buffer  (Millipore)

 
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 97
    Name:
    Pluronic F 127
    Description:

    Catalog Number:
    P2443
    Price:
    None
    Applications:
    Pluronic(R) F-127 was used to coat a siliconized coverslip to hold an egg extract in a study. Pluronic F-127 was added to phosphate buffered saline (PBS), to lower unspecific cell and protein adhesion to a PDMS-based microfluidic device. A study reports its use as a release vehicle to transport low-dose perivascular lipopolysaccharide (LPS) on mouse vein grafts. PLGA/pluronic F127 may be used to fabricate nerve guidance conduits (NGCs) for regeneration of peripheral nerve. Fabrication of poly (lactide-co-glycolide) (PLGA) - Pluronic F127 glass composites was reported. Pluronic F-127 was used for fluorescent labeling of blood vessels, astrocytes, and neurons.
    Buy from Supplier


    Structured Review

    Millipore buffer
    Pluronic F 127

    https://www.bioz.com/result/buffer/product/Millipore
    Average 97 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    buffer - by Bioz Stars, 2021-05
    97/100 stars

    Images

    Related Articles

    Concentration Assay:

    Article Title: Disturbance of cellular homeostasis as a molecular risk evaluation of human endothelial cells exposed to nanoparticles
    Article Snippet: Finally the NPs were recovered by ultra-centrifugation (20,000 rpm) at 25 °C for 10 min (Centrifugal Beckman Coulter J 25, Brea, CA, USA) and AMF images were taken if NPs were ready for experiments referred to as human endothelium cells . .. Pluronic F127 Ms production The Pluronic F127 Ms was prepared using dispersed Pluronics F127 (Sigma-Aldrich) at a concentration of 12% (w/w) in water. .. Briefly, 100 mL of water were added to 12 mg of Pluronics F127 and gently stirred using a magnetic bar (Magnetic Stirrer, IKA, C-MAG HS-7) for 3 min and then processed for 3 min using an ultrasonic processor (UP100H, Hielscher, Power: 60%, Cycle: 1) in an ice bath at 10 °C.

    other:

    Article Title: Targeted dual-color silica nanoparticles provide univocal identification of micrometastases in preclinical models of colorectal cancer
    Article Snippet: Chemicals and antibodies Pluronic® F127 (PF-127), tetraethyl orthosilicate (TEOS, 99.99%), chlorotrimethylsilane (TMSCl, ≥98%), HCl (≥37%), AlMe3 (toluene solution 2.0 M), Rhod base ( > 98%), reagent grade dimethylformamide and diethylether (Et2 O) were from Sigma-Aldrich (St Louis, MO).

    Article Title: A Novel Strategy for Creating Tissue-Engineered Biomimetic Blood Vessels Using 3D Bioprinting Technology
    Article Snippet: Specifically, 40 wt % Pluronic F127 (Sigma) in deionized, ultrafiltrated (DIUF) water was homogenized using a Thinky mixer until the powder was fully dissolved, and subsequently stored at 4 °C.

    Molecular Weight:

    Article Title: Biocompatible and Antibacterial Nitric Oxide-Releasing Pluronic F-127/Chitosan Hydrogel for Topical Applications
    Article Snippet: Interestingly, the concentration of NO-releasing hydrogel required for an antibacterial effect was not toxic towards mammalian cells, indicating the promising and safe uses of this biomaterial in topical applications. .. Materials Chitosan (CS, low molecular weight, 75% deacetylation), glutathione (GSH), sodium nitrite (NaNO2 ), Pluronic F-127 (PL) ([poly(ethylene oxide)]106 [poly(propylene oxide)]70 [poly(ethylene oxide)]106 , molar weight of 12,600 kDa), phosphate buffer saline (PBS, pH 7.4), MTT (3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide) and phenol were obtained from Sigma-Aldrich (St. Louis, MO, USA). ..

    MTT Assay:

    Article Title: Biocompatible and Antibacterial Nitric Oxide-Releasing Pluronic F-127/Chitosan Hydrogel for Topical Applications
    Article Snippet: Interestingly, the concentration of NO-releasing hydrogel required for an antibacterial effect was not toxic towards mammalian cells, indicating the promising and safe uses of this biomaterial in topical applications. .. Materials Chitosan (CS, low molecular weight, 75% deacetylation), glutathione (GSH), sodium nitrite (NaNO2 ), Pluronic F-127 (PL) ([poly(ethylene oxide)]106 [poly(propylene oxide)]70 [poly(ethylene oxide)]106 , molar weight of 12,600 kDa), phosphate buffer saline (PBS, pH 7.4), MTT (3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide) and phenol were obtained from Sigma-Aldrich (St. Louis, MO, USA). ..

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 99
    Millipore buffer f
    Effect of loss of Rpn10/p54 (A and C) proteasome subunit or Usp5 deubiquitylase (B and C) on the abundance of ubiquitin forms. Whole protein extracts in <t>buffer</t> F (lanes 1, 2, 5 and 6; +NEM) and buffer T (lanes 3, 4, 7 and 8; -NEM) of wandering L3 larvae were investigated by western blotting using polyclonal anti-Ub antibody at a dilution of 1:1000. The bands just below the 10 kDa mark on the immunoblots (A and B) represent free monoubiquitins, and only the intensity of these bands were determined and used for quantification. 5 μg total protein extracts were loaded to lanes 2 and 6, while samples were diluted 1.7-fold to lanes 1 and 5; twofold to lanes 3, 4 and 8; and 3.3-fold to lane 7 before loading to avoid overloading the monoubiquitin band. Ubiquitin content (small table in C) was calculated by plotting band intensities against Ub standards and a regression line equation was generated by applying the four parameter curve fit model (R 2 = 0.9979 for Rpn10/p54 and R 2 = 0.9933 for Usp5), values were normalized to total protein content and shown as a column diagram.
    Buffer F, 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/buffer f/product/Millipore
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    buffer f - by Bioz Stars, 2021-05
    99/100 stars
      Buy from Supplier

    92
    Millipore cytochrome c reaction buffer
    LC-MS/MS spectra of the NAC-BQ modified <t>cytochrome</t> c peptide. The LC-MS/MS raw data was analyzed by Sequest, X!Tandem, and P-Mod, followed by manual validation. The peptide 39 KTGCQAPGFTYTDANK 53 was identified with a 268-Da adduct on K 39 .
    Cytochrome C Reaction Buffer, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/cytochrome c reaction buffer/product/Millipore
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    cytochrome c reaction buffer - by Bioz Stars, 2021-05
    92/100 stars
      Buy from Supplier

    Image Search Results


    Effect of loss of Rpn10/p54 (A and C) proteasome subunit or Usp5 deubiquitylase (B and C) on the abundance of ubiquitin forms. Whole protein extracts in buffer F (lanes 1, 2, 5 and 6; +NEM) and buffer T (lanes 3, 4, 7 and 8; -NEM) of wandering L3 larvae were investigated by western blotting using polyclonal anti-Ub antibody at a dilution of 1:1000. The bands just below the 10 kDa mark on the immunoblots (A and B) represent free monoubiquitins, and only the intensity of these bands were determined and used for quantification. 5 μg total protein extracts were loaded to lanes 2 and 6, while samples were diluted 1.7-fold to lanes 1 and 5; twofold to lanes 3, 4 and 8; and 3.3-fold to lane 7 before loading to avoid overloading the monoubiquitin band. Ubiquitin content (small table in C) was calculated by plotting band intensities against Ub standards and a regression line equation was generated by applying the four parameter curve fit model (R 2 = 0.9979 for Rpn10/p54 and R 2 = 0.9933 for Usp5), values were normalized to total protein content and shown as a column diagram.

    Journal: PLoS ONE

    Article Title: Developmental and tissue specific changes of ubiquitin forms in Drosophila melanogaster

    doi: 10.1371/journal.pone.0209080

    Figure Lengend Snippet: Effect of loss of Rpn10/p54 (A and C) proteasome subunit or Usp5 deubiquitylase (B and C) on the abundance of ubiquitin forms. Whole protein extracts in buffer F (lanes 1, 2, 5 and 6; +NEM) and buffer T (lanes 3, 4, 7 and 8; -NEM) of wandering L3 larvae were investigated by western blotting using polyclonal anti-Ub antibody at a dilution of 1:1000. The bands just below the 10 kDa mark on the immunoblots (A and B) represent free monoubiquitins, and only the intensity of these bands were determined and used for quantification. 5 μg total protein extracts were loaded to lanes 2 and 6, while samples were diluted 1.7-fold to lanes 1 and 5; twofold to lanes 3, 4 and 8; and 3.3-fold to lane 7 before loading to avoid overloading the monoubiquitin band. Ubiquitin content (small table in C) was calculated by plotting band intensities against Ub standards and a regression line equation was generated by applying the four parameter curve fit model (R 2 = 0.9979 for Rpn10/p54 and R 2 = 0.9933 for Usp5), values were normalized to total protein content and shown as a column diagram.

    Article Snippet: The animal and tissue samples were homogenized by plastic tissue grinders in pre-chilled microfuge tubes either in 100 μl ice cold buffer F [100 mM Tris, pH 7.6, 150 mM NaCl, 1mM EDTA, 10 mM N-Ethylmaleimide (NEM, Sigma-Aldrich), 20μM MG132 (Calbiochem) and 1× EDTA-Free Complete Protease Inhibitor Cocktail (Roche)] or 100 μl buffer T [Buffer F supplemented with 2mM DTT to preserve the catalytic activity of DUBs, but without NEM], respectively.

    Techniques: Western Blot, Generated

    Effect of loss of Rpn10/p54 (A and C) proteasome subunit or Usp5 deubiquitylase (B and C) on the abundance of ubiquitin forms. Whole protein extracts in buffer F (lanes 1, 2, 5 and 6; +NEM) and buffer T (lanes 3, 4, 7 and 8; -NEM) of wandering L3 larvae were investigated by western blotting using polyclonal anti-Ub antibody at a dilution of 1:1000. The bands just below the 10 kDa mark on the immunoblots (A and B) represent free monoubiquitins, and only the intensity of these bands were determined and used for quantification. 5 μg total protein extracts were loaded to lanes 2 and 6, while samples were diluted 1.7-fold to lanes 1 and 5; twofold to lanes 3, 4 and 8; and 3.3-fold to lane 7 before loading to avoid overloading the monoubiquitin band. Ubiquitin content (small table in C) was calculated by plotting band intensities against Ub standards and a regression line equation was generated by applying the four parameter curve fit model (R 2 = 0.9979 for Rpn10/p54 and R 2 = 0.9933 for Usp5), values were normalized to total protein content and shown as a column diagram.

    Journal: PLoS ONE

    Article Title: Developmental and tissue specific changes of ubiquitin forms in Drosophila melanogaster

    doi: 10.1371/journal.pone.0209080

    Figure Lengend Snippet: Effect of loss of Rpn10/p54 (A and C) proteasome subunit or Usp5 deubiquitylase (B and C) on the abundance of ubiquitin forms. Whole protein extracts in buffer F (lanes 1, 2, 5 and 6; +NEM) and buffer T (lanes 3, 4, 7 and 8; -NEM) of wandering L3 larvae were investigated by western blotting using polyclonal anti-Ub antibody at a dilution of 1:1000. The bands just below the 10 kDa mark on the immunoblots (A and B) represent free monoubiquitins, and only the intensity of these bands were determined and used for quantification. 5 μg total protein extracts were loaded to lanes 2 and 6, while samples were diluted 1.7-fold to lanes 1 and 5; twofold to lanes 3, 4 and 8; and 3.3-fold to lane 7 before loading to avoid overloading the monoubiquitin band. Ubiquitin content (small table in C) was calculated by plotting band intensities against Ub standards and a regression line equation was generated by applying the four parameter curve fit model (R 2 = 0.9979 for Rpn10/p54 and R 2 = 0.9933 for Usp5), values were normalized to total protein content and shown as a column diagram.

    Article Snippet: The animal and tissue samples were homogenized by plastic tissue grinders in pre-chilled microfuge tubes either in 100 μl ice cold buffer F [100 mM Tris, pH 7.6, 150 mM NaCl, 1mM EDTA, 10 mM N-Ethylmaleimide (NEM, Sigma-Aldrich), 20μM MG132 (Calbiochem) and 1× EDTA-Free Complete Protease Inhibitor Cocktail (Roche)] or 100 μl buffer T [Buffer F supplemented with 2mM DTT to preserve the catalytic activity of DUBs, but without NEM], respectively.

    Techniques: Western Blot, Generated

    LC-MS/MS spectra of the NAC-BQ modified cytochrome c peptide. The LC-MS/MS raw data was analyzed by Sequest, X!Tandem, and P-Mod, followed by manual validation. The peptide 39 KTGCQAPGFTYTDANK 53 was identified with a 268-Da adduct on K 39 .

    Journal: Methods in molecular biology (Clifton, N.J.)

    Article Title: Utilization of LC-MS/MS Analyses to Identify Site-Specific Chemical Protein Adducts In Vitro

    doi: 10.1007/978-1-60761-849-2_19

    Figure Lengend Snippet: LC-MS/MS spectra of the NAC-BQ modified cytochrome c peptide. The LC-MS/MS raw data was analyzed by Sequest, X!Tandem, and P-Mod, followed by manual validation. The peptide 39 KTGCQAPGFTYTDANK 53 was identified with a 268-Da adduct on K 39 .

    Article Snippet: Cytochrome c reaction buffer: 10 mM Tris–HCl, pH 7.5 used with horse heart cytochrome c (Sigma).

    Techniques: Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry, Modification

    MALDI-TOF whole protein spectra for cytochrome c reacted with NAC-BQ. ( a ) Control spectrum of cytochrome c in 10 mM Tris–HCl pH 7.5, where the peak at 12,360 m/z indicates native cytochrome c . ( b ) Cytochrome c was incubated in 10 mM Tris–HCl

    Journal: Methods in molecular biology (Clifton, N.J.)

    Article Title: Utilization of MALDI-TOF to Determine Chemical-Protein Adduct Formation In Vitro

    doi: 10.1007/978-1-60761-849-2_18

    Figure Lengend Snippet: MALDI-TOF whole protein spectra for cytochrome c reacted with NAC-BQ. ( a ) Control spectrum of cytochrome c in 10 mM Tris–HCl pH 7.5, where the peak at 12,360 m/z indicates native cytochrome c . ( b ) Cytochrome c was incubated in 10 mM Tris–HCl

    Article Snippet: Cytochrome c reaction buffer: 10 mM Tris–HCl (Sigma), pH 7.5, used with horse heart cytochrome c (Sigma).

    Techniques: Incubation