proteinase k  (Thermo Fisher)


Bioz Verified Symbol Thermo Fisher is a verified supplier  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 99

    Structured Review

    Thermo Fisher proteinase k
    No change in <t>Proteinase-K-resistant</t> aggregates in curcumin diet mice. (A) Western blot detection of Syn-GFP microaggregates, following Proteinase-K digestion of synaptosome and cytosolic protein fractions from control and curcumin diet mice. (B) Quantification of Syn-GFP band intensity shows no change in the resistant fraction between control and curcumin diet mice.
    Proteinase K, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 296 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/proteinase k/product/Thermo Fisher
    Average 99 stars, based on 296 article reviews
    Price from $9.99 to $1999.99
    proteinase k - by Bioz Stars, 2020-04
    99/100 stars

    Images

    1) Product Images from "Curcumin Treatment Improves Motor Behavior in α-Synuclein Transgenic Mice"

    Article Title: Curcumin Treatment Improves Motor Behavior in α-Synuclein Transgenic Mice

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0128510

    No change in Proteinase-K-resistant aggregates in curcumin diet mice. (A) Western blot detection of Syn-GFP microaggregates, following Proteinase-K digestion of synaptosome and cytosolic protein fractions from control and curcumin diet mice. (B) Quantification of Syn-GFP band intensity shows no change in the resistant fraction between control and curcumin diet mice.
    Figure Legend Snippet: No change in Proteinase-K-resistant aggregates in curcumin diet mice. (A) Western blot detection of Syn-GFP microaggregates, following Proteinase-K digestion of synaptosome and cytosolic protein fractions from control and curcumin diet mice. (B) Quantification of Syn-GFP band intensity shows no change in the resistant fraction between control and curcumin diet mice.

    Techniques Used: Mouse Assay, Western Blot

    2) Product Images from "Simple Silica Column–Based Method to Quantify Inorganic Polyphosphates in Cartilage and Other Tissues"

    Article Title: Simple Silica Column–Based Method to Quantify Inorganic Polyphosphates in Cartilage and Other Tissues

    Journal: Cartilage

    doi: 10.1177/1947603517690856

    Proteinase K pretreatment enhances polyP recovery. Seven nanomoles polyP samples mixed with various concentrations of fetal bovine serum (FBS) were incubated in the presence (+PK) or absence (–PK) of proteinase K (1 mg/mL), alone or together with
    Figure Legend Snippet: Proteinase K pretreatment enhances polyP recovery. Seven nanomoles polyP samples mixed with various concentrations of fetal bovine serum (FBS) were incubated in the presence (+PK) or absence (–PK) of proteinase K (1 mg/mL), alone or together with

    Techniques Used: Incubation

    3) Product Images from "Antagonistic Potential of Native Trichoderma viride Strain against Potent Tea Fungal Pathogens in North East India"

    Article Title: Antagonistic Potential of Native Trichoderma viride Strain against Potent Tea Fungal Pathogens in North East India

    Journal: The Plant Pathology Journal

    doi: 10.5423/PPJ.OA.01.2015.0004

    Effects of proteinase K and heat on the antifungal activity of culture filtrates of Trichoderma strain SDRLIN1to phytopathogenic fungi.
    Figure Legend Snippet: Effects of proteinase K and heat on the antifungal activity of culture filtrates of Trichoderma strain SDRLIN1to phytopathogenic fungi.

    Techniques Used: Activity Assay

    4) Product Images from "Acinetobacter baumannii Outer Membrane Vesicles Elicit a Potent Innate Immune Response via Membrane Proteins"

    Article Title: Acinetobacter baumannii Outer Membrane Vesicles Elicit a Potent Innate Immune Response via Membrane Proteins

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0071751

    The pro-inflammatory response of HEp-2 cells to A. baumannii OMVs treated with proteinase K and EDTA. (A) Protein profiles of A. baumannii OMVs. Lane M, size marker; 1, purified intact OMVs; 2, OMVs treated with EDTA; 3, OMVs treated with proteinase K; 4, proteinase K. (B) Expression of pro-inflammatory cytokine genes to proteinase K- and EDTA-treated A. baumannii OMVs was assessed by quantitative real-time PCR. HEp-2 cells were treated with the same concentration (15 µg/ml) of A. baumannii OMVs for 24 h as a positive control. Data are presented as mean ± SD of duplicate determinations.
    Figure Legend Snippet: The pro-inflammatory response of HEp-2 cells to A. baumannii OMVs treated with proteinase K and EDTA. (A) Protein profiles of A. baumannii OMVs. Lane M, size marker; 1, purified intact OMVs; 2, OMVs treated with EDTA; 3, OMVs treated with proteinase K; 4, proteinase K. (B) Expression of pro-inflammatory cytokine genes to proteinase K- and EDTA-treated A. baumannii OMVs was assessed by quantitative real-time PCR. HEp-2 cells were treated with the same concentration (15 µg/ml) of A. baumannii OMVs for 24 h as a positive control. Data are presented as mean ± SD of duplicate determinations.

    Techniques Used: Marker, Purification, Expressing, Real-time Polymerase Chain Reaction, Concentration Assay, Positive Control

    5) Product Images from "Probing the Borrelia burgdorferi Surface Lipoprotein Secretion Pathway Using a Conditionally Folding Protein Domain ▿"

    Article Title: Probing the Borrelia burgdorferi Surface Lipoprotein Secretion Pathway Using a Conditionally Folding Protein Domain ▿

    Journal: Journal of Bacteriology

    doi: 10.1128/JB.06042-11

    Chelation-dependent surface exposure of OspA-CaM fusion proteins at steady state. (A) Accessibility of full-length OspA-CaM or OspA tether-CaM fusion proteins to proteinase K. Cells expressing the fusion constructs were grown in BSK-SFcc containing either
    Figure Legend Snippet: Chelation-dependent surface exposure of OspA-CaM fusion proteins at steady state. (A) Accessibility of full-length OspA-CaM or OspA tether-CaM fusion proteins to proteinase K. Cells expressing the fusion constructs were grown in BSK-SFcc containing either

    Techniques Used: Chick Chorioallantoic Membrane Assay, Expressing, Construct

    6) Product Images from "Simple Silica Column–Based Method to Quantify Inorganic Polyphosphates in Cartilage and Other Tissues"

    Article Title: Simple Silica Column–Based Method to Quantify Inorganic Polyphosphates in Cartilage and Other Tissues

    Journal: Cartilage

    doi: 10.1177/1947603517690856

    Proteinase K pretreatment enhances polyP recovery. Seven nanomoles polyP samples mixed with various concentrations of fetal bovine serum (FBS) were incubated in the presence (+PK) or absence (–PK) of proteinase K (1 mg/mL), alone or together with
    Figure Legend Snippet: Proteinase K pretreatment enhances polyP recovery. Seven nanomoles polyP samples mixed with various concentrations of fetal bovine serum (FBS) were incubated in the presence (+PK) or absence (–PK) of proteinase K (1 mg/mL), alone or together with

    Techniques Used: Incubation

    7) Product Images from "Metallochaperones Are Needed for Mycobacterium tuberculosis and Escherichia coli Nicotinamidase-Pyrazinamidase Activity"

    Article Title: Metallochaperones Are Needed for Mycobacterium tuberculosis and Escherichia coli Nicotinamidase-Pyrazinamidase Activity

    Journal: Journal of Bacteriology

    doi: 10.1128/JB.00331-19

    (A) Reactivation of PZAse-MT–Apo with ZnuA versus degraded ZnuA. (B) Reactivation of PZAse-MT–Apo with Rv2059 versus degraded Rv2059. The colors represent different experimental conditions: red, PZAse-MT; blue, PZAse-MT–Tx; green, PZAse-MT–Apo; orange, ZnuA or Rv2059; magenta, Zn; purple, proteolytically degraded ZnuA or Rv2059; and yellow, ZnuA or Rv2059 and thermally inactivated proteinase K (iPk). The bars represent mean estimated activity, and the whiskers represent 95% confidence intervals.
    Figure Legend Snippet: (A) Reactivation of PZAse-MT–Apo with ZnuA versus degraded ZnuA. (B) Reactivation of PZAse-MT–Apo with Rv2059 versus degraded Rv2059. The colors represent different experimental conditions: red, PZAse-MT; blue, PZAse-MT–Tx; green, PZAse-MT–Apo; orange, ZnuA or Rv2059; magenta, Zn; purple, proteolytically degraded ZnuA or Rv2059; and yellow, ZnuA or Rv2059 and thermally inactivated proteinase K (iPk). The bars represent mean estimated activity, and the whiskers represent 95% confidence intervals.

    Techniques Used: Activity Assay

    8) Product Images from "Engineered Stochastic Adhesion Between Microbes as a Protection Mechanism Against Environmental Stress"

    Article Title: Engineered Stochastic Adhesion Between Microbes as a Protection Mechanism Against Environmental Stress

    Journal: Cellular and Molecular Bioengineering

    doi: 10.1007/s12195-018-0552-9

    Dissociation of bacterial aggregates by proteinase K treatment. (a) The cartoon demonstrates the experimental setup using proteinase K to disperse adhesion-based bacterial aggregates. (b) Comparison of the number of aggregates found in samples expressing eCPX-Dockerin-Ac after treatment with proteinase K to untreated samples. * indicates that differences between samples are significant below a p-value less than 0.05. Significance was determined by a one-tailed t test with an unequal variance that returned a p-value of 0.013. (c) Control sample demonstrating normal aggregate formation by expression of eCPX-Dockerin-Ac. Red circles highlight aggregates. (d) Control sample demonstrating normal planktonic state of BL21DE3 cells. (e) An experimental sample of cells expressing eCPX-Dockerin-Ac treated with 0.1 μ L/mL proteinase K demonstrating dissociation of aggregates found in the untreated sample (b) . (f) Control sample demonstrating the normal planktonic state of BL21DE3 cells treated with 0.1 μ L/mL proteinase K. (c–f) ”).
    Figure Legend Snippet: Dissociation of bacterial aggregates by proteinase K treatment. (a) The cartoon demonstrates the experimental setup using proteinase K to disperse adhesion-based bacterial aggregates. (b) Comparison of the number of aggregates found in samples expressing eCPX-Dockerin-Ac after treatment with proteinase K to untreated samples. * indicates that differences between samples are significant below a p-value less than 0.05. Significance was determined by a one-tailed t test with an unequal variance that returned a p-value of 0.013. (c) Control sample demonstrating normal aggregate formation by expression of eCPX-Dockerin-Ac. Red circles highlight aggregates. (d) Control sample demonstrating normal planktonic state of BL21DE3 cells. (e) An experimental sample of cells expressing eCPX-Dockerin-Ac treated with 0.1 μ L/mL proteinase K demonstrating dissociation of aggregates found in the untreated sample (b) . (f) Control sample demonstrating the normal planktonic state of BL21DE3 cells treated with 0.1 μ L/mL proteinase K. (c–f) ”).

    Techniques Used: Expressing, One-tailed Test

    9) Product Images from "Drug-Free Albumin-Triggered Sensitization of Cancer Cells to Anticancer Drugs"

    Article Title: Drug-Free Albumin-Triggered Sensitization of Cancer Cells to Anticancer Drugs

    Journal: Journal of controlled release : official journal of the Controlled Release Society

    doi: 10.1016/j.jconrel.2018.11.015

    CD20 crosslinking activities and calcium influx induction after Fab'-MORF1 pretargeted Raji cells were treated with (A, B) HSA-mal, (C,D) HSA-MORF2, and (E, F) HSA-(MORF2) x  with high valence. (A, C, E) CD20 highly expressing Raji cells were exposed to Fab'-MORF1-Cy5 (1 μM MORF1, 1 h), and then further treated with (A) HSA-mal-Cy3 (1 μM HSA, 5 h), (C) HSA-(MORF2) 1.4 -Cy3 (1 μM MORF2, 5 h), or (E) HSA-(MORF2) 11.4 -Cy3 (1 μM MORF2, 5 h). Afterward, cell nuclei were stained with Hoechst 33342, and cells were visualized under confocal microscopy. Red: Cy5; Green: Cy3; Blue: nucleus. Meanwhile, surface CD20 receptors of treated cells were enzymatically digested by proteinase K. Flow cytometry was applied to detect the Cy3, Cy5 and their FRET signal before and after CD20 digestion. (B, D, F) Time-dependent change in intracellular Ca 2+  as determined by flow cytometry-based quantification of Fluo-3AM fluorescence intensity. Raji cells, pretreated with Fab'-MORF1 and loaded with Fluo-3AM, were excited at 488 nm and the emission at 530 nm was measured on flow cytometry. A baseline was obtained for 120 s before stimulation with (B) HSA-mal, (D) HSA-(MORF2) 1.2 , (F) HSA-(MORF2) 9.4  crosslinking (indicated by black arrow).To deplete cholesterol and inhibit CD20 crosslinking, cells were pre-incubated 20 min at 37°C in the presence of β-CD (β-cyclodextrin). (G) Apoptosis induction after Raji cells were consecutively treated with Fab'-MORF1 (1 μM MORF1, 1 h) and HSA-(MORF2) x  (1 μM MORF2, 18 h, x=0, 1.2, 5.4, 9.4, 16.6). Then cells were washed with PBS, followed by the AnnexinV-FITC/PI double staining and flow cytometry analysis. Cells that were not treated or treated with RTX (0.5 μM, 1 h)/GAH (0.5 μM, 18 h) were set as controls.
    Figure Legend Snippet: CD20 crosslinking activities and calcium influx induction after Fab'-MORF1 pretargeted Raji cells were treated with (A, B) HSA-mal, (C,D) HSA-MORF2, and (E, F) HSA-(MORF2) x with high valence. (A, C, E) CD20 highly expressing Raji cells were exposed to Fab'-MORF1-Cy5 (1 μM MORF1, 1 h), and then further treated with (A) HSA-mal-Cy3 (1 μM HSA, 5 h), (C) HSA-(MORF2) 1.4 -Cy3 (1 μM MORF2, 5 h), or (E) HSA-(MORF2) 11.4 -Cy3 (1 μM MORF2, 5 h). Afterward, cell nuclei were stained with Hoechst 33342, and cells were visualized under confocal microscopy. Red: Cy5; Green: Cy3; Blue: nucleus. Meanwhile, surface CD20 receptors of treated cells were enzymatically digested by proteinase K. Flow cytometry was applied to detect the Cy3, Cy5 and their FRET signal before and after CD20 digestion. (B, D, F) Time-dependent change in intracellular Ca 2+ as determined by flow cytometry-based quantification of Fluo-3AM fluorescence intensity. Raji cells, pretreated with Fab'-MORF1 and loaded with Fluo-3AM, were excited at 488 nm and the emission at 530 nm was measured on flow cytometry. A baseline was obtained for 120 s before stimulation with (B) HSA-mal, (D) HSA-(MORF2) 1.2 , (F) HSA-(MORF2) 9.4 crosslinking (indicated by black arrow).To deplete cholesterol and inhibit CD20 crosslinking, cells were pre-incubated 20 min at 37°C in the presence of β-CD (β-cyclodextrin). (G) Apoptosis induction after Raji cells were consecutively treated with Fab'-MORF1 (1 μM MORF1, 1 h) and HSA-(MORF2) x (1 μM MORF2, 18 h, x=0, 1.2, 5.4, 9.4, 16.6). Then cells were washed with PBS, followed by the AnnexinV-FITC/PI double staining and flow cytometry analysis. Cells that were not treated or treated with RTX (0.5 μM, 1 h)/GAH (0.5 μM, 18 h) were set as controls.

    Techniques Used: Expressing, Staining, Confocal Microscopy, Flow Cytometry, Cytometry, Fluorescence, Incubation, Double Staining

    10) Product Images from "Characterization of Ethanol Extracted Cell Wall Components of Mycobacterium avium Subsp. paratuberculosis"

    Article Title: Characterization of Ethanol Extracted Cell Wall Components of Mycobacterium avium Subsp. paratuberculosis

    Journal: Veterinary Sciences

    doi: 10.3390/vetsci6040088

    Preparation of EtOH extract for mass spectrometry analysis. ( a ) Map bacilli were washed 6 times prior to EtOH extraction (labeled × 6) to avoid bovine serum albumin (BSA) contamination. A second extract was prepared after washing Map once (label × 1). Lipids and carbohydrate were removed from the EtOH extract through a second chloroform:methanol:water extraction. This second extraction was run on 12% SDS-PAGE denaturing gels and exposed to Coomassie stain (CBB) and silver stain. The location of BSA migration is identified for both gel images. ( b ) Proteinase K treatment of Map EtOH extract. Inclusion of proteinase K or the EtOH extract along with staining method is indicated beneath the gel. Kilodalton size markers are shown in the left margins of all gels.
    Figure Legend Snippet: Preparation of EtOH extract for mass spectrometry analysis. ( a ) Map bacilli were washed 6 times prior to EtOH extraction (labeled × 6) to avoid bovine serum albumin (BSA) contamination. A second extract was prepared after washing Map once (label × 1). Lipids and carbohydrate were removed from the EtOH extract through a second chloroform:methanol:water extraction. This second extraction was run on 12% SDS-PAGE denaturing gels and exposed to Coomassie stain (CBB) and silver stain. The location of BSA migration is identified for both gel images. ( b ) Proteinase K treatment of Map EtOH extract. Inclusion of proteinase K or the EtOH extract along with staining method is indicated beneath the gel. Kilodalton size markers are shown in the left margins of all gels.

    Techniques Used: Mass Spectrometry, Labeling, SDS Page, Staining, Silver Staining, Migration

    Bovine antibody binds to a carbohydrate component of the Map EtOH extract, not to protein. ( a ) Surface antigens of Map K-10 were extracted with 80% ethanol (EtOH Whole) and fractionated by Folch extraction method into organic (chloroform), interface and aqueous fractions. After evaporating methanol for immobilization of the lipids (and other molecules) onto the wells of a microtitre plate, they were incubated with serum samples (1:100 dilution) collected from JD-positive (solid bar) and negative (open bar) cattle. Histogram bars represent mean antibody binding ± standard deviation of quadruplicate determinations. Most of the antigenicity is in the organic fraction. ( b ) EtOH extract treated with proteases shows no negative effects on bovine antibody binding. The extract was treated with either 10 µg/mL trypsin or 10 µg/mL proteinase K with each treatment actually enhancing antibody binding. This enhancement was not statistically significant. However, EtOH extract antigens are efficiently removed by ConA-agarose as shown by lack of antibody binding ( c ). Absorption with agarose only does not affect antibody binding to the EtOH extract. This experiment was repeated in triplicate with qraduplicate measurements for each. p values less than 0.01 are denoted by an asterisk.
    Figure Legend Snippet: Bovine antibody binds to a carbohydrate component of the Map EtOH extract, not to protein. ( a ) Surface antigens of Map K-10 were extracted with 80% ethanol (EtOH Whole) and fractionated by Folch extraction method into organic (chloroform), interface and aqueous fractions. After evaporating methanol for immobilization of the lipids (and other molecules) onto the wells of a microtitre plate, they were incubated with serum samples (1:100 dilution) collected from JD-positive (solid bar) and negative (open bar) cattle. Histogram bars represent mean antibody binding ± standard deviation of quadruplicate determinations. Most of the antigenicity is in the organic fraction. ( b ) EtOH extract treated with proteases shows no negative effects on bovine antibody binding. The extract was treated with either 10 µg/mL trypsin or 10 µg/mL proteinase K with each treatment actually enhancing antibody binding. This enhancement was not statistically significant. However, EtOH extract antigens are efficiently removed by ConA-agarose as shown by lack of antibody binding ( c ). Absorption with agarose only does not affect antibody binding to the EtOH extract. This experiment was repeated in triplicate with qraduplicate measurements for each. p values less than 0.01 are denoted by an asterisk.

    Techniques Used: Incubation, Binding Assay, Standard Deviation

    11) Product Images from "Simple Silica Column–Based Method to Quantify Inorganic Polyphosphates in Cartilage and Other Tissues"

    Article Title: Simple Silica Column–Based Method to Quantify Inorganic Polyphosphates in Cartilage and Other Tissues

    Journal: Cartilage

    doi: 10.1177/1947603517690856

    Proteinase K pretreatment enhances polyP recovery. Seven nanomoles polyP samples mixed with various concentrations of fetal bovine serum (FBS) were incubated in the presence (+PK) or absence (–PK) of proteinase K (1 mg/mL), alone or together with
    Figure Legend Snippet: Proteinase K pretreatment enhances polyP recovery. Seven nanomoles polyP samples mixed with various concentrations of fetal bovine serum (FBS) were incubated in the presence (+PK) or absence (–PK) of proteinase K (1 mg/mL), alone or together with

    Techniques Used: Incubation

    Related Articles

    Amplification:

    Article Title: Cell Lineage Analysis Reveals Three Different Progenitor Pools for Neurosensory Elements in the Otic Vesicle
    Article Snippet: In the double fluorescence in situ hybridization, fluorescein (FLUO)- and digoxigenin-labeled probes were detected with Tyramide Signal Amplification fluorescein and Fast Red, respectively. .. Embryos were permeabilized with 10 μg/ml Proteinase K (Invitrogen) at room temperature for 10–30 min, fixed for 20 min in 4% PFA, and incubated overnight at 4°C with primary antibodies in blocking solution.

    Cytometry:

    Article Title: Drug-Free Albumin-Triggered Sensitization of Cancer Cells to Anticancer Drugs
    Article Snippet: Briefly, cells were washed with cold PBS after the treatments, and then incubated with 0.4 mg/mL proteinase K (Thermo Scientific) for 20 min at 37 °C to degrade surface CD20. .. Then the detached nanoconjugates were removed by washing the cells with cold PBS twice, prior to flow cytometry analysis for intracellular fluorescence of Cy5 and Cy3.

    Blocking Assay:

    Article Title: Cell Lineage Analysis Reveals Three Different Progenitor Pools for Neurosensory Elements in the Otic Vesicle
    Article Snippet: .. Embryos were permeabilized with 10 μg/ml Proteinase K (Invitrogen) at room temperature for 10–30 min, fixed for 20 min in 4% PFA, and incubated overnight at 4°C with primary antibodies in blocking solution. .. Primary antibodies were polyclonal antibody (pAb) anti-neuroD1 , pAb anti-GFP (1:400; Clontech), and pAb anti-DsRed (1:1000; Clontech).

    Enzyme-linked Immunosorbent Assay:

    Article Title: Characterization of Ethanol Extracted Cell Wall Components of Mycobacterium avium Subsp. paratuberculosis
    Article Snippet: Paragraph title: 2.5. ELISA to Measure Antibody Binding ... In the protease experiment, 10 µL of trypsin (Thermofisher, final concentration 200 µg/mL) or proteinase K (ACROS, final concentration 200 µg/mL) was added along with 40 µL of 50 mM Tris buffer (pH 8.0)-20 mM CaCl2 .

    Incubation:

    Article Title: Characterization of Ethanol Extracted Cell Wall Components of Mycobacterium avium Subsp. paratuberculosis
    Article Snippet: In the protease experiment, 10 µL of trypsin (Thermofisher, final concentration 200 µg/mL) or proteinase K (ACROS, final concentration 200 µg/mL) was added along with 40 µL of 50 mM Tris buffer (pH 8.0)-20 mM CaCl2 . .. These protease reactions were incubated at 37 °C for 3 h and then diluted 1:10 with EtOH.

    Article Title: Metallochaperones Are Needed for Mycobacterium tuberculosis and Escherichia coli Nicotinamidase-Pyrazinamidase Activity
    Article Snippet: .. For proteolytic degradation, the proteins were incubated with proteinase K (Ambion) at 65°C for 4 h. Proteinase K was then itself inactivated by incubation at 120°C for 1 h. The proteinase K/metallochaperone molar ratios used were 1:2,000 for ZnuA and 1:25 for Rv2059 for optimal degradation and inactivation. .. Protein degradation was verified by SDS-PAGE and revealed using Coomassie brilliant blue for ZnuA and silver nitrate for Rv2059 due to its lower molecular weight.

    Article Title: Simple Silica Column–Based Method to Quantify Inorganic Polyphosphates in Cartilage and Other Tissues
    Article Snippet: .. To determine if proteinase K is necessary to extract polyP from protein containing tissues/solutions, 7 nmol polyP-45 (50 µM) was mixed with 20% or 50% (v/v) FBS and incubated in the presence or absence of proteinase K (1 mg/mL, Life Technologies, Burlington, Ontario, Canada) in 10 mM Tris, pH 8.0, for 4 hours at 56°C with periodic agitation. .. Silica spin column isolation was performed on proteinase K–treated samples and aliquots of Tris HCl, pH 7.5 solution was added to the eluents (final Tris concentration of 500 mM) before fluorescence was measured.

    Article Title: Cell Lineage Analysis Reveals Three Different Progenitor Pools for Neurosensory Elements in the Otic Vesicle
    Article Snippet: .. Embryos were permeabilized with 10 μg/ml Proteinase K (Invitrogen) at room temperature for 10–30 min, fixed for 20 min in 4% PFA, and incubated overnight at 4°C with primary antibodies in blocking solution. .. Primary antibodies were polyclonal antibody (pAb) anti-neuroD1 , pAb anti-GFP (1:400; Clontech), and pAb anti-DsRed (1:1000; Clontech).

    Article Title: Probing the Borrelia burgdorferi Surface Lipoprotein Secretion Pathway Using a Conditionally Folding Protein Domain ▿
    Article Snippet: To assess the surface exposure of a protein by its accessibility to proteinase K, intact B. burgdorferi cells were harvested, washed, and treated in situ with 200 μg/ml proteinase K (Invitrogen) as described previously ( ). .. Spirochetes were resuspended in phosphate-buffered saline (PBS) containing 5 mM MgCl2 (PBS+Mg), 2% bovine serum albumin (BSA), with or without 0.06% (vol/vol) Triton X-100 , and were incubated with the primary antibodies described above against CaM (dilution, 1:300) or OppAIV (1:100).

    Article Title: Drug-Free Albumin-Triggered Sensitization of Cancer Cells to Anticancer Drugs
    Article Snippet: .. Briefly, cells were washed with cold PBS after the treatments, and then incubated with 0.4 mg/mL proteinase K (Thermo Scientific) for 20 min at 37 °C to degrade surface CD20. .. Afterward, the degradation was stopped by neutralizing the proteinase K with the same volume of 10% FBS containing cell culture medium (FBS stops the enzymatic activity).

    Article Title: Simple Silica Column–Based Method to Quantify Inorganic Polyphosphates in Cartilage and Other Tissues
    Article Snippet: .. To determine if proteinase K is necessary to extract polyP from protein containing tissues/solutions, 7 nmol polyP-45 (50 µM) was mixed with 20% or 50% (v/v) FBS and incubated in the presence or absence of proteinase K (1 mg/mL, Life Technologies, Burlington, Ontario, Canada) in 10 mM Tris, pH 8.0, for 4 hours at 56°C with periodic agitation. .. To determine if proteinase K is necessary to extract polyP from protein containing tissues/solutions, 7 nmol polyP-45 (50 µM) was mixed with 20% or 50% (v/v) FBS and incubated in the presence or absence of proteinase K (1 mg/mL, Life Technologies, Burlington, Ontario, Canada) in 10 mM Tris, pH 8.0, for 4 hours at 56°C with periodic agitation.

    Activity Assay:

    Article Title: Antagonistic Potential of Native Trichoderma viride Strain against Potent Tea Fungal Pathogens in North East India
    Article Snippet: .. Effects of proteinase K and heat on the antifungal activity of cell free culture filtrate To assess the stability of the extracellular metabolites, 20 days old culture filtrates of strain SDRLIN1 were either treated with 0.1 mg/ml proteinase K (Thermo Scientific, Lithuania) at 37°C for 60 min or boiled for 45 min. ..

    Article Title: Drug-Free Albumin-Triggered Sensitization of Cancer Cells to Anticancer Drugs
    Article Snippet: Briefly, cells were washed with cold PBS after the treatments, and then incubated with 0.4 mg/mL proteinase K (Thermo Scientific) for 20 min at 37 °C to degrade surface CD20. .. Afterward, the degradation was stopped by neutralizing the proteinase K with the same volume of 10% FBS containing cell culture medium (FBS stops the enzymatic activity).

    Western Blot:

    Article Title: Curcumin Treatment Improves Motor Behavior in α-Synuclein Transgenic Mice
    Article Snippet: .. Proteinase-K and Western Blot analysis Proteinase-K-resistant aggregates were analyzed by incubating synaptosome and cytosolic brain fractions with 10 μg/mL Proteinase-K (Thermo Scientific) for 30 minutes at 37°C, followed by SDS-PAGE western blot using the Li-cor Odyssey CLx quantitative western blot imaging system. .. Syn-GFP blot signal was detected using a rabbit polyclonal antibody against GFP (Abcam, 1:2000), and data was quantified using LiCor Image Studio software.

    Article Title: Probing the Borrelia burgdorferi Surface Lipoprotein Secretion Pathway Using a Conditionally Folding Protein Domain ▿
    Article Snippet: To assess the surface exposure of a protein by its accessibility to proteinase K, intact B. burgdorferi cells were harvested, washed, and treated in situ with 200 μg/ml proteinase K (Invitrogen) as described previously ( ). .. Whole-cell protein preparations were analyzed by SDS-PAGE and Western immunoblotting.

    Flow Cytometry:

    Article Title: Drug-Free Albumin-Triggered Sensitization of Cancer Cells to Anticancer Drugs
    Article Snippet: Briefly, cells were washed with cold PBS after the treatments, and then incubated with 0.4 mg/mL proteinase K (Thermo Scientific) for 20 min at 37 °C to degrade surface CD20. .. Then the detached nanoconjugates were removed by washing the cells with cold PBS twice, prior to flow cytometry analysis for intracellular fluorescence of Cy5 and Cy3.

    Immunolabeling:

    Article Title: Cell Lineage Analysis Reveals Three Different Progenitor Pools for Neurosensory Elements in the Otic Vesicle
    Article Snippet: Paragraph title: In situ hybridization and immunolabeling ... Embryos were permeabilized with 10 μg/ml Proteinase K (Invitrogen) at room temperature for 10–30 min, fixed for 20 min in 4% PFA, and incubated overnight at 4°C with primary antibodies in blocking solution.

    Cell Culture:

    Article Title: Drug-Free Albumin-Triggered Sensitization of Cancer Cells to Anticancer Drugs
    Article Snippet: Briefly, cells were washed with cold PBS after the treatments, and then incubated with 0.4 mg/mL proteinase K (Thermo Scientific) for 20 min at 37 °C to degrade surface CD20. .. Afterward, the degradation was stopped by neutralizing the proteinase K with the same volume of 10% FBS containing cell culture medium (FBS stops the enzymatic activity).

    In Situ Hybridization:

    Article Title: Cell Lineage Analysis Reveals Three Different Progenitor Pools for Neurosensory Elements in the Otic Vesicle
    Article Snippet: Paragraph title: In situ hybridization and immunolabeling ... Embryos were permeabilized with 10 μg/ml Proteinase K (Invitrogen) at room temperature for 10–30 min, fixed for 20 min in 4% PFA, and incubated overnight at 4°C with primary antibodies in blocking solution.

    Imaging:

    Article Title: Curcumin Treatment Improves Motor Behavior in α-Synuclein Transgenic Mice
    Article Snippet: .. Proteinase-K and Western Blot analysis Proteinase-K-resistant aggregates were analyzed by incubating synaptosome and cytosolic brain fractions with 10 μg/mL Proteinase-K (Thermo Scientific) for 30 minutes at 37°C, followed by SDS-PAGE western blot using the Li-cor Odyssey CLx quantitative western blot imaging system. .. Syn-GFP blot signal was detected using a rabbit polyclonal antibody against GFP (Abcam, 1:2000), and data was quantified using LiCor Image Studio software.

    Binding Assay:

    Article Title: Characterization of Ethanol Extracted Cell Wall Components of Mycobacterium avium Subsp. paratuberculosis
    Article Snippet: Paragraph title: 2.5. ELISA to Measure Antibody Binding ... In the protease experiment, 10 µL of trypsin (Thermofisher, final concentration 200 µg/mL) or proteinase K (ACROS, final concentration 200 µg/mL) was added along with 40 µL of 50 mM Tris buffer (pH 8.0)-20 mM CaCl2 .

    Article Title: Drug-Free Albumin-Triggered Sensitization of Cancer Cells to Anticancer Drugs
    Article Snippet: After Raji cells were given the consecutive treatments as described above, the surface CD20-bound Fab'-MORF1-Cy5 were enzymatically digested , according to a previously published protocol [ ], to remove the extracellular binding nanoconjugates and analyze the intracellular internalization. .. Briefly, cells were washed with cold PBS after the treatments, and then incubated with 0.4 mg/mL proteinase K (Thermo Scientific) for 20 min at 37 °C to degrade surface CD20.

    Immunofluorescence:

    Article Title: Probing the Borrelia burgdorferi Surface Lipoprotein Secretion Pathway Using a Conditionally Folding Protein Domain ▿
    Article Snippet: To assess the surface exposure of a protein by its accessibility to proteinase K, intact B. burgdorferi cells were harvested, washed, and treated in situ with 200 μg/ml proteinase K (Invitrogen) as described previously ( ). .. Accessibility to antibodies was assessed by indirect fluorescent antibody assay (IFA) microscopy as described previously ( ).

    Molecular Weight:

    Article Title: Metallochaperones Are Needed for Mycobacterium tuberculosis and Escherichia coli Nicotinamidase-Pyrazinamidase Activity
    Article Snippet: For proteolytic degradation, the proteins were incubated with proteinase K (Ambion) at 65°C for 4 h. Proteinase K was then itself inactivated by incubation at 120°C for 1 h. The proteinase K/metallochaperone molar ratios used were 1:2,000 for ZnuA and 1:25 for Rv2059 for optimal degradation and inactivation. .. Protein degradation was verified by SDS-PAGE and revealed using Coomassie brilliant blue for ZnuA and silver nitrate for Rv2059 due to its lower molecular weight.

    Nucleic Acid Electrophoresis:

    Article Title: Acinetobacter baumannii Outer Membrane Vesicles Elicit a Potent Innate Immune Response via Membrane Proteins
    Article Snippet: Treatment of OMVs with Proteinase K and Ethylenediaminetetraacetic Acid (EDTA) Purified OMVs were treated with 0.1 µg/ml of proteinase K (Fermentas) for 1 h at 37°C for degradation of surface-exposed proteins in the OMVs and 0.1 M EDTA for 1 h at 37°C for disintegration of OMV membrane. .. OMV samples, including intact OMVs and proteinase K- and EDTA-treated OMVs, were separated by 12% sodium dodecyl sulfate-polyacrylamide gel electrophoresis and stained with Coomassie brilliant blue R-250 (Bio-Rad).

    Fluorescence:

    Article Title: Simple Silica Column–Based Method to Quantify Inorganic Polyphosphates in Cartilage and Other Tissues
    Article Snippet: To determine if proteinase K is necessary to extract polyP from protein containing tissues/solutions, 7 nmol polyP-45 (50 µM) was mixed with 20% or 50% (v/v) FBS and incubated in the presence or absence of proteinase K (1 mg/mL, Life Technologies, Burlington, Ontario, Canada) in 10 mM Tris, pH 8.0, for 4 hours at 56°C with periodic agitation. .. The recovery ratio was calculated by dividing the DAPI fluorescence of eluted samples by the non–enzyme-treated control (50 µM polyP-45 in 10 mM Tris-EDTA, pH 8.0).

    Article Title: Cell Lineage Analysis Reveals Three Different Progenitor Pools for Neurosensory Elements in the Otic Vesicle
    Article Snippet: In the double fluorescence in situ hybridization, fluorescein (FLUO)- and digoxigenin-labeled probes were detected with Tyramide Signal Amplification fluorescein and Fast Red, respectively. .. Embryos were permeabilized with 10 μg/ml Proteinase K (Invitrogen) at room temperature for 10–30 min, fixed for 20 min in 4% PFA, and incubated overnight at 4°C with primary antibodies in blocking solution.

    Article Title: Drug-Free Albumin-Triggered Sensitization of Cancer Cells to Anticancer Drugs
    Article Snippet: Briefly, cells were washed with cold PBS after the treatments, and then incubated with 0.4 mg/mL proteinase K (Thermo Scientific) for 20 min at 37 °C to degrade surface CD20. .. Then the detached nanoconjugates were removed by washing the cells with cold PBS twice, prior to flow cytometry analysis for intracellular fluorescence of Cy5 and Cy3.

    Article Title: Simple Silica Column–Based Method to Quantify Inorganic Polyphosphates in Cartilage and Other Tissues
    Article Snippet: To determine if proteinase K is necessary to extract polyP from protein containing tissues/solutions, 7 nmol polyP-45 (50 µM) was mixed with 20% or 50% (v/v) FBS and incubated in the presence or absence of proteinase K (1 mg/mL, Life Technologies, Burlington, Ontario, Canada) in 10 mM Tris, pH 8.0, for 4 hours at 56°C with periodic agitation. .. Silica spin column isolation was performed on proteinase K–treated samples and aliquots of Tris HCl, pH 7.5 solution was added to the eluents (final Tris concentration of 500 mM) before fluorescence was measured.

    Isolation:

    Article Title: Simple Silica Column–Based Method to Quantify Inorganic Polyphosphates in Cartilage and Other Tissues
    Article Snippet: To determine if proteinase K is necessary to extract polyP from protein containing tissues/solutions, 7 nmol polyP-45 (50 µM) was mixed with 20% or 50% (v/v) FBS and incubated in the presence or absence of proteinase K (1 mg/mL, Life Technologies, Burlington, Ontario, Canada) in 10 mM Tris, pH 8.0, for 4 hours at 56°C with periodic agitation. .. The recovery ratio was calculated by dividing the DAPI fluorescence of eluted samples by the non–enzyme-treated control (50 µM polyP-45 in 10 mM Tris-EDTA, pH 8.0).

    Article Title: Simple Silica Column–Based Method to Quantify Inorganic Polyphosphates in Cartilage and Other Tissues
    Article Snippet: To determine if proteinase K is necessary to extract polyP from protein containing tissues/solutions, 7 nmol polyP-45 (50 µM) was mixed with 20% or 50% (v/v) FBS and incubated in the presence or absence of proteinase K (1 mg/mL, Life Technologies, Burlington, Ontario, Canada) in 10 mM Tris, pH 8.0, for 4 hours at 56°C with periodic agitation. .. Silica spin column isolation was performed on proteinase K–treated samples and aliquots of Tris HCl, pH 7.5 solution was added to the eluents (final Tris concentration of 500 mM) before fluorescence was measured.

    Microscopy:

    Article Title: Cell Lineage Analysis Reveals Three Different Progenitor Pools for Neurosensory Elements in the Otic Vesicle
    Article Snippet: Embryos were permeabilized with 10 μg/ml Proteinase K (Invitrogen) at room temperature for 10–30 min, fixed for 20 min in 4% PFA, and incubated overnight at 4°C with primary antibodies in blocking solution. .. For anti-neuroD1, immunolabeling was done on sections, and antigen retrieval was performed by boiling the sections in 10 m m citric acid at 95°C for 1 h. After extensive washings with PBST, embryos were incubated with secondary antibodies conjugated with Alexa Fluor 488 (green) or Alexa Fluor 549 (red) (1:400; Invitrogen) in blocking solution at room temperature for 3 h. After PBS washings, whole-mount embryos and sections were imaged under a fluorescence microscope (Leica DM6000B).

    Article Title: Probing the Borrelia burgdorferi Surface Lipoprotein Secretion Pathway Using a Conditionally Folding Protein Domain ▿
    Article Snippet: To assess the surface exposure of a protein by its accessibility to proteinase K, intact B. burgdorferi cells were harvested, washed, and treated in situ with 200 μg/ml proteinase K (Invitrogen) as described previously ( ). .. Accessibility to antibodies was assessed by indirect fluorescent antibody assay (IFA) microscopy as described previously ( ).

    Purification:

    Article Title: Acinetobacter baumannii Outer Membrane Vesicles Elicit a Potent Innate Immune Response via Membrane Proteins
    Article Snippet: .. Treatment of OMVs with Proteinase K and Ethylenediaminetetraacetic Acid (EDTA) Purified OMVs were treated with 0.1 µg/ml of proteinase K (Fermentas) for 1 h at 37°C for degradation of surface-exposed proteins in the OMVs and 0.1 M EDTA for 1 h at 37°C for disintegration of OMV membrane. .. OMV samples, including intact OMVs and proteinase K- and EDTA-treated OMVs, were separated by 12% sodium dodecyl sulfate-polyacrylamide gel electrophoresis and stained with Coomassie brilliant blue R-250 (Bio-Rad).

    Labeling:

    Article Title: Cell Lineage Analysis Reveals Three Different Progenitor Pools for Neurosensory Elements in the Otic Vesicle
    Article Snippet: In the case of chromogenic in situ hybridization, labeled probes were detected with Fast Red and NBT/BCIP substrate. .. Embryos were permeabilized with 10 μg/ml Proteinase K (Invitrogen) at room temperature for 10–30 min, fixed for 20 min in 4% PFA, and incubated overnight at 4°C with primary antibodies in blocking solution.

    Chromogenic In Situ Hybridization:

    Article Title: Cell Lineage Analysis Reveals Three Different Progenitor Pools for Neurosensory Elements in the Otic Vesicle
    Article Snippet: In the case of chromogenic in situ hybridization, labeled probes were detected with Fast Red and NBT/BCIP substrate. .. Embryos were permeabilized with 10 μg/ml Proteinase K (Invitrogen) at room temperature for 10–30 min, fixed for 20 min in 4% PFA, and incubated overnight at 4°C with primary antibodies in blocking solution.

    SDS Page:

    Article Title: Metallochaperones Are Needed for Mycobacterium tuberculosis and Escherichia coli Nicotinamidase-Pyrazinamidase Activity
    Article Snippet: For proteolytic degradation, the proteins were incubated with proteinase K (Ambion) at 65°C for 4 h. Proteinase K was then itself inactivated by incubation at 120°C for 1 h. The proteinase K/metallochaperone molar ratios used were 1:2,000 for ZnuA and 1:25 for Rv2059 for optimal degradation and inactivation. .. Protein degradation was verified by SDS-PAGE and revealed using Coomassie brilliant blue for ZnuA and silver nitrate for Rv2059 due to its lower molecular weight.

    Article Title: Curcumin Treatment Improves Motor Behavior in α-Synuclein Transgenic Mice
    Article Snippet: .. Proteinase-K and Western Blot analysis Proteinase-K-resistant aggregates were analyzed by incubating synaptosome and cytosolic brain fractions with 10 μg/mL Proteinase-K (Thermo Scientific) for 30 minutes at 37°C, followed by SDS-PAGE western blot using the Li-cor Odyssey CLx quantitative western blot imaging system. .. Syn-GFP blot signal was detected using a rabbit polyclonal antibody against GFP (Abcam, 1:2000), and data was quantified using LiCor Image Studio software.

    Article Title: Probing the Borrelia burgdorferi Surface Lipoprotein Secretion Pathway Using a Conditionally Folding Protein Domain ▿
    Article Snippet: To assess the surface exposure of a protein by its accessibility to proteinase K, intact B. burgdorferi cells were harvested, washed, and treated in situ with 200 μg/ml proteinase K (Invitrogen) as described previously ( ). .. Whole-cell protein preparations were analyzed by SDS-PAGE and Western immunoblotting.

    Plasmid Preparation:

    Article Title: Characterization of Ethanol Extracted Cell Wall Components of Mycobacterium avium Subsp. paratuberculosis
    Article Snippet: In the protease experiment, 10 µL of trypsin (Thermofisher, final concentration 200 µg/mL) or proteinase K (ACROS, final concentration 200 µg/mL) was added along with 40 µL of 50 mM Tris buffer (pH 8.0)-20 mM CaCl2 . .. In the protease experiment, 10 µL of trypsin (Thermofisher, final concentration 200 µg/mL) or proteinase K (ACROS, final concentration 200 µg/mL) was added along with 40 µL of 50 mM Tris buffer (pH 8.0)-20 mM CaCl2 .

    Software:

    Article Title: Curcumin Treatment Improves Motor Behavior in α-Synuclein Transgenic Mice
    Article Snippet: Proteinase-K and Western Blot analysis Proteinase-K-resistant aggregates were analyzed by incubating synaptosome and cytosolic brain fractions with 10 μg/mL Proteinase-K (Thermo Scientific) for 30 minutes at 37°C, followed by SDS-PAGE western blot using the Li-cor Odyssey CLx quantitative western blot imaging system. .. Syn-GFP blot signal was detected using a rabbit polyclonal antibody against GFP (Abcam, 1:2000), and data was quantified using LiCor Image Studio software.

    In Situ:

    Article Title: Probing the Borrelia burgdorferi Surface Lipoprotein Secretion Pathway Using a Conditionally Folding Protein Domain ▿
    Article Snippet: .. To assess the surface exposure of a protein by its accessibility to proteinase K, intact B. burgdorferi cells were harvested, washed, and treated in situ with 200 μg/ml proteinase K (Invitrogen) as described previously ( ). .. Whole-cell protein preparations were analyzed by SDS-PAGE and Western immunoblotting.

    Concentration Assay:

    Article Title: Characterization of Ethanol Extracted Cell Wall Components of Mycobacterium avium Subsp. paratuberculosis
    Article Snippet: .. In the protease experiment, 10 µL of trypsin (Thermofisher, final concentration 200 µg/mL) or proteinase K (ACROS, final concentration 200 µg/mL) was added along with 40 µL of 50 mM Tris buffer (pH 8.0)-20 mM CaCl2 . .. These protease reactions were incubated at 37 °C for 3 h and then diluted 1:10 with EtOH.

    Article Title: Simple Silica Column–Based Method to Quantify Inorganic Polyphosphates in Cartilage and Other Tissues
    Article Snippet: To determine if proteinase K is necessary to extract polyP from protein containing tissues/solutions, 7 nmol polyP-45 (50 µM) was mixed with 20% or 50% (v/v) FBS and incubated in the presence or absence of proteinase K (1 mg/mL, Life Technologies, Burlington, Ontario, Canada) in 10 mM Tris, pH 8.0, for 4 hours at 56°C with periodic agitation. .. The recovery ratio was calculated by dividing the DAPI fluorescence of eluted samples by the non–enzyme-treated control (50 µM polyP-45 in 10 mM Tris-EDTA, pH 8.0).

    Article Title: Simple Silica Column–Based Method to Quantify Inorganic Polyphosphates in Cartilage and Other Tissues
    Article Snippet: To determine if proteinase K is necessary to extract polyP from protein containing tissues/solutions, 7 nmol polyP-45 (50 µM) was mixed with 20% or 50% (v/v) FBS and incubated in the presence or absence of proteinase K (1 mg/mL, Life Technologies, Burlington, Ontario, Canada) in 10 mM Tris, pH 8.0, for 4 hours at 56°C with periodic agitation. .. Silica spin column isolation was performed on proteinase K–treated samples and aliquots of Tris HCl, pH 7.5 solution was added to the eluents (final Tris concentration of 500 mM) before fluorescence was measured.

    Staining:

    Article Title: Acinetobacter baumannii Outer Membrane Vesicles Elicit a Potent Innate Immune Response via Membrane Proteins
    Article Snippet: Treatment of OMVs with Proteinase K and Ethylenediaminetetraacetic Acid (EDTA) Purified OMVs were treated with 0.1 µg/ml of proteinase K (Fermentas) for 1 h at 37°C for degradation of surface-exposed proteins in the OMVs and 0.1 M EDTA for 1 h at 37°C for disintegration of OMV membrane. .. OMV samples, including intact OMVs and proteinase K- and EDTA-treated OMVs, were separated by 12% sodium dodecyl sulfate-polyacrylamide gel electrophoresis and stained with Coomassie brilliant blue R-250 (Bio-Rad).

    Chick Chorioallantoic Membrane Assay:

    Article Title: Probing the Borrelia burgdorferi Surface Lipoprotein Secretion Pathway Using a Conditionally Folding Protein Domain ▿
    Article Snippet: To assess the surface exposure of a protein by its accessibility to proteinase K, intact B. burgdorferi cells were harvested, washed, and treated in situ with 200 μg/ml proteinase K (Invitrogen) as described previously ( ). .. Spirochetes were resuspended in phosphate-buffered saline (PBS) containing 5 mM MgCl2 (PBS+Mg), 2% bovine serum albumin (BSA), with or without 0.06% (vol/vol) Triton X-100 , and were incubated with the primary antibodies described above against CaM (dilution, 1:300) or OppAIV (1:100).

    Hood:

    Article Title: Characterization of Ethanol Extracted Cell Wall Components of Mycobacterium avium Subsp. paratuberculosis
    Article Snippet: ELISA to Measure Antibody Binding The Map ethanol extract (4 mg) was dried under a fume hood at room temperature overnight. .. In the protease experiment, 10 µL of trypsin (Thermofisher, final concentration 200 µg/mL) or proteinase K (ACROS, final concentration 200 µg/mL) was added along with 40 µL of 50 mM Tris buffer (pH 8.0)-20 mM CaCl2 .

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 99
    Thermo Fisher proteinase k
    Schematic diagram of specimen expansion and microtubule cytoskeleton of Giardia lamblia . Structures containing microtubules are displayed in green and disc-associated proteins (DAPs) are displayed in magenta. (a) Fixed Giardia specimens were immunostained, treated with a linker group, embedded in a swellable acrylamide/acrylate polymer, and digested with <t>Proteinase</t> K (inset below). (b) Dialysis in water expanded the specimen by 3.5×. Key landmarks are also shown in b , including structures of the adhesive disc (microtubules, DAP86676, overlap zone (OZ), and ventral groove (VG)), the eight flagella of Giardia (axonemal microtubules, anterior flagella (AF), and DAP16263 associated with the two ventral flagella (VF)), and the ~10 µm × 15 µm cell body (dashed line). (c,d) Dorsal and ventral layers of adhesive disc microtubules in the overlap zone with plus and minus ends of microtubules as indicated. DAP16263 is shown in its assigned location from this work in c . (e) Transverse view of adhesive disc microtubules and their associated microribbons containing DAP86676. (f) Transverse view of ventral flagella with canonical “9 + 2” microtubule axoneme geometry, and localization of DAP16263 to the paraflagellar rod as determined in this work. The long fin of the ventral flagellum, opposite to the paraflagellar rod, is truncated as shown.
    Proteinase K, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 296 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/proteinase k/product/Thermo Fisher
    Average 99 stars, based on 296 article reviews
    Price from $9.99 to $1999.99
    proteinase k - by Bioz Stars, 2020-04
    99/100 stars
      Buy from Supplier

    Image Search Results


    Schematic diagram of specimen expansion and microtubule cytoskeleton of Giardia lamblia . Structures containing microtubules are displayed in green and disc-associated proteins (DAPs) are displayed in magenta. (a) Fixed Giardia specimens were immunostained, treated with a linker group, embedded in a swellable acrylamide/acrylate polymer, and digested with Proteinase K (inset below). (b) Dialysis in water expanded the specimen by 3.5×. Key landmarks are also shown in b , including structures of the adhesive disc (microtubules, DAP86676, overlap zone (OZ), and ventral groove (VG)), the eight flagella of Giardia (axonemal microtubules, anterior flagella (AF), and DAP16263 associated with the two ventral flagella (VF)), and the ~10 µm × 15 µm cell body (dashed line). (c,d) Dorsal and ventral layers of adhesive disc microtubules in the overlap zone with plus and minus ends of microtubules as indicated. DAP16263 is shown in its assigned location from this work in c . (e) Transverse view of adhesive disc microtubules and their associated microribbons containing DAP86676. (f) Transverse view of ventral flagella with canonical “9 + 2” microtubule axoneme geometry, and localization of DAP16263 to the paraflagellar rod as determined in this work. The long fin of the ventral flagellum, opposite to the paraflagellar rod, is truncated as shown.

    Journal: ACS nano

    Article Title: Hybrid Structured Illumination Expansion Microscopy Reveals Microbial Cytoskeleton Organization

    doi: 10.1021/acsnano.7b07200

    Figure Lengend Snippet: Schematic diagram of specimen expansion and microtubule cytoskeleton of Giardia lamblia . Structures containing microtubules are displayed in green and disc-associated proteins (DAPs) are displayed in magenta. (a) Fixed Giardia specimens were immunostained, treated with a linker group, embedded in a swellable acrylamide/acrylate polymer, and digested with Proteinase K (inset below). (b) Dialysis in water expanded the specimen by 3.5×. Key landmarks are also shown in b , including structures of the adhesive disc (microtubules, DAP86676, overlap zone (OZ), and ventral groove (VG)), the eight flagella of Giardia (axonemal microtubules, anterior flagella (AF), and DAP16263 associated with the two ventral flagella (VF)), and the ~10 µm × 15 µm cell body (dashed line). (c,d) Dorsal and ventral layers of adhesive disc microtubules in the overlap zone with plus and minus ends of microtubules as indicated. DAP16263 is shown in its assigned location from this work in c . (e) Transverse view of adhesive disc microtubules and their associated microribbons containing DAP86676. (f) Transverse view of ventral flagella with canonical “9 + 2” microtubule axoneme geometry, and localization of DAP16263 to the paraflagellar rod as determined in this work. The long fin of the ventral flagellum, opposite to the paraflagellar rod, is truncated as shown.

    Article Snippet: PBS and TAE (Tris Acetate EDTA) 10×stock solutions, and Proteinase K ( > 600 U/mL, EO0491) were obtained from Thermo Fisher.

    Techniques: