proteinase k solution  (Millipore)

 
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    Name:
    Proteinase K from Tritirachium album
    Description:

    Catalog Number:
    p5568
    Price:
    None
    Applications:
    Product has been used to break down cardiac muscle during histopathology studies. It has also been used during the digestion of HEK-293 cells.
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    Structured Review

    Millipore proteinase k solution
    Kinetic Analysis of αS Oligomerization (A) Scheme for the minimalistic kinetic model used to fit the early stages of αS aggregation. (B) Results of the global fitting (continuous lines) of the kinetics of formation of the two types of oligomeric species estimated under bulk conditions from smFRET experiments. Data for type A oligomers and type B oligomers are shown as orange circles and blue squares, respectively (average and standard error of five different experiments). The vertical dashed line is at 30 hr, corresponding to the lag phase of fibril formation estimated under bulk conditions, up to which time our model accounts well for the different microscopic processes governing the aggregation reaction. (C) Cartoon showing the conversion of an 8-mer of αS from a collapsed to an ordered <t>proteinase-K-resistant</t> form. Residues of each monomer are colored according to their location in the amino acid sequence. The average distance between fluorophores, represented as green and red spheres, is different for each type of oligomer and hence gives rise to different average FRET efficiencies.

    https://www.bioz.com/result/proteinase k solution/product/Millipore
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    proteinase k solution - by Bioz Stars, 2021-03
    99/100 stars

    Images

    1) Product Images from "Direct Observation of the Interconversion of Normal and Toxic Forms of ?-Synuclein"

    Article Title: Direct Observation of the Interconversion of Normal and Toxic Forms of ?-Synuclein

    Journal: Cell

    doi: 10.1016/j.cell.2012.03.037

    Kinetic Analysis of αS Oligomerization (A) Scheme for the minimalistic kinetic model used to fit the early stages of αS aggregation. (B) Results of the global fitting (continuous lines) of the kinetics of formation of the two types of oligomeric species estimated under bulk conditions from smFRET experiments. Data for type A oligomers and type B oligomers are shown as orange circles and blue squares, respectively (average and standard error of five different experiments). The vertical dashed line is at 30 hr, corresponding to the lag phase of fibril formation estimated under bulk conditions, up to which time our model accounts well for the different microscopic processes governing the aggregation reaction. (C) Cartoon showing the conversion of an 8-mer of αS from a collapsed to an ordered proteinase-K-resistant form. Residues of each monomer are colored according to their location in the amino acid sequence. The average distance between fluorophores, represented as green and red spheres, is different for each type of oligomer and hence gives rise to different average FRET efficiencies.
    Figure Legend Snippet: Kinetic Analysis of αS Oligomerization (A) Scheme for the minimalistic kinetic model used to fit the early stages of αS aggregation. (B) Results of the global fitting (continuous lines) of the kinetics of formation of the two types of oligomeric species estimated under bulk conditions from smFRET experiments. Data for type A oligomers and type B oligomers are shown as orange circles and blue squares, respectively (average and standard error of five different experiments). The vertical dashed line is at 30 hr, corresponding to the lag phase of fibril formation estimated under bulk conditions, up to which time our model accounts well for the different microscopic processes governing the aggregation reaction. (C) Cartoon showing the conversion of an 8-mer of αS from a collapsed to an ordered proteinase-K-resistant form. Residues of each monomer are colored according to their location in the amino acid sequence. The average distance between fluorophores, represented as green and red spheres, is different for each type of oligomer and hence gives rise to different average FRET efficiencies.

    Techniques Used: Sequencing

    Characterization of the Different Oligomeric Species Formed during αS Aggregation and Fibril Formation (A) The time dependence of the mass fraction of the four oligomeric distributions A small (red squares), A medium (orange circles), B medium (green triangles), and B large (blue triangles). The data shown correspond to the average and standard error of five different experiments. (B) Proteinase K degradation curves of the different protein species (monomer in red, type A oligomer in orange, type B oligomer in blue, and fibrils in black). The data shown here correspond to the average and standard error of three different experiments. See also Figure S3 .
    Figure Legend Snippet: Characterization of the Different Oligomeric Species Formed during αS Aggregation and Fibril Formation (A) The time dependence of the mass fraction of the four oligomeric distributions A small (red squares), A medium (orange circles), B medium (green triangles), and B large (blue triangles). The data shown correspond to the average and standard error of five different experiments. (B) Proteinase K degradation curves of the different protein species (monomer in red, type A oligomer in orange, type B oligomer in blue, and fibrils in black). The data shown here correspond to the average and standard error of three different experiments. See also Figure S3 .

    Techniques Used:

    Analysis of the Stability of the Different Protein Species against Proteinase K Degradation, Related to Figure 3 (A) Incubations of an aliquot of an aggregation sample at late incubation times (around 100 h) with different concentrations of proteinase K were analyzed by single-molecule fluorescence to determine the stability of the different oligomeric species against proteinase K degradation. The pair of A small and A med distributions shows similar dependence on proteinase K concentration, as well as for the pair of B med and B large distributions, although this latter pair has much higher resistance to proteinase K. (B) The stability to proteinase K degradation of monomeric and fibrillar forms of αS was estimated from the disappearance of the band corresponding to full-length monomeric in a SDS-PAGE gel. Different concentrations of proteinase K were used as indicated in the figure. All samples from monomeric, fibrillar and oligomeric forms of αS were treated exactly in the same way for direct comparison.
    Figure Legend Snippet: Analysis of the Stability of the Different Protein Species against Proteinase K Degradation, Related to Figure 3 (A) Incubations of an aliquot of an aggregation sample at late incubation times (around 100 h) with different concentrations of proteinase K were analyzed by single-molecule fluorescence to determine the stability of the different oligomeric species against proteinase K degradation. The pair of A small and A med distributions shows similar dependence on proteinase K concentration, as well as for the pair of B med and B large distributions, although this latter pair has much higher resistance to proteinase K. (B) The stability to proteinase K degradation of monomeric and fibrillar forms of αS was estimated from the disappearance of the band corresponding to full-length monomeric in a SDS-PAGE gel. Different concentrations of proteinase K were used as indicated in the figure. All samples from monomeric, fibrillar and oligomeric forms of αS were treated exactly in the same way for direct comparison.

    Techniques Used: Incubation, Fluorescence, Concentration Assay, SDS Page

    2) Product Images from "The L444P Gba1 mutation enhances alpha-synuclein induced loss of nigral dopaminergic neurons in mice"

    Article Title: The L444P Gba1 mutation enhances alpha-synuclein induced loss of nigral dopaminergic neurons in mice

    Journal: Brain

    doi: 10.1093/brain/awx221

    Alpha-synuclein immunohistochemistry after proteinase K treatment in L444P/+ and KO/+ mouse brains. ( A – C ) Accumulation of small alpha-synuclein proteinase K-resistant aggregates in the polymorph layer of the hippocampal dendate gyrus ( A ), stratum lucidum of the hippocampal cornu ammonis 3 (CA3) region ( B ) and striatum ( C ) of KO/+ mice, but not L444P/+ mice compared to their corresponding wild-type ( +/+ ) control littermates. ( D – E ) No proteinase K-resistant alpha-synuclein aggregates were found in the substantia nigra ( D ) and parvocellular reticular nucleus of the brainstem ( E ) of KO/+ and L444P/+ mice compared to their corresponding wild-type control littermates. Scale bars = 100 μm. Representative images are shown. Three mice of each genotype were analysed.
    Figure Legend Snippet: Alpha-synuclein immunohistochemistry after proteinase K treatment in L444P/+ and KO/+ mouse brains. ( A – C ) Accumulation of small alpha-synuclein proteinase K-resistant aggregates in the polymorph layer of the hippocampal dendate gyrus ( A ), stratum lucidum of the hippocampal cornu ammonis 3 (CA3) region ( B ) and striatum ( C ) of KO/+ mice, but not L444P/+ mice compared to their corresponding wild-type ( +/+ ) control littermates. ( D – E ) No proteinase K-resistant alpha-synuclein aggregates were found in the substantia nigra ( D ) and parvocellular reticular nucleus of the brainstem ( E ) of KO/+ and L444P/+ mice compared to their corresponding wild-type control littermates. Scale bars = 100 μm. Representative images are shown. Three mice of each genotype were analysed.

    Techniques Used: Immunohistochemistry, Mouse Assay

    Related Articles

    Western Blot:

    Article Title: MlaFEDB displays flippase activity to promote phospholipid transport towards the outer membrane of Gram-negative bacteria
    Article Snippet: For detection of NBD-lipid fluorescence Silica TLC plates were left unstained and visualised using an Amersham Imager 680 blot and gel imager (GE Healthcare). .. Western blottingIn order to determine the orientation of MlaFEDB once reconstituted into polar lipid liposomes, MlaFEDB:NBD-PE was subjected to Proteinase K digestion. .. 1 mg of MlaFEDB:NBD-PE was incubated with 0.05 mg/ml Proteinase K (Thermo Fisher) for 10 mins at 4 °C.

    Concentration Assay:

    Article Title: Direct Observation of the Interconversion of Normal and Toxic Forms of ?-Synuclein
    Article Snippet: .. To determine the sensitivity of monomers to proteinase K degradation, we used an equimolecular concentration of AF488- and AF647-labeled A90C αS of 70 μM in Tris 25 mM pH 7.4, 0.1 M NaCl; 2 μl of sample were diluted into 500 μl of buffer and 1 μl of proteinase K solution (Proteinase K from Tritirachium album , Sigma-Aldrich ) was added to a final concentration of 0.01, 0.1, 0.4, 2, and 10 μg/ml (i.e., at protein:proteinase K ratios varying from 1:0.0025 to 1:2.5). .. The reaction sample was then incubated for 20 min at 37°C and the reactions stopped by addition of SDS-PAGE loading buffer and loaded in SDS-PAGE gels.

    Electrophoresis:

    Article Title: A Novel, Reliable and Highly Versatile Method to Evaluate Different Prion Decontamination Procedures
    Article Snippet: To investigate whether addition of detergents could improve the efficiency of prion inactivation, prion-coated Teflon® beads were treated for 1 h with bleach or NaOH solutions, both containing 1% Triton-X-100 (Sigma-Aldrich) and subjected to mild shaking. .. Under the same PMSA conditions (see below), using 1 and 2 beads with reaction times of 1, 2, and 4 h and their respective positive and negative controls, the presence or absence of rec-PrPres propagation was evaluated by proteinase K digestion, electrophoresis and total protein staining. .. Preparation and Purification of Recombinant PrP for the PMSA Substrate The bacterial expression of bank vole I109 recombinant prion protein (rec-VoPrP) was achieved using a pOPIN E expression vector prepared using standard molecular biology procedures, as described previously ( ; ; ).

    Staining:

    Article Title: A Novel, Reliable and Highly Versatile Method to Evaluate Different Prion Decontamination Procedures
    Article Snippet: To investigate whether addition of detergents could improve the efficiency of prion inactivation, prion-coated Teflon® beads were treated for 1 h with bleach or NaOH solutions, both containing 1% Triton-X-100 (Sigma-Aldrich) and subjected to mild shaking. .. Under the same PMSA conditions (see below), using 1 and 2 beads with reaction times of 1, 2, and 4 h and their respective positive and negative controls, the presence or absence of rec-PrPres propagation was evaluated by proteinase K digestion, electrophoresis and total protein staining. .. Preparation and Purification of Recombinant PrP for the PMSA Substrate The bacterial expression of bank vole I109 recombinant prion protein (rec-VoPrP) was achieved using a pOPIN E expression vector prepared using standard molecular biology procedures, as described previously ( ; ; ).

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  • 99
    Millipore proteinase k digestion
    Proteinase K Digestion, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/proteinase k digestion/product/Millipore
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    proteinase k digestion - by Bioz Stars, 2021-03
    99/100 stars
      Buy from Supplier

    97
    Millipore proteinase k solution
    Proteinase K Solution, supplied by Millipore, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/proteinase k solution/product/Millipore
    Average 97 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    proteinase k solution - by Bioz Stars, 2021-03
    97/100 stars
      Buy from Supplier

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