plate mixer Search Results


plate mixer  (BIOTEC Co Ltd)
90
BIOTEC Co Ltd plate mixer
Plate Mixer, supplied by BIOTEC Co Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/plate+mixer/plate+mixer/pm38999824-58-7-9
Average 90 stars, based on 1 article reviews
plate mixer - by Bioz Stars, 2026-10
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plate mixer p-10  (Juji Field Inc)
90
Juji Field Inc plate mixer p-10
Plate Mixer P 10, supplied by Juji Field Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/plate+mixer/plate+mixer+p+10/us10676783-160-48-53
Average 90 stars, based on 1 article reviews
plate mixer p-10 - by Bioz Stars, 2026-10
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mp orbital plate shaker incu-mixer mp  (Benchmark Scientific)
90
Benchmark Scientific mp orbital plate shaker incu-mixer mp
Additional factors influencing in vitro fibril formation. Amyloidogenic VL protein was subjected to fibril formation under standard conditions (37 °C, 900 rpm at 20 μM in PBS, pH7.4) in the presence of 10 μM ThT. Fluorescence signal (ex440nm/em485nm) at each time point was normalized to the ThT signal at time 0 and presented as mean ± S.E. (error bars). All experiments were performed under the same standard conditions except for one variable changed as indicated for each subfigure. A, amyloid fibril formation at different protein concentrations. WIL (λ6) VL protein was subjected to fibril formation at 80 μM (blue circles), 60 μM (red circles), 20 μM (green circles) as well as 10 μM, 5 μM, and 1 μM concentrations (not shown on the graph). B, Amyloid fibril formation at different shaking <t>speed/shaker</t> model. WIL (λ6) VL protein was subjected to fibril formation at 410 rpm (blue triangles), 500 rpm (red squares), and 1200 rpm (not shown on the graph) on MP <t>orbital</t> <t>plate</t> shaker and speed setting #3 of Thermo orbital plate shaker. **, statistical significance with p < 0.01. ***, statistical significance with p < 0.001. ns, not significant. The mark of successful fibril formation (normalized ThT signal over 4) is shown on both fibril formation graphs with a dashed black line. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
Mp Orbital Plate Shaker Incu Mixer Mp, supplied by Benchmark Scientific, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/plate+mixer/orbital+plate+shaker+incu+mixer+mp/pmc09982448-164-36-42
Average 90 stars, based on 1 article reviews
mp orbital plate shaker incu-mixer mp - by Bioz Stars, 2026-10
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plate mixer  (AGC Techno Glass Co Ltd)
90
AGC Techno Glass Co Ltd plate mixer
Additional factors influencing in vitro fibril formation. Amyloidogenic VL protein was subjected to fibril formation under standard conditions (37 °C, 900 rpm at 20 μM in PBS, pH7.4) in the presence of 10 μM ThT. Fluorescence signal (ex440nm/em485nm) at each time point was normalized to the ThT signal at time 0 and presented as mean ± S.E. (error bars). All experiments were performed under the same standard conditions except for one variable changed as indicated for each subfigure. A, amyloid fibril formation at different protein concentrations. WIL (λ6) VL protein was subjected to fibril formation at 80 μM (blue circles), 60 μM (red circles), 20 μM (green circles) as well as 10 μM, 5 μM, and 1 μM concentrations (not shown on the graph). B, Amyloid fibril formation at different shaking <t>speed/shaker</t> model. WIL (λ6) VL protein was subjected to fibril formation at 410 rpm (blue triangles), 500 rpm (red squares), and 1200 rpm (not shown on the graph) on MP <t>orbital</t> <t>plate</t> shaker and speed setting #3 of Thermo orbital plate shaker. **, statistical significance with p < 0.01. ***, statistical significance with p < 0.001. ns, not significant. The mark of successful fibril formation (normalized ThT signal over 4) is shown on both fibril formation graphs with a dashed black line. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
Plate Mixer, supplied by AGC Techno Glass Co Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/plate+mixer/plate+mixer/pm33149906-36-21-24
Average 90 stars, based on 1 article reviews
plate mixer - by Bioz Stars, 2026-10
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plate shaker incu-mixer mp  (Benchmark Scientific)
90
Benchmark Scientific plate shaker incu-mixer mp
Additional factors influencing in vitro fibril formation. Amyloidogenic VL protein was subjected to fibril formation under standard conditions (37 °C, 900 rpm at 20 μM in PBS, pH7.4) in the presence of 10 μM ThT. Fluorescence signal (ex440nm/em485nm) at each time point was normalized to the ThT signal at time 0 and presented as mean ± S.E. (error bars). All experiments were performed under the same standard conditions except for one variable changed as indicated for each subfigure. A, amyloid fibril formation at different protein concentrations. WIL (λ6) VL protein was subjected to fibril formation at 80 μM (blue circles), 60 μM (red circles), 20 μM (green circles) as well as 10 μM, 5 μM, and 1 μM concentrations (not shown on the graph). B, Amyloid fibril formation at different shaking <t>speed/shaker</t> model. WIL (λ6) VL protein was subjected to fibril formation at 410 rpm (blue triangles), 500 rpm (red squares), and 1200 rpm (not shown on the graph) on MP <t>orbital</t> <t>plate</t> shaker and speed setting #3 of Thermo orbital plate shaker. **, statistical significance with p < 0.01. ***, statistical significance with p < 0.001. ns, not significant. The mark of successful fibril formation (normalized ThT signal over 4) is shown on both fibril formation graphs with a dashed black line. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
Plate Shaker Incu Mixer Mp, supplied by Benchmark Scientific, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/plate+mixer/plate+shaker+incu+mixer+mp/pmc09089379-20-3-7
Average 90 stars, based on 1 article reviews
plate shaker incu-mixer mp - by Bioz Stars, 2026-10
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household mixer equipped with a grinding apparatus (5 plate diameter)  (KitchenAid Inc)
90
KitchenAid Inc household mixer equipped with a grinding apparatus (5 plate diameter)
Additional factors influencing in vitro fibril formation. Amyloidogenic VL protein was subjected to fibril formation under standard conditions (37 °C, 900 rpm at 20 μM in PBS, pH7.4) in the presence of 10 μM ThT. Fluorescence signal (ex440nm/em485nm) at each time point was normalized to the ThT signal at time 0 and presented as mean ± S.E. (error bars). All experiments were performed under the same standard conditions except for one variable changed as indicated for each subfigure. A, amyloid fibril formation at different protein concentrations. WIL (λ6) VL protein was subjected to fibril formation at 80 μM (blue circles), 60 μM (red circles), 20 μM (green circles) as well as 10 μM, 5 μM, and 1 μM concentrations (not shown on the graph). B, Amyloid fibril formation at different shaking <t>speed/shaker</t> model. WIL (λ6) VL protein was subjected to fibril formation at 410 rpm (blue triangles), 500 rpm (red squares), and 1200 rpm (not shown on the graph) on MP <t>orbital</t> <t>plate</t> shaker and speed setting #3 of Thermo orbital plate shaker. **, statistical significance with p < 0.01. ***, statistical significance with p < 0.001. ns, not significant. The mark of successful fibril formation (normalized ThT signal over 4) is shown on both fibril formation graphs with a dashed black line. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
Household Mixer Equipped With A Grinding Apparatus (5 Plate Diameter), supplied by KitchenAid Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/plate+mixer/household+mixer+equipped+with+a+grinding+apparatus++5+plate+diameter+/10__1021_slash_jf4006142-79-25-17
Average 90 stars, based on 1 article reviews
household mixer equipped with a grinding apparatus (5 plate diameter) - by Bioz Stars, 2026-10
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plate s2 mixer cavity  (CEM Corporation)
90
CEM Corporation plate s2 mixer cavity
Additional factors influencing in vitro fibril formation. Amyloidogenic VL protein was subjected to fibril formation under standard conditions (37 °C, 900 rpm at 20 μM in PBS, pH7.4) in the presence of 10 μM ThT. Fluorescence signal (ex440nm/em485nm) at each time point was normalized to the ThT signal at time 0 and presented as mean ± S.E. (error bars). All experiments were performed under the same standard conditions except for one variable changed as indicated for each subfigure. A, amyloid fibril formation at different protein concentrations. WIL (λ6) VL protein was subjected to fibril formation at 80 μM (blue circles), 60 μM (red circles), 20 μM (green circles) as well as 10 μM, 5 μM, and 1 μM concentrations (not shown on the graph). B, Amyloid fibril formation at different shaking <t>speed/shaker</t> model. WIL (λ6) VL protein was subjected to fibril formation at 410 rpm (blue triangles), 500 rpm (red squares), and 1200 rpm (not shown on the graph) on MP <t>orbital</t> <t>plate</t> shaker and speed setting #3 of Thermo orbital plate shaker. **, statistical significance with p < 0.01. ***, statistical significance with p < 0.001. ns, not significant. The mark of successful fibril formation (normalized ThT signal over 4) is shown on both fibril formation graphs with a dashed black line. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
Plate S2 Mixer Cavity, supplied by CEM Corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/plate+mixer/plate+s2+mixer+cavity/us08695346-130-19-18
Average 90 stars, based on 1 article reviews
plate s2 mixer cavity - by Bioz Stars, 2026-10
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plate mixer mx-m96  (SCILOGEX Inc)
90
SCILOGEX Inc plate mixer mx-m96
Additional factors influencing in vitro fibril formation. Amyloidogenic VL protein was subjected to fibril formation under standard conditions (37 °C, 900 rpm at 20 μM in PBS, pH7.4) in the presence of 10 μM ThT. Fluorescence signal (ex440nm/em485nm) at each time point was normalized to the ThT signal at time 0 and presented as mean ± S.E. (error bars). All experiments were performed under the same standard conditions except for one variable changed as indicated for each subfigure. A, amyloid fibril formation at different protein concentrations. WIL (λ6) VL protein was subjected to fibril formation at 80 μM (blue circles), 60 μM (red circles), 20 μM (green circles) as well as 10 μM, 5 μM, and 1 μM concentrations (not shown on the graph). B, Amyloid fibril formation at different shaking <t>speed/shaker</t> model. WIL (λ6) VL protein was subjected to fibril formation at 410 rpm (blue triangles), 500 rpm (red squares), and 1200 rpm (not shown on the graph) on MP <t>orbital</t> <t>plate</t> shaker and speed setting #3 of Thermo orbital plate shaker. **, statistical significance with p < 0.01. ***, statistical significance with p < 0.001. ns, not significant. The mark of successful fibril formation (normalized ThT signal over 4) is shown on both fibril formation graphs with a dashed black line. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
Plate Mixer Mx M96, supplied by SCILOGEX Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/plate+mixer/plate+mixer+mx+m96/10__1016_slash_j__rechem__2023__101187-34-21-24
Average 90 stars, based on 1 article reviews
plate mixer mx-m96 - by Bioz Stars, 2026-10
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plate mixer  (Labnet International Inc)
90
Labnet International Inc plate mixer
Additional factors influencing in vitro fibril formation. Amyloidogenic VL protein was subjected to fibril formation under standard conditions (37 °C, 900 rpm at 20 μM in PBS, pH7.4) in the presence of 10 μM ThT. Fluorescence signal (ex440nm/em485nm) at each time point was normalized to the ThT signal at time 0 and presented as mean ± S.E. (error bars). All experiments were performed under the same standard conditions except for one variable changed as indicated for each subfigure. A, amyloid fibril formation at different protein concentrations. WIL (λ6) VL protein was subjected to fibril formation at 80 μM (blue circles), 60 μM (red circles), 20 μM (green circles) as well as 10 μM, 5 μM, and 1 μM concentrations (not shown on the graph). B, Amyloid fibril formation at different shaking <t>speed/shaker</t> model. WIL (λ6) VL protein was subjected to fibril formation at 410 rpm (blue triangles), 500 rpm (red squares), and 1200 rpm (not shown on the graph) on MP <t>orbital</t> <t>plate</t> shaker and speed setting #3 of Thermo orbital plate shaker. **, statistical significance with p < 0.01. ***, statistical significance with p < 0.001. ns, not significant. The mark of successful fibril formation (normalized ThT signal over 4) is shown on both fibril formation graphs with a dashed black line. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
Plate Mixer, supplied by Labnet International Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/plate+mixer/plate+mixer/pmc02730752-52-6-8
Average 90 stars, based on 1 article reviews
plate mixer - by Bioz Stars, 2026-10
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plate mixer  (FINEPCR Co Ltd)
90
FINEPCR Co Ltd plate mixer
Additional factors influencing in vitro fibril formation. Amyloidogenic VL protein was subjected to fibril formation under standard conditions (37 °C, 900 rpm at 20 μM in PBS, pH7.4) in the presence of 10 μM ThT. Fluorescence signal (ex440nm/em485nm) at each time point was normalized to the ThT signal at time 0 and presented as mean ± S.E. (error bars). All experiments were performed under the same standard conditions except for one variable changed as indicated for each subfigure. A, amyloid fibril formation at different protein concentrations. WIL (λ6) VL protein was subjected to fibril formation at 80 μM (blue circles), 60 μM (red circles), 20 μM (green circles) as well as 10 μM, 5 μM, and 1 μM concentrations (not shown on the graph). B, Amyloid fibril formation at different shaking <t>speed/shaker</t> model. WIL (λ6) VL protein was subjected to fibril formation at 410 rpm (blue triangles), 500 rpm (red squares), and 1200 rpm (not shown on the graph) on MP <t>orbital</t> <t>plate</t> shaker and speed setting #3 of Thermo orbital plate shaker. **, statistical significance with p < 0.01. ***, statistical significance with p < 0.001. ns, not significant. The mark of successful fibril formation (normalized ThT signal over 4) is shown on both fibril formation graphs with a dashed black line. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
Plate Mixer, supplied by FINEPCR Co Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/plate+mixer/plate+mixer/us10556906-226-10-12
Average 90 stars, based on 1 article reviews
plate mixer - by Bioz Stars, 2026-10
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mixer/grinder with a 1/8'' plate and a bone separator  (Hollymatic Corporation)
90
Hollymatic Corporation mixer/grinder with a 1/8'' plate and a bone separator
Additional factors influencing in vitro fibril formation. Amyloidogenic VL protein was subjected to fibril formation under standard conditions (37 °C, 900 rpm at 20 μM in PBS, pH7.4) in the presence of 10 μM ThT. Fluorescence signal (ex440nm/em485nm) at each time point was normalized to the ThT signal at time 0 and presented as mean ± S.E. (error bars). All experiments were performed under the same standard conditions except for one variable changed as indicated for each subfigure. A, amyloid fibril formation at different protein concentrations. WIL (λ6) VL protein was subjected to fibril formation at 80 μM (blue circles), 60 μM (red circles), 20 μM (green circles) as well as 10 μM, 5 μM, and 1 μM concentrations (not shown on the graph). B, Amyloid fibril formation at different shaking <t>speed/shaker</t> model. WIL (λ6) VL protein was subjected to fibril formation at 410 rpm (blue triangles), 500 rpm (red squares), and 1200 rpm (not shown on the graph) on MP <t>orbital</t> <t>plate</t> shaker and speed setting #3 of Thermo orbital plate shaker. **, statistical significance with p < 0.01. ***, statistical significance with p < 0.001. ns, not significant. The mark of successful fibril formation (normalized ThT signal over 4) is shown on both fibril formation graphs with a dashed black line. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
Mixer/Grinder With A 1/8'' Plate And A Bone Separator, supplied by Hollymatic Corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/plate+mixer/mixer+grinder+with+a+1+8+++plate+and+a+bone+separator/us11819032-225-34-26
Average 90 stars, based on 1 article reviews
mixer/grinder with a 1/8'' plate and a bone separator - by Bioz Stars, 2026-10
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bioshake 3000 elm orbital plate mixer  (QUANTIFOIL gmbh)
90
QUANTIFOIL gmbh bioshake 3000 elm orbital plate mixer
Additional factors influencing in vitro fibril formation. Amyloidogenic VL protein was subjected to fibril formation under standard conditions (37 °C, 900 rpm at 20 μM in PBS, pH7.4) in the presence of 10 μM ThT. Fluorescence signal (ex440nm/em485nm) at each time point was normalized to the ThT signal at time 0 and presented as mean ± S.E. (error bars). All experiments were performed under the same standard conditions except for one variable changed as indicated for each subfigure. A, amyloid fibril formation at different protein concentrations. WIL (λ6) VL protein was subjected to fibril formation at 80 μM (blue circles), 60 μM (red circles), 20 μM (green circles) as well as 10 μM, 5 μM, and 1 μM concentrations (not shown on the graph). B, Amyloid fibril formation at different shaking <t>speed/shaker</t> model. WIL (λ6) VL protein was subjected to fibril formation at 410 rpm (blue triangles), 500 rpm (red squares), and 1200 rpm (not shown on the graph) on MP <t>orbital</t> <t>plate</t> shaker and speed setting #3 of Thermo orbital plate shaker. **, statistical significance with p < 0.01. ***, statistical significance with p < 0.001. ns, not significant. The mark of successful fibril formation (normalized ThT signal over 4) is shown on both fibril formation graphs with a dashed black line. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
Bioshake 3000 Elm Orbital Plate Mixer, supplied by QUANTIFOIL gmbh, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/plate+mixer/bioshake+3000+elm+orbital+plate+mixer/bio_rxiv__2022__09__09__507123-151-30-36
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bioshake 3000 elm orbital plate mixer - by Bioz Stars, 2026-10
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Image Search Results


Additional factors influencing in vitro fibril formation. Amyloidogenic VL protein was subjected to fibril formation under standard conditions (37 °C, 900 rpm at 20 μM in PBS, pH7.4) in the presence of 10 μM ThT. Fluorescence signal (ex440nm/em485nm) at each time point was normalized to the ThT signal at time 0 and presented as mean ± S.E. (error bars). All experiments were performed under the same standard conditions except for one variable changed as indicated for each subfigure. A, amyloid fibril formation at different protein concentrations. WIL (λ6) VL protein was subjected to fibril formation at 80 μM (blue circles), 60 μM (red circles), 20 μM (green circles) as well as 10 μM, 5 μM, and 1 μM concentrations (not shown on the graph). B, Amyloid fibril formation at different shaking speed/shaker model. WIL (λ6) VL protein was subjected to fibril formation at 410 rpm (blue triangles), 500 rpm (red squares), and 1200 rpm (not shown on the graph) on MP orbital plate shaker and speed setting #3 of Thermo orbital plate shaker. **, statistical significance with p < 0.01. ***, statistical significance with p < 0.001. ns, not significant. The mark of successful fibril formation (normalized ThT signal over 4) is shown on both fibril formation graphs with a dashed black line. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

Journal: Biochemistry and Biophysics Reports

Article Title: Producing amyloid fibrils in vitro: A tool for studying AL amyloidosis

doi: 10.1016/j.bbrep.2023.101442

Figure Lengend Snippet: Additional factors influencing in vitro fibril formation. Amyloidogenic VL protein was subjected to fibril formation under standard conditions (37 °C, 900 rpm at 20 μM in PBS, pH7.4) in the presence of 10 μM ThT. Fluorescence signal (ex440nm/em485nm) at each time point was normalized to the ThT signal at time 0 and presented as mean ± S.E. (error bars). All experiments were performed under the same standard conditions except for one variable changed as indicated for each subfigure. A, amyloid fibril formation at different protein concentrations. WIL (λ6) VL protein was subjected to fibril formation at 80 μM (blue circles), 60 μM (red circles), 20 μM (green circles) as well as 10 μM, 5 μM, and 1 μM concentrations (not shown on the graph). B, Amyloid fibril formation at different shaking speed/shaker model. WIL (λ6) VL protein was subjected to fibril formation at 410 rpm (blue triangles), 500 rpm (red squares), and 1200 rpm (not shown on the graph) on MP orbital plate shaker and speed setting #3 of Thermo orbital plate shaker. **, statistical significance with p < 0.01. ***, statistical significance with p < 0.001. ns, not significant. The mark of successful fibril formation (normalized ThT signal over 4) is shown on both fibril formation graphs with a dashed black line. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

Article Snippet: To test this hypothesis, WIL VL protein was subjected to fibril formation under standard conditions (37 °C, 20 μM of protein in PBS, pH7.4, 10 μM ThT) at 410 rpm, 500 rpm, and 1200 rpm on MP orbital plate shaker (Incu-Mixer MP (Benchmark Scientific, Sayreville, NJ), as well as at speed setting #3 (∼300 rpm) of Thermo orbital plate shaker (Thermo Scientific Titer Plate Shaker 4625), B.

Techniques: In Vitro, Fluorescence