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GE Healthcare heat inactivated 60°c fetal bovine serum
Heat Inactivated 60°C Fetal Bovine Serum, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/heat inactivated 60°c fetal bovine serum/product/GE Healthcare
Average 85 stars, based on 1 article reviews
Price from $9.99 to $1999.99
heat inactivated 60°c fetal bovine serum - by Bioz Stars, 2020-08
85/100 stars

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Article Title: Respiratory Syncytial Virus (RSV) F and G Proteins Induce IL-1?, CC and CXC Chemokine Responses by Normal Human Bronchoepithelial Cells
Article Snippet: Viruses were propagated in VeroE6 cells maintained in DMEM (Sigma-Aldrich Corp., St. Louis, MO, USA.) supplemented with 5% heat-inactivated (60°C) fetal bovine serum (FBS; Hyclone Laboratories, Salt Lake City, UT) as previously described [ ].

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    GE Healthcare β lac
    AFM imaging of amyloid fibrils undergoing division through fragmentation promoted by mechanical stirring. Hen egg white Lyz, bovine milk <t>β-Lac,</t> and human α-Syn amyloid fibril samples (all 120 µ M monomer equivalent concentration) were stirred for up to 15 days. Samples were taken out periodically, deposited on mica and imaged using AFM. Typical AFM images representing 10×10 μm surface areas are show together with 4x magnified insets. The scale bar represents 2 μm in all images.
    β Lac, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 80/100, based on 0 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/β lac/product/GE Healthcare
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    GE Healthcare hybridization buffer
    AFM imaging of amyloid fibrils undergoing division through fragmentation promoted by mechanical stirring. Hen egg white Lyz, bovine milk <t>β-Lac,</t> and human α-Syn amyloid fibril samples (all 120 µ M monomer equivalent concentration) were stirred for up to 15 days. Samples were taken out periodically, deposited on mica and imaged using AFM. Typical AFM images representing 10×10 μm surface areas are show together with 4x magnified insets. The scale bar represents 2 μm in all images.
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    GE Healthcare histrap ff crude column
    AFM imaging of amyloid fibrils undergoing division through fragmentation promoted by mechanical stirring. Hen egg white Lyz, bovine milk <t>β-Lac,</t> and human α-Syn amyloid fibril samples (all 120 µ M monomer equivalent concentration) were stirred for up to 15 days. Samples were taken out periodically, deposited on mica and imaged using AFM. Typical AFM images representing 10×10 μm surface areas are show together with 4x magnified insets. The scale bar represents 2 μm in all images.
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    88
    GE Healthcare hitrap mabselect sure
    AFM imaging of amyloid fibrils undergoing division through fragmentation promoted by mechanical stirring. Hen egg white Lyz, bovine milk <t>β-Lac,</t> and human α-Syn amyloid fibril samples (all 120 µ M monomer equivalent concentration) were stirred for up to 15 days. Samples were taken out periodically, deposited on mica and imaged using AFM. Typical AFM images representing 10×10 μm surface areas are show together with 4x magnified insets. The scale bar represents 2 μm in all images.
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    Image Search Results


    AFM imaging of amyloid fibrils undergoing division through fragmentation promoted by mechanical stirring. Hen egg white Lyz, bovine milk β-Lac, and human α-Syn amyloid fibril samples (all 120 µ M monomer equivalent concentration) were stirred for up to 15 days. Samples were taken out periodically, deposited on mica and imaged using AFM. Typical AFM images representing 10×10 μm surface areas are show together with 4x magnified insets. The scale bar represents 2 μm in all images.

    Journal: bioRxiv

    Article Title: The division of amyloid fibrils – Systematic comparison of fibril fragmentation stability by linking theory with experiments

    doi: 10.1101/506386

    Figure Lengend Snippet: AFM imaging of amyloid fibrils undergoing division through fragmentation promoted by mechanical stirring. Hen egg white Lyz, bovine milk β-Lac, and human α-Syn amyloid fibril samples (all 120 µ M monomer equivalent concentration) were stirred for up to 15 days. Samples were taken out periodically, deposited on mica and imaged using AFM. Typical AFM images representing 10×10 μm surface areas are show together with 4x magnified insets. The scale bar represents 2 μm in all images.

    Article Snippet: 500 µ l aliquots were then heated without agitation for differing periods of time, with Lyz heated at 60 °C for 2 days and β-Lac heated at 90 °C for 5 hr. α-Syn fibrils were formed by buffer exchange of purified monomers into fibril forming buffer (20mM Sodium phosphate, pH7.5) using a PD-10 column (GE Healthcare).

    Techniques: Imaging, Concentration Assay

    Comparing the stability towards division of different amyloid fibril types. The decay of mean lengths (a), the division rate constants as function of fibril length (b), and the self-similar length distribution shapes (c) for hen egg Lyz (blue), bovine milk β-Lac (yellow), human α-Syn (red) and human β 2 m (black, data from Xue and Radford 2013 35 ) amyloid fibril samples undergoing division by fibril fragmentation under mechanical perturbation. All curves were calculated using α, γ, and g(x g ) obtained from our analysis of the experimental AFM images. In (a), the thicker portion of the lines denote the time range where the characteristic self-similar length distribution shape is observed in the imaging experiments (i.e. corresponding to the time regime represented by the solid fitted lines in Fig. 5 ), and crosses are the experimental data points that have closely reached the self-similar distribution shapes shown in the same plot. In (b), the thicker portion of the lines denote the range of fibril lengths observed experimentally on the AFM images. In (c), the distributions were calculated using self-similar distributions g(x g ) in Supplementary Fig. S3 after two weeks.

    Journal: bioRxiv

    Article Title: The division of amyloid fibrils – Systematic comparison of fibril fragmentation stability by linking theory with experiments

    doi: 10.1101/506386

    Figure Lengend Snippet: Comparing the stability towards division of different amyloid fibril types. The decay of mean lengths (a), the division rate constants as function of fibril length (b), and the self-similar length distribution shapes (c) for hen egg Lyz (blue), bovine milk β-Lac (yellow), human α-Syn (red) and human β 2 m (black, data from Xue and Radford 2013 35 ) amyloid fibril samples undergoing division by fibril fragmentation under mechanical perturbation. All curves were calculated using α, γ, and g(x g ) obtained from our analysis of the experimental AFM images. In (a), the thicker portion of the lines denote the time range where the characteristic self-similar length distribution shape is observed in the imaging experiments (i.e. corresponding to the time regime represented by the solid fitted lines in Fig. 5 ), and crosses are the experimental data points that have closely reached the self-similar distribution shapes shown in the same plot. In (b), the thicker portion of the lines denote the range of fibril lengths observed experimentally on the AFM images. In (c), the distributions were calculated using self-similar distributions g(x g ) in Supplementary Fig. S3 after two weeks.

    Article Snippet: 500 µ l aliquots were then heated without agitation for differing periods of time, with Lyz heated at 60 °C for 2 days and β-Lac heated at 90 °C for 5 hr. α-Syn fibrils were formed by buffer exchange of purified monomers into fibril forming buffer (20mM Sodium phosphate, pH7.5) using a PD-10 column (GE Healthcare).

    Techniques: Imaging