inactive/unbound conformation, the CARD domain of RIG-I is folded to block the helicase domain from RNA binding RNA, but allows the CTD to search for its ligand. Upon binding of the blunt end of a dsRNA molecule to the CTD, the CARD domain opens to allow the helicase domain to bind the remaining dsRNA molecule. Absence of the CARD domain in the helicase/CTD mutant enables higher affinity binding to dsRNA ligands as compared to the full length RIG-I. The lysine residues at amino acid positions 858 and 861 have previously demonstrated importance in latching onto the 5′-triphosphorylated end of viral dsRNA ligands. F. RNA bound to RIG-I after exposure to IR (6 Gy) was treated with: RNase A (lane 3), dsRNA-specific RNase III (lane 4), single-strand specific nuclease S1 (lane 5) and DNase I (lane 7). Lane 2 shows the input and lanes 1 and 6 display markers.

    Journal: Oncotarget

    Article Title: Cancer therapies activate RIG-I-like receptor pathway through endogenous non-coding RNAs

    doi: 10.18632/oncotarget.8420

    Figure Lengend Snippet: IR induces RIG-I binding to endogenous double-stranded RNAs A. HEK293 reporter cells were irradiated after transfection with either an empty vector, a full length human RIG-I, a RIG-I lacking CARD domains (RIG-I helicase/CTD), or a RIG-I harboring K858A and K861A mutations in the C-terminal domain (RIG-I K858A-K861A), in addition to an IFN-beta promoter-driven luciferase construct. A Renilla reporter construct served as a transfection control. Data are presented as mean fold-change relative to the non-irradiated empty vector control. B. Donor HEK293 cells were either unirradiated or treated with IR (3 or 6 Gy). Total RNA was purified and transferred to independent batches of HEK293 reporter cells transfected by RIG-I constructs as described in (A). A synthetic double-stranded RNA construct comprised of 5′-triphosphorylated dsRNA and an unphosphorylated counterpart served as positive and negative controls, respectively (inset). C. Experimental design for isolation and purification of RNA bound to RIG-I after exposure to IR. *To validate RNA sequencing data by qPCR experiments, UV crosslinking was performed prior to cell lysis and immunoprecipitation of RIG-I. See methods for further details. D. Purified RNA from total cellular extracts (Lanes 2 and 3) and complexes with RIG-I (Lanes 4 and 5). Lane 1 is the marker. Data are representative of at least 3 independent experiments. E. HEK293 cells over-expressing the HA-tagged full length RIG-I (Lanes 2 and 3), the RIG-I helicase-CTD mutant (Lanes 4 and 5) and the RIG-I K858A-K861A CTD mutant (Lanes 6 and 7) were either un-irradiated or exposed to IR (6 Gy), lysed and incubated with anti-HA monoclonal antibody to pulldown the respective WT and mutant RIG-I proteins. RIG-I diagrams illustrate the mechanism of RIG-I activation (adapted from [ 57 ]). In the inactive/unbound conformation, the CARD domain of RIG-I is folded to block the helicase domain from RNA binding RNA, but allows the CTD to search for its ligand. Upon binding of the blunt end of a dsRNA molecule to the CTD, the CARD domain opens to allow the helicase domain to bind the remaining dsRNA molecule. Absence of the CARD domain in the helicase/CTD mutant enables higher affinity binding to dsRNA ligands as compared to the full length RIG-I. The lysine residues at amino acid positions 858 and 861 have previously demonstrated importance in latching onto the 5′-triphosphorylated end of viral dsRNA ligands. F. RNA bound to RIG-I after exposure to IR (6 Gy) was treated with: RNase A (lane 3), dsRNA-specific RNase III (lane 4), single-strand specific nuclease S1 (lane 5) and DNase I (lane 7). Lane 2 shows the input and lanes 1 and 6 display markers.

    Article Snippet: qRT-PCR analysis 1 μg total RNA was subjected to DNase I treatment in a 30 μL reaction volume using DNase I, RNase-free (Thermo Scientific) following the manufacturer's protocol. cDNA was synthesized from 10 μL of the DNase treated RNA using the High-Capacity cDNA Reverse Transcription Kit (LifeTechnologies) following the manufacturer's protocol.

    Techniques: Binding Assay, Irradiation, Transfection, Plasmid Preparation, Luciferase, Construct, Purification, Isolation, RNA Sequencing Assay, Real-time Polymerase Chain Reaction, Lysis, Immunoprecipitation, Marker, Expressing, Mutagenesis, Incubation, Activation Assay, Blocking Assay, RNA Binding Assay