rnase a  (Worthington Biochemical)


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  • 93
    Name:
    Ribonuclease A
    Description:
    A chromatographically purified lyophilized powder
    Catalog Number:
    ls003431
    Price:
    75
    Source:
    Bovine Pancreas
    Size:
    200 mg
    Cas Number:
    9001.99.4
    Buy from Supplier


    Structured Review

    Worthington Biochemical rnase a
    Development of an RNase-coupled EC dissociation assay. ( A  for detailed description of the assay. ( B ) Sequence of RNA and site of RNase A-catalyzed cleavage is shown. Red  C  represents cytosine monophosphate incorporated by Pol I during the labeling reaction. ( C ) Denaturing PAGE separation of WT EC dissociation time course collected at 0.29 M KCl using the salt-jump strategy (see text). ( D ) Same as in ( C ), except ECs were heated 5 min at 95°C and cooled to 25°C before the salt-jump. To see this figure in color, go online.
    A chromatographically purified lyophilized powder
    https://www.bioz.com/result/rnase a/product/Worthington Biochemical
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rnase a - by Bioz Stars, 2021-03
    93/100 stars

    Images

    1) Product Images from "The A12.2 Subunit Is an Intrinsic Destabilizer of the RNA Polymerase I Elongation Complex"

    Article Title: The A12.2 Subunit Is an Intrinsic Destabilizer of the RNA Polymerase I Elongation Complex

    Journal: Biophysical Journal

    doi: 10.1016/j.bpj.2018.04.015

    Development of an RNase-coupled EC dissociation assay. ( A  for detailed description of the assay. ( B ) Sequence of RNA and site of RNase A-catalyzed cleavage is shown. Red  C  represents cytosine monophosphate incorporated by Pol I during the labeling reaction. ( C ) Denaturing PAGE separation of WT EC dissociation time course collected at 0.29 M KCl using the salt-jump strategy (see text). ( D ) Same as in ( C ), except ECs were heated 5 min at 95°C and cooled to 25°C before the salt-jump. To see this figure in color, go online.
    Figure Legend Snippet: Development of an RNase-coupled EC dissociation assay. ( A for detailed description of the assay. ( B ) Sequence of RNA and site of RNase A-catalyzed cleavage is shown. Red C represents cytosine monophosphate incorporated by Pol I during the labeling reaction. ( C ) Denaturing PAGE separation of WT EC dissociation time course collected at 0.29 M KCl using the salt-jump strategy (see text). ( D ) Same as in ( C ), except ECs were heated 5 min at 95°C and cooled to 25°C before the salt-jump. To see this figure in color, go online.

    Techniques Used: Sequencing, Labeling, Polyacrylamide Gel Electrophoresis

    EC dissociation and RNase A-catalyzed RNA cleavage time courses collected as a function of [KCl]. ( A . ( B  ( A  ( B .
    Figure Legend Snippet: EC dissociation and RNase A-catalyzed RNA cleavage time courses collected as a function of [KCl]. ( A . ( B ( A ( B .

    Techniques Used:

    2) Product Images from "Mammalian DEAD Box Protein Ddx51 Acts in 3? End Maturation of 28S rRNA by Promoting the Release of U8 snoRNA ▿Mammalian DEAD Box Protein Ddx51 Acts in 3? End Maturation of 28S rRNA by Promoting the Release of U8 snoRNA ▿ §"

    Article Title: Mammalian DEAD Box Protein Ddx51 Acts in 3? End Maturation of 28S rRNA by Promoting the Release of U8 snoRNA ▿Mammalian DEAD Box Protein Ddx51 Acts in 3? End Maturation of 28S rRNA by Promoting the Release of U8 snoRNA ▿ §

    Journal: Molecular and Cellular Biology

    doi: 10.1128/MCB.00226-10

    Ddx51 and Nog1 interact in a yeast-two hybrid system in vitro and colocalize in cells. (A) A two-hybrid interaction between Ddx51 (prey) and LexA-fused baits: wild-type Nog1, mutant Nog1G224A with an altered conformation of the GTP-binding domain, and the nuclear protein lamin (negative control). Growth on leucine-deficient medium and activation of the LacZ reporter were used to score the interaction. (B) In vitro binding of Nog1 and Ddx51. In vitro -transcribed and -translated S-tagged Nog1 and Myc-tagged Ddx51 were coincubated with the S-agarose affinity resin for 1 h at room temperature. After washes, bound proteins were eluted with the SDS-PAGE loading buffer and analyzed by Western blotting. In, input; S, supernatant; B, beads. (C) Ddx51 cofractionates with preribosomes. Purified nuclei from Myc-Ddx51-expressing cells were lysed by sonication and separated on a sucrose gradient. Positions of preribosomes are marked by peaks of absorbance at 254 nm. Gradient fractions were analyzed by Western blotting using antibodies against the Myc tag to detect Ddx51 and specific antibodies against ribosome assembly factors Nog1 and Bop1. RNase A treatment prior to loading on a gradient was used to disrupt preribosomes in the nuclear extract. (D) Ddx51 localizes predominantly to the nucleolus. Stably transfected GFP-Ddx51 cells (top row) were costained with an antibody against nucleolar marker fibrillarin followed by Alexa 594-conjugated secondary antibodies (red). Stably transfected Myc-Ddx51 cells (bottom row) were probed with anti-Myc and affinity-purified Nog1 antibodies. Alexa 488 (green) and 568 (red) secondary antibodies were used for the visualization of the endogenous Nog1 and Myc-Ddx51, respectively.
    Figure Legend Snippet: Ddx51 and Nog1 interact in a yeast-two hybrid system in vitro and colocalize in cells. (A) A two-hybrid interaction between Ddx51 (prey) and LexA-fused baits: wild-type Nog1, mutant Nog1G224A with an altered conformation of the GTP-binding domain, and the nuclear protein lamin (negative control). Growth on leucine-deficient medium and activation of the LacZ reporter were used to score the interaction. (B) In vitro binding of Nog1 and Ddx51. In vitro -transcribed and -translated S-tagged Nog1 and Myc-tagged Ddx51 were coincubated with the S-agarose affinity resin for 1 h at room temperature. After washes, bound proteins were eluted with the SDS-PAGE loading buffer and analyzed by Western blotting. In, input; S, supernatant; B, beads. (C) Ddx51 cofractionates with preribosomes. Purified nuclei from Myc-Ddx51-expressing cells were lysed by sonication and separated on a sucrose gradient. Positions of preribosomes are marked by peaks of absorbance at 254 nm. Gradient fractions were analyzed by Western blotting using antibodies against the Myc tag to detect Ddx51 and specific antibodies against ribosome assembly factors Nog1 and Bop1. RNase A treatment prior to loading on a gradient was used to disrupt preribosomes in the nuclear extract. (D) Ddx51 localizes predominantly to the nucleolus. Stably transfected GFP-Ddx51 cells (top row) were costained with an antibody against nucleolar marker fibrillarin followed by Alexa 594-conjugated secondary antibodies (red). Stably transfected Myc-Ddx51 cells (bottom row) were probed with anti-Myc and affinity-purified Nog1 antibodies. Alexa 488 (green) and 568 (red) secondary antibodies were used for the visualization of the endogenous Nog1 and Myc-Ddx51, respectively.

    Techniques Used: In Vitro, Mutagenesis, Binding Assay, Negative Control, Activation Assay, SDS Page, Western Blot, Purification, Expressing, Sonication, Stable Transfection, Transfection, Marker, Affinity Purification

    3) Product Images from "PYRIDOXAMINE ANALOGS SCAVENGE LIPID-DERIVED ?-KETOALDEHYDES AND PROTECT AGAINST H2O2-MEDIATED CYTOTOXICITY †"

    Article Title: PYRIDOXAMINE ANALOGS SCAVENGE LIPID-DERIVED ?-KETOALDEHYDES AND PROTECT AGAINST H2O2-MEDIATED CYTOTOXICITY †

    Journal:

    doi: 10.1021/bi061860g

    PM protects enzymes from inhibition by γKA. A. The synthetic γKA, 15-E 2 -IsoK inhibits activity of RNase A in a dose-dependent manner. RNase A (41 μg/ml) was incubated with 0-200 μM IsoK for 2 h and RNase A activity measured.
    Figure Legend Snippet: PM protects enzymes from inhibition by γKA. A. The synthetic γKA, 15-E 2 -IsoK inhibits activity of RNase A in a dose-dependent manner. RNase A (41 μg/ml) was incubated with 0-200 μM IsoK for 2 h and RNase A activity measured.

    Techniques Used: Inhibition, Activity Assay, Incubation

    4) Product Images from "Localization-dependent translation requires a functional interaction between the 5? and 3? ends of oskar mRNA"

    Article Title: Localization-dependent translation requires a functional interaction between the 5? and 3? ends of oskar mRNA

    Journal: Genes & Development

    doi:

    p50 binds both to the 5′ end of osk ) was incubated and UV cross-linked to proteins in the oocyte extract in the absence of competitor RNA (lane 1 ). Competitions were carried out with a 100-fold excess of either repressor fragment (rep, lane 2 ), Eco RI– Bgl II fragment containing the 5′ activator in sense orientation (5′/act-s, lane 3), or the same Eco RI– Bgl II fragment in antisense orientation (5′/act-as, lane 4 ). Immunoprecipitation of proteins UV cross-linked to radiolabeled repressor fragment (lane 5 ) by anti-Bruno antiserum (lane 6 ) or preimmune serum (lane 7 ). Simultaneous binding of p50 and Bruno was tested by treating with RNase A only after the immunoprecipitation. (Lane 8 ) Anti-Bruno antiserum; (lane 9 ) preimmune serum. We noted that in some cases (as shown here) the intensity of the upper band of the p50 doublet was reduced after coprecipitation. The locations of the 5′ and 3′ competitors in the osk transcript are indicated below. The radiolabeled probe is indicated by an asterisk. The reverse experiment, with activator element RNA as a radioactive probe, and cold activator and repressor RNA elements as unlabeled competitors, yielded the same result with respect to p50 (data not shown).
    Figure Legend Snippet: p50 binds both to the 5′ end of osk ) was incubated and UV cross-linked to proteins in the oocyte extract in the absence of competitor RNA (lane 1 ). Competitions were carried out with a 100-fold excess of either repressor fragment (rep, lane 2 ), Eco RI– Bgl II fragment containing the 5′ activator in sense orientation (5′/act-s, lane 3), or the same Eco RI– Bgl II fragment in antisense orientation (5′/act-as, lane 4 ). Immunoprecipitation of proteins UV cross-linked to radiolabeled repressor fragment (lane 5 ) by anti-Bruno antiserum (lane 6 ) or preimmune serum (lane 7 ). Simultaneous binding of p50 and Bruno was tested by treating with RNase A only after the immunoprecipitation. (Lane 8 ) Anti-Bruno antiserum; (lane 9 ) preimmune serum. We noted that in some cases (as shown here) the intensity of the upper band of the p50 doublet was reduced after coprecipitation. The locations of the 5′ and 3′ competitors in the osk transcript are indicated below. The radiolabeled probe is indicated by an asterisk. The reverse experiment, with activator element RNA as a radioactive probe, and cold activator and repressor RNA elements as unlabeled competitors, yielded the same result with respect to p50 (data not shown).

    Techniques Used: Incubation, Activated Clotting Time Assay, Immunoprecipitation, Binding Assay

    Related Articles

    Incubation:

    Article Title: Immune complexes containing scleroderma-specific autoantibodies induce a profibrotic and proinflammatory phenotype in skin fibroblasts
    Article Snippet: The protein secretion of MMP-2 and Pro-CollagenIα1, the mRNA levels of coIα1 and mmp-1 , and the activation rate of NFκB, p38MAPK, p54SAPK-JNK and p46SAPK-JNK were also evaluated in response to stimulation with ICs from SLE and PAPS sera. .. SSc-ICs were incubated for 1 h at 37 °C with recombinant DNase I or RNase (20 KU/ml and 8 μg/ml, respectively; Worthington Biochemical Corporation, Lakewood, NJ, USA) and then added to cells for 24 h. RT-PCR for tlr2 , tlr3 , ifn - α and et-1 was then performed. .. Cells were preincubated for 1 h at 37 °C with inhibitors of NFκB (MG-132, 20 μmol; Sigma-Aldrich) and p38MAPK (SB202190, 20 μmol; Cell Signaling Technology).

    Article Title: Immune complexes containing scleroderma-specific autoantibodies induce a profibrotic and proinflammatory phenotype in skin fibroblasts
    Article Snippet: SLE and APS immune complexes The protein secretion of MMP-2 and Pro-CollagenIα1, the mRNA levels of coIα1 and mmp-1 , and the activation rate of NFκB, p38MAPK, p54SAPK-JNK and p46SAPK-JNK were also evaluated in response to stimulation with ICs from SLE and PAPS sera. .. DNase and RNase treatment SSc-ICs were incubated for 1 h at 37 °C with recombinant DNase I or RNase (20 KU/ml and 8 μg/ml, respectively; Worthington Biochemical Corporation, Lakewood, NJ, USA) and then added to cells for 24 h. RT-PCR for tlr2 , tlr3 , ifn -α and et-1 was then performed. .. NFκB and p38MAPK inhibitors Cells were preincubated for 1 h at 37 °C with inhibitors of NFκB (MG-132, 20 μmol; Sigma-Aldrich) and p38MAPK (SB202190, 20 μmol; Cell Signaling Technology).

    Article Title: Mammalian DEAD Box Protein Ddx51 Acts in 3? End Maturation of 28S rRNA by Promoting the Release of U8 snoRNA ▿Mammalian DEAD Box Protein Ddx51 Acts in 3? End Maturation of 28S rRNA by Promoting the Release of U8 snoRNA ▿ §
    Article Snippet: To isolate proteins, we added 10 μg of bovine serum albumin to each 1-ml fraction, followed by trichloroacetic acid to a 10% final concentration. .. The pellet was washed with 1 ml of ethanol and 1 ml of acetone, air dried, resuspended in 20 mM Tris-HCl (pH 6.8)-1 mM EDTA-50 U/ml RNase A (Worthington), incubated for 15 min at 37°C, and mixed with SDS-PAGE loading buffer for separation on a gel and Western blotting. .. We identified Ddx51, a previously uncharacterized protein belonging to the DEAD box helicase family , in a two-hybrid screen for proteins interacting with the mammalian ribosome assembly factor Nog1.

    Recombinant:

    Article Title: Immune complexes containing scleroderma-specific autoantibodies induce a profibrotic and proinflammatory phenotype in skin fibroblasts
    Article Snippet: The protein secretion of MMP-2 and Pro-CollagenIα1, the mRNA levels of coIα1 and mmp-1 , and the activation rate of NFκB, p38MAPK, p54SAPK-JNK and p46SAPK-JNK were also evaluated in response to stimulation with ICs from SLE and PAPS sera. .. SSc-ICs were incubated for 1 h at 37 °C with recombinant DNase I or RNase (20 KU/ml and 8 μg/ml, respectively; Worthington Biochemical Corporation, Lakewood, NJ, USA) and then added to cells for 24 h. RT-PCR for tlr2 , tlr3 , ifn - α and et-1 was then performed. .. Cells were preincubated for 1 h at 37 °C with inhibitors of NFκB (MG-132, 20 μmol; Sigma-Aldrich) and p38MAPK (SB202190, 20 μmol; Cell Signaling Technology).

    Article Title: Immune complexes containing scleroderma-specific autoantibodies induce a profibrotic and proinflammatory phenotype in skin fibroblasts
    Article Snippet: SLE and APS immune complexes The protein secretion of MMP-2 and Pro-CollagenIα1, the mRNA levels of coIα1 and mmp-1 , and the activation rate of NFκB, p38MAPK, p54SAPK-JNK and p46SAPK-JNK were also evaluated in response to stimulation with ICs from SLE and PAPS sera. .. DNase and RNase treatment SSc-ICs were incubated for 1 h at 37 °C with recombinant DNase I or RNase (20 KU/ml and 8 μg/ml, respectively; Worthington Biochemical Corporation, Lakewood, NJ, USA) and then added to cells for 24 h. RT-PCR for tlr2 , tlr3 , ifn -α and et-1 was then performed. .. NFκB and p38MAPK inhibitors Cells were preincubated for 1 h at 37 °C with inhibitors of NFκB (MG-132, 20 μmol; Sigma-Aldrich) and p38MAPK (SB202190, 20 μmol; Cell Signaling Technology).

    Reverse Transcription Polymerase Chain Reaction:

    Article Title: Immune complexes containing scleroderma-specific autoantibodies induce a profibrotic and proinflammatory phenotype in skin fibroblasts
    Article Snippet: The protein secretion of MMP-2 and Pro-CollagenIα1, the mRNA levels of coIα1 and mmp-1 , and the activation rate of NFκB, p38MAPK, p54SAPK-JNK and p46SAPK-JNK were also evaluated in response to stimulation with ICs from SLE and PAPS sera. .. SSc-ICs were incubated for 1 h at 37 °C with recombinant DNase I or RNase (20 KU/ml and 8 μg/ml, respectively; Worthington Biochemical Corporation, Lakewood, NJ, USA) and then added to cells for 24 h. RT-PCR for tlr2 , tlr3 , ifn - α and et-1 was then performed. .. Cells were preincubated for 1 h at 37 °C with inhibitors of NFκB (MG-132, 20 μmol; Sigma-Aldrich) and p38MAPK (SB202190, 20 μmol; Cell Signaling Technology).

    Article Title: Immune complexes containing scleroderma-specific autoantibodies induce a profibrotic and proinflammatory phenotype in skin fibroblasts
    Article Snippet: SLE and APS immune complexes The protein secretion of MMP-2 and Pro-CollagenIα1, the mRNA levels of coIα1 and mmp-1 , and the activation rate of NFκB, p38MAPK, p54SAPK-JNK and p46SAPK-JNK were also evaluated in response to stimulation with ICs from SLE and PAPS sera. .. DNase and RNase treatment SSc-ICs were incubated for 1 h at 37 °C with recombinant DNase I or RNase (20 KU/ml and 8 μg/ml, respectively; Worthington Biochemical Corporation, Lakewood, NJ, USA) and then added to cells for 24 h. RT-PCR for tlr2 , tlr3 , ifn -α and et-1 was then performed. .. NFκB and p38MAPK inhibitors Cells were preincubated for 1 h at 37 °C with inhibitors of NFκB (MG-132, 20 μmol; Sigma-Aldrich) and p38MAPK (SB202190, 20 μmol; Cell Signaling Technology).

    Cell Cycle Assay:

    Article Title: Identification and characterization of circulating human transitional B cells
    Article Snippet: The caspase inhibitor z-VAD was used at 20μM (EMD Biosciences, San Diego, CA). .. Cell-cycle analysis was performed using 0.05 mg/mL propidium iodide in hypotonic sodium citrate with 1800 U/mL ribonuclease A (Worthington Biochemical Corp, Lakewood, NJ). .. Single-cell polymerase chain reaction (PCR) was used to amplify rear-ranged heavy-chain Ig genes from genomic DNA.

    SDS Page:

    Article Title: Mammalian DEAD Box Protein Ddx51 Acts in 3? End Maturation of 28S rRNA by Promoting the Release of U8 snoRNA ▿Mammalian DEAD Box Protein Ddx51 Acts in 3? End Maturation of 28S rRNA by Promoting the Release of U8 snoRNA ▿ §
    Article Snippet: To isolate proteins, we added 10 μg of bovine serum albumin to each 1-ml fraction, followed by trichloroacetic acid to a 10% final concentration. .. The pellet was washed with 1 ml of ethanol and 1 ml of acetone, air dried, resuspended in 20 mM Tris-HCl (pH 6.8)-1 mM EDTA-50 U/ml RNase A (Worthington), incubated for 15 min at 37°C, and mixed with SDS-PAGE loading buffer for separation on a gel and Western blotting. .. We identified Ddx51, a previously uncharacterized protein belonging to the DEAD box helicase family , in a two-hybrid screen for proteins interacting with the mammalian ribosome assembly factor Nog1.

    Western Blot:

    Article Title: Mammalian DEAD Box Protein Ddx51 Acts in 3? End Maturation of 28S rRNA by Promoting the Release of U8 snoRNA ▿Mammalian DEAD Box Protein Ddx51 Acts in 3? End Maturation of 28S rRNA by Promoting the Release of U8 snoRNA ▿ §
    Article Snippet: To isolate proteins, we added 10 μg of bovine serum albumin to each 1-ml fraction, followed by trichloroacetic acid to a 10% final concentration. .. The pellet was washed with 1 ml of ethanol and 1 ml of acetone, air dried, resuspended in 20 mM Tris-HCl (pH 6.8)-1 mM EDTA-50 U/ml RNase A (Worthington), incubated for 15 min at 37°C, and mixed with SDS-PAGE loading buffer for separation on a gel and Western blotting. .. We identified Ddx51, a previously uncharacterized protein belonging to the DEAD box helicase family , in a two-hybrid screen for proteins interacting with the mammalian ribosome assembly factor Nog1.

    Purification:

    Article Title: Protein Phase Behavior in Aqueous Solutions: Crystallization, Liquid-Liquid Phase Separation, Gels, and Aggregates
    Article Snippet: Third, the correlation between the positions of the aggregation and solubility lines and the second osmotic virial coefficient is discussed, and finally, failure of the theoretical phase diagram ( ) to capture the temperature dependence observed experimentally is emphasized to show the limit of current theoretical approaches. .. Ovalbumin was obtained from fresh single-comb white Leghorn eggs following the purification protocol used by Judge et al. ( , ). β -Lactoglobulin from bovine milk (L0130) and lysozyme from chicken egg white (L6876) were purchased from Sigma (St. Louis, MO), STI (21730) was obtained from USB (Cleveland, OH), and ribonuclease A (LS003433) was purchased from Worthington (Lakewood, NJ). .. Sodium chloride (S-271) and sodium phosphate (P-285) were obtained from Fisher Scientific (Hampton, NH).

    Synthesized:

    Article Title: PYRIDOXAMINE ANALOGS SCAVENGE LIPID-DERIVED ?-KETOALDEHYDES AND PROTECT AGAINST H2O2-MEDIATED CYTOTOXICITY †
    Article Snippet: .. Salicylamine was purchased from Fischer Scientific USA (Pittsburgh, PA) and additional salicylamine hydrochloride was synthesized by the method of Reany et al ( ) RNase A was obtained from Worthington Biochemical (Lakewood, NJ). .. Dazoxiben was a generous gift from Pfizer Limited (Sandwich, U.K.).

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  • 93
    Worthington Biochemical rnase a
    Ddx51 and Nog1 interact in a yeast-two hybrid system in vitro and colocalize in cells. (A) A two-hybrid interaction between Ddx51 (prey) and LexA-fused baits: wild-type Nog1, mutant Nog1G224A with an altered conformation of the GTP-binding domain, and the nuclear protein lamin (negative control). Growth on leucine-deficient medium and activation of the LacZ reporter were used to score the interaction. (B) In vitro binding of Nog1 and Ddx51. In vitro -transcribed and -translated S-tagged Nog1 and Myc-tagged Ddx51 were coincubated with the S-agarose affinity resin for 1 h at room temperature. After washes, bound proteins were eluted with the SDS-PAGE loading buffer and analyzed by Western blotting. In, input; S, supernatant; B, beads. (C) Ddx51 cofractionates with preribosomes. Purified nuclei from Myc-Ddx51-expressing cells were lysed by sonication and separated on a sucrose gradient. Positions of preribosomes are marked by peaks of absorbance at 254 nm. Gradient fractions were analyzed by Western blotting using antibodies against the Myc tag to detect Ddx51 and specific antibodies against ribosome assembly factors Nog1 and Bop1. <t>RNase</t> A treatment prior to loading on a gradient was used to disrupt preribosomes in the nuclear extract. (D) Ddx51 localizes predominantly to the nucleolus. Stably transfected GFP-Ddx51 cells (top row) were costained with an antibody against nucleolar marker fibrillarin followed by Alexa 594-conjugated secondary antibodies (red). Stably transfected Myc-Ddx51 cells (bottom row) were probed with anti-Myc and affinity-purified Nog1 antibodies. Alexa 488 (green) and 568 (red) secondary antibodies were used for the visualization of the endogenous Nog1 and Myc-Ddx51, respectively.
    Rnase A, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rnase a/product/Worthington Biochemical
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rnase a - by Bioz Stars, 2021-03
    93/100 stars
      Buy from Supplier

    93
    Worthington Biochemical rnase t1
    Components of the S. pombe <t>RNase</t> MRP complex. (A) RNA component of S. pombe RNase MRP ( mrp1 ). RNA was separated from the purified RNase MRP with acid-phenol treatment and subjected to 8 M urea-7.5% PAGE (SYBR Gold staining). (B) Nucleotide sequence of S. pombe mrp1 RNA and the fragments used for the sequence analysis. Solid or dashed double-headed arrows show the fragments obtained by digestion with <t>RNase</t> T1 or MazF/PemK RNase, respectively. RNase T1 fragments were identified by Ariadne search program, and PemK/MazF fragments were identified by manual inspection of MS/MS spectra (see also Table S2 ). m 3 Gppp, trimethylguanosine cap. (C) Protein components of S. pombe RNase MRP. The RNase-MRP preparation affinity-purified using FEM3-tagged Rmp1 as bait (Rmp1-FEM3) was separated by SDS-PAGE and visualized with Coomassie Brilliant Blue staining. The proteins identified by LC-MS/MS are shown on the right (see also Table S3 and Figure S6 ). The IgG probably resulted from sloughing from the beads during the affinity purification.
    Rnase T1, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rnase t1/product/Worthington Biochemical
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rnase t1 - by Bioz Stars, 2021-03
    93/100 stars
      Buy from Supplier

    Image Search Results


    Ddx51 and Nog1 interact in a yeast-two hybrid system in vitro and colocalize in cells. (A) A two-hybrid interaction between Ddx51 (prey) and LexA-fused baits: wild-type Nog1, mutant Nog1G224A with an altered conformation of the GTP-binding domain, and the nuclear protein lamin (negative control). Growth on leucine-deficient medium and activation of the LacZ reporter were used to score the interaction. (B) In vitro binding of Nog1 and Ddx51. In vitro -transcribed and -translated S-tagged Nog1 and Myc-tagged Ddx51 were coincubated with the S-agarose affinity resin for 1 h at room temperature. After washes, bound proteins were eluted with the SDS-PAGE loading buffer and analyzed by Western blotting. In, input; S, supernatant; B, beads. (C) Ddx51 cofractionates with preribosomes. Purified nuclei from Myc-Ddx51-expressing cells were lysed by sonication and separated on a sucrose gradient. Positions of preribosomes are marked by peaks of absorbance at 254 nm. Gradient fractions were analyzed by Western blotting using antibodies against the Myc tag to detect Ddx51 and specific antibodies against ribosome assembly factors Nog1 and Bop1. RNase A treatment prior to loading on a gradient was used to disrupt preribosomes in the nuclear extract. (D) Ddx51 localizes predominantly to the nucleolus. Stably transfected GFP-Ddx51 cells (top row) were costained with an antibody against nucleolar marker fibrillarin followed by Alexa 594-conjugated secondary antibodies (red). Stably transfected Myc-Ddx51 cells (bottom row) were probed with anti-Myc and affinity-purified Nog1 antibodies. Alexa 488 (green) and 568 (red) secondary antibodies were used for the visualization of the endogenous Nog1 and Myc-Ddx51, respectively.

    Journal: Molecular and Cellular Biology

    Article Title: Mammalian DEAD Box Protein Ddx51 Acts in 3? End Maturation of 28S rRNA by Promoting the Release of U8 snoRNA ▿Mammalian DEAD Box Protein Ddx51 Acts in 3? End Maturation of 28S rRNA by Promoting the Release of U8 snoRNA ▿ §

    doi: 10.1128/MCB.00226-10

    Figure Lengend Snippet: Ddx51 and Nog1 interact in a yeast-two hybrid system in vitro and colocalize in cells. (A) A two-hybrid interaction between Ddx51 (prey) and LexA-fused baits: wild-type Nog1, mutant Nog1G224A with an altered conformation of the GTP-binding domain, and the nuclear protein lamin (negative control). Growth on leucine-deficient medium and activation of the LacZ reporter were used to score the interaction. (B) In vitro binding of Nog1 and Ddx51. In vitro -transcribed and -translated S-tagged Nog1 and Myc-tagged Ddx51 were coincubated with the S-agarose affinity resin for 1 h at room temperature. After washes, bound proteins were eluted with the SDS-PAGE loading buffer and analyzed by Western blotting. In, input; S, supernatant; B, beads. (C) Ddx51 cofractionates with preribosomes. Purified nuclei from Myc-Ddx51-expressing cells were lysed by sonication and separated on a sucrose gradient. Positions of preribosomes are marked by peaks of absorbance at 254 nm. Gradient fractions were analyzed by Western blotting using antibodies against the Myc tag to detect Ddx51 and specific antibodies against ribosome assembly factors Nog1 and Bop1. RNase A treatment prior to loading on a gradient was used to disrupt preribosomes in the nuclear extract. (D) Ddx51 localizes predominantly to the nucleolus. Stably transfected GFP-Ddx51 cells (top row) were costained with an antibody against nucleolar marker fibrillarin followed by Alexa 594-conjugated secondary antibodies (red). Stably transfected Myc-Ddx51 cells (bottom row) were probed with anti-Myc and affinity-purified Nog1 antibodies. Alexa 488 (green) and 568 (red) secondary antibodies were used for the visualization of the endogenous Nog1 and Myc-Ddx51, respectively.

    Article Snippet: The pellet was washed with 1 ml of ethanol and 1 ml of acetone, air dried, resuspended in 20 mM Tris-HCl (pH 6.8)-1 mM EDTA-50 U/ml RNase A (Worthington), incubated for 15 min at 37°C, and mixed with SDS-PAGE loading buffer for separation on a gel and Western blotting.

    Techniques: In Vitro, Mutagenesis, Binding Assay, Negative Control, Activation Assay, SDS Page, Western Blot, Purification, Expressing, Sonication, Stable Transfection, Transfection, Marker, Affinity Purification

    PM protects enzymes from inhibition by γKA. A. The synthetic γKA, 15-E 2 -IsoK inhibits activity of RNase A in a dose-dependent manner. RNase A (41 μg/ml) was incubated with 0-200 μM IsoK for 2 h and RNase A activity measured.

    Journal:

    Article Title: PYRIDOXAMINE ANALOGS SCAVENGE LIPID-DERIVED ?-KETOALDEHYDES AND PROTECT AGAINST H2O2-MEDIATED CYTOTOXICITY †

    doi: 10.1021/bi061860g

    Figure Lengend Snippet: PM protects enzymes from inhibition by γKA. A. The synthetic γKA, 15-E 2 -IsoK inhibits activity of RNase A in a dose-dependent manner. RNase A (41 μg/ml) was incubated with 0-200 μM IsoK for 2 h and RNase A activity measured.

    Article Snippet: Salicylamine was purchased from Fischer Scientific USA (Pittsburgh, PA) and additional salicylamine hydrochloride was synthesized by the method of Reany et al ( ) RNase A was obtained from Worthington Biochemical (Lakewood, NJ).

    Techniques: Inhibition, Activity Assay, Incubation

    Comparison between (○) b 2 and (▪) aggregation line at pH 7, 23°C for ( A ) ovalbumin in (NH 4 ) 2 SO 4 , ( B ) ribonuclease A in (NH 4 ) 2 SO 4 , ( C ) lysozyme in (NH 4 ) 2 SO 4 , and ( D ) lysozyme in NaCl. (⋄) Solubility line for ( D ) lysozyme

    Journal:

    Article Title: Protein Phase Behavior in Aqueous Solutions: Crystallization, Liquid-Liquid Phase Separation, Gels, and Aggregates

    doi: 10.1529/biophysj.107.116152

    Figure Lengend Snippet: Comparison between (○) b 2 and (▪) aggregation line at pH 7, 23°C for ( A ) ovalbumin in (NH 4 ) 2 SO 4 , ( B ) ribonuclease A in (NH 4 ) 2 SO 4 , ( C ) lysozyme in (NH 4 ) 2 SO 4 , and ( D ) lysozyme in NaCl. (⋄) Solubility line for ( D ) lysozyme

    Article Snippet: Ovalbumin was obtained from fresh single-comb white Leghorn eggs following the purification protocol used by Judge et al. ( , ). β -Lactoglobulin from bovine milk (L0130) and lysozyme from chicken egg white (L6876) were purchased from Sigma (St. Louis, MO), STI (21730) was obtained from USB (Cleveland, OH), and ribonuclease A (LS003433) was purchased from Worthington (Lakewood, NJ).

    Techniques: Solubility

    Aggregation lines for (♦) ribonuclease A, (▴) STI, (▾) lysozyme, (•) ovalbumin, (□)  β -lactoglobulin B, and (▪)  β -lactoglobulin A in ammonium sulfate, and (∇) lysozyme in sodium chloride.

    Journal:

    Article Title: Protein Phase Behavior in Aqueous Solutions: Crystallization, Liquid-Liquid Phase Separation, Gels, and Aggregates

    doi: 10.1529/biophysj.107.116152

    Figure Lengend Snippet: Aggregation lines for (♦) ribonuclease A, (▴) STI, (▾) lysozyme, (•) ovalbumin, (□) β -lactoglobulin B, and (▪) β -lactoglobulin A in ammonium sulfate, and (∇) lysozyme in sodium chloride.

    Article Snippet: Ovalbumin was obtained from fresh single-comb white Leghorn eggs following the purification protocol used by Judge et al. ( , ). β -Lactoglobulin from bovine milk (L0130) and lysozyme from chicken egg white (L6876) were purchased from Sigma (St. Louis, MO), STI (21730) was obtained from USB (Cleveland, OH), and ribonuclease A (LS003433) was purchased from Worthington (Lakewood, NJ).

    Techniques:

    Phase behavior of ribonuclease A as a function of the protein concentration 1 day after preparation in 1.6 M ammonium sulfate, 100 mM sodium phosphate, pH 7, 23°C. The scale bar represents 0.3 mm.

    Journal:

    Article Title: Protein Phase Behavior in Aqueous Solutions: Crystallization, Liquid-Liquid Phase Separation, Gels, and Aggregates

    doi: 10.1529/biophysj.107.116152

    Figure Lengend Snippet: Phase behavior of ribonuclease A as a function of the protein concentration 1 day after preparation in 1.6 M ammonium sulfate, 100 mM sodium phosphate, pH 7, 23°C. The scale bar represents 0.3 mm.

    Article Snippet: Ovalbumin was obtained from fresh single-comb white Leghorn eggs following the purification protocol used by Judge et al. ( , ). β -Lactoglobulin from bovine milk (L0130) and lysozyme from chicken egg white (L6876) were purchased from Sigma (St. Louis, MO), STI (21730) was obtained from USB (Cleveland, OH), and ribonuclease A (LS003433) was purchased from Worthington (Lakewood, NJ).

    Techniques: Protein Concentration

    (▪) First and (□) second aggregation lines for ( A ) ovalbumin and ( B ) ribonuclease A at 23°C. The pH was maintained at pH 7 by 5 mM sodium phosphate for ovalbumin and 100 mM sodium phosphate for ribonuclease A. The dotted line delimits

    Journal:

    Article Title: Protein Phase Behavior in Aqueous Solutions: Crystallization, Liquid-Liquid Phase Separation, Gels, and Aggregates

    doi: 10.1529/biophysj.107.116152

    Figure Lengend Snippet: (▪) First and (□) second aggregation lines for ( A ) ovalbumin and ( B ) ribonuclease A at 23°C. The pH was maintained at pH 7 by 5 mM sodium phosphate for ovalbumin and 100 mM sodium phosphate for ribonuclease A. The dotted line delimits

    Article Snippet: Ovalbumin was obtained from fresh single-comb white Leghorn eggs following the purification protocol used by Judge et al. ( , ). β -Lactoglobulin from bovine milk (L0130) and lysozyme from chicken egg white (L6876) were purchased from Sigma (St. Louis, MO), STI (21730) was obtained from USB (Cleveland, OH), and ribonuclease A (LS003433) was purchased from Worthington (Lakewood, NJ).

    Techniques:

    Effect of temperature on aggregation line for ( A ) ovalbumin, ( B ) ribonuclease A, ( C ) STI, ( D )  β -lactoglobulin A, ( E )  β -lactoglobulin B, and ( F ) lysozyme as a function of (NH 4 ) 2 SO 4  concentration at pH 7. (▴) 4°C, (•)

    Journal:

    Article Title: Protein Phase Behavior in Aqueous Solutions: Crystallization, Liquid-Liquid Phase Separation, Gels, and Aggregates

    doi: 10.1529/biophysj.107.116152

    Figure Lengend Snippet: Effect of temperature on aggregation line for ( A ) ovalbumin, ( B ) ribonuclease A, ( C ) STI, ( D ) β -lactoglobulin A, ( E ) β -lactoglobulin B, and ( F ) lysozyme as a function of (NH 4 ) 2 SO 4 concentration at pH 7. (▴) 4°C, (•)

    Article Snippet: Ovalbumin was obtained from fresh single-comb white Leghorn eggs following the purification protocol used by Judge et al. ( , ). β -Lactoglobulin from bovine milk (L0130) and lysozyme from chicken egg white (L6876) were purchased from Sigma (St. Louis, MO), STI (21730) was obtained from USB (Cleveland, OH), and ribonuclease A (LS003433) was purchased from Worthington (Lakewood, NJ).

    Techniques: Concentration Assay

    Components of the S. pombe RNase MRP complex. (A) RNA component of S. pombe RNase MRP ( mrp1 ). RNA was separated from the purified RNase MRP with acid-phenol treatment and subjected to 8 M urea-7.5% PAGE (SYBR Gold staining). (B) Nucleotide sequence of S. pombe mrp1 RNA and the fragments used for the sequence analysis. Solid or dashed double-headed arrows show the fragments obtained by digestion with RNase T1 or MazF/PemK RNase, respectively. RNase T1 fragments were identified by Ariadne search program, and PemK/MazF fragments were identified by manual inspection of MS/MS spectra (see also Table S2 ). m 3 Gppp, trimethylguanosine cap. (C) Protein components of S. pombe RNase MRP. The RNase-MRP preparation affinity-purified using FEM3-tagged Rmp1 as bait (Rmp1-FEM3) was separated by SDS-PAGE and visualized with Coomassie Brilliant Blue staining. The proteins identified by LC-MS/MS are shown on the right (see also Table S3 and Figure S6 ). The IgG probably resulted from sloughing from the beads during the affinity purification.

    Journal: PLoS ONE

    Article Title: RNase MRP Cleaves Pre-tRNASer-Met in the tRNA Maturation Pathway

    doi: 10.1371/journal.pone.0112488

    Figure Lengend Snippet: Components of the S. pombe RNase MRP complex. (A) RNA component of S. pombe RNase MRP ( mrp1 ). RNA was separated from the purified RNase MRP with acid-phenol treatment and subjected to 8 M urea-7.5% PAGE (SYBR Gold staining). (B) Nucleotide sequence of S. pombe mrp1 RNA and the fragments used for the sequence analysis. Solid or dashed double-headed arrows show the fragments obtained by digestion with RNase T1 or MazF/PemK RNase, respectively. RNase T1 fragments were identified by Ariadne search program, and PemK/MazF fragments were identified by manual inspection of MS/MS spectra (see also Table S2 ). m 3 Gppp, trimethylguanosine cap. (C) Protein components of S. pombe RNase MRP. The RNase-MRP preparation affinity-purified using FEM3-tagged Rmp1 as bait (Rmp1-FEM3) was separated by SDS-PAGE and visualized with Coomassie Brilliant Blue staining. The proteins identified by LC-MS/MS are shown on the right (see also Table S3 and Figure S6 ). The IgG probably resulted from sloughing from the beads during the affinity purification.

    Article Snippet: RNases for in-gel digestion, RNase T1 (Worthington), MazF (Takara Bio), and PemK were further purified before use .

    Techniques: Purification, Polyacrylamide Gel Electrophoresis, Staining, Sequencing, Mass Spectrometry, Affinity Purification, SDS Page, Liquid Chromatography with Mass Spectroscopy

    Isolation of the catalytically active core of RNase MRP. (A) Urea-PAGE profiles of mrp1 RNA fragments produced by RNase A–mediated limited nucleolysis of RNase MRP (SYBR Gold staining). The S. pombe RNase MRP obtained from a 2-l culture of logarithmically growing cells was digested on FLAG M2 agarose beads at 4°C for 1 h with increasing amounts of RNase A. Lane 1, no RNase A; lane 2, 1 µg/ml; lane 3, 5 µg/ml; lane 4, 10 µg/ml. A portion (5%) of each reaction was loaded per lane. (B) A core of RNase MRP produced by RNase A–mediated limited nucleolysis cleaves pre-tRNA Ser-Met . RNase MRP (pulled down with tagged Rmp1 from JJ095 cells using FLAG M2 agarose) and the mock preparation (pulled down from SP6 cells) were incubated with (+) or without (−) RNase A. Each digested preparation (1 pmol each) was incubated with pre-tRNA Ser-Met (8 pmol) at 37°C for 30 min, and each reaction mixture was subjected to urea-PAGE (SYBR-Gold staining). Band 1, mrp1 RNA; 2, pre-tRNA Ser-Met ; 3, pre-tRNA Ser +trailer; 4, tRNA Met . (C) Double-reciprocal plot of the catalytic reaction of RNase A–mediated partial nucleolysis of RNase MRP. The reaction was performed for 30 min with synthetic pre-tRNA Ser-Met as a substrate under the conditions as in Figure 3B . The plot indicates K M of 0.974 µM and Vmax of 12.9 nM/min. (D) RNA fragments produced by RNase T1 digestion of Band 1 (indicated by solid lines) and Band 2 (broken lines) in (A). The fragments identified by LC-MS/MS are mapped on the mrp1 RNA sequence, where the conserved helices and strands of mrp1 [1] , [29] , [31] are shown in shaded boxes. (E) Nuclease-resistant regions mapped in the secondary structure of mrp1 . The map was according to the previous study [2] with modifications made by the assistance of CentroidHomFold ( http://www.ncrna.org/centroidhomfold ). Dashed-line boxes denote the two putative domains [2] . The nuclease-resistant region is shaded gray. The nucleotides with dotted bar are the consensus sequence ANAGNNA known as the mCR-IV motif [2] . (F) SDS-PAGE profiles of the protein components of RNase MRP before (−) and after (+) RNase A–mediated limited nucleolysis (Coomassie Brilliant Blue staining). The proteins assigned by LC-MS/MS are also shown. Note that the catalytic core of RNase MRP produced by partial nucleolysis contains 8 (underlined) of the 11 total subunits.

    Journal: PLoS ONE

    Article Title: RNase MRP Cleaves Pre-tRNASer-Met in the tRNA Maturation Pathway

    doi: 10.1371/journal.pone.0112488

    Figure Lengend Snippet: Isolation of the catalytically active core of RNase MRP. (A) Urea-PAGE profiles of mrp1 RNA fragments produced by RNase A–mediated limited nucleolysis of RNase MRP (SYBR Gold staining). The S. pombe RNase MRP obtained from a 2-l culture of logarithmically growing cells was digested on FLAG M2 agarose beads at 4°C for 1 h with increasing amounts of RNase A. Lane 1, no RNase A; lane 2, 1 µg/ml; lane 3, 5 µg/ml; lane 4, 10 µg/ml. A portion (5%) of each reaction was loaded per lane. (B) A core of RNase MRP produced by RNase A–mediated limited nucleolysis cleaves pre-tRNA Ser-Met . RNase MRP (pulled down with tagged Rmp1 from JJ095 cells using FLAG M2 agarose) and the mock preparation (pulled down from SP6 cells) were incubated with (+) or without (−) RNase A. Each digested preparation (1 pmol each) was incubated with pre-tRNA Ser-Met (8 pmol) at 37°C for 30 min, and each reaction mixture was subjected to urea-PAGE (SYBR-Gold staining). Band 1, mrp1 RNA; 2, pre-tRNA Ser-Met ; 3, pre-tRNA Ser +trailer; 4, tRNA Met . (C) Double-reciprocal plot of the catalytic reaction of RNase A–mediated partial nucleolysis of RNase MRP. The reaction was performed for 30 min with synthetic pre-tRNA Ser-Met as a substrate under the conditions as in Figure 3B . The plot indicates K M of 0.974 µM and Vmax of 12.9 nM/min. (D) RNA fragments produced by RNase T1 digestion of Band 1 (indicated by solid lines) and Band 2 (broken lines) in (A). The fragments identified by LC-MS/MS are mapped on the mrp1 RNA sequence, where the conserved helices and strands of mrp1 [1] , [29] , [31] are shown in shaded boxes. (E) Nuclease-resistant regions mapped in the secondary structure of mrp1 . The map was according to the previous study [2] with modifications made by the assistance of CentroidHomFold ( http://www.ncrna.org/centroidhomfold ). Dashed-line boxes denote the two putative domains [2] . The nuclease-resistant region is shaded gray. The nucleotides with dotted bar are the consensus sequence ANAGNNA known as the mCR-IV motif [2] . (F) SDS-PAGE profiles of the protein components of RNase MRP before (−) and after (+) RNase A–mediated limited nucleolysis (Coomassie Brilliant Blue staining). The proteins assigned by LC-MS/MS are also shown. Note that the catalytic core of RNase MRP produced by partial nucleolysis contains 8 (underlined) of the 11 total subunits.

    Article Snippet: RNases for in-gel digestion, RNase T1 (Worthington), MazF (Takara Bio), and PemK were further purified before use .

    Techniques: Isolation, Polyacrylamide Gel Electrophoresis, Produced, Staining, Incubation, Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry, Sequencing, SDS Page