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Amicon ultra 4 spin filter tube

Manufactured by Merck Group

The Amicon Ultra-4 spin filter tube is a laboratory centrifugal device used for the concentration and purification of macromolecules, such as proteins, from solutions. The device utilizes a semi-permeable membrane to selectively retain the desired macromolecules while allowing smaller molecules and solvents to pass through during the centrifugation process.

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4 protocols using amicon ultra 4 spin filter tube

1

Time-lapse Imaging of Bacterial Cell Dynamics

Check if the same lab product or an alternative is used in the 5 most similar protocols
Leaf245 was grown in R-2A+M broth and the supernatant was concentrated
200-fold with an Amicon Ultra-4 spin filter tube (100 kDa, Merck). Leaf374 grown
on R-2A+M agar was resuspended in PBS pH7.4 (10 mM
Na2HPO4, 1.8 mM KH2PO4, 137 mM NaCl,
2.7 mM KCl), spotted on a LB agar pad and dried. The concentrated supernatant of
Leaf 245 was added (10 μL) and imaging was started one minute later.
Phase contrast images were acquired on a Zeiss Axio Observer Z1 inverted
microscope (Carl Zeiss AG) equipped with an EC Plan-Neofluar 100x/1.3 objective.
Images were taken every 20 seconds over the course of 20 minutes and combined to
a time lapse video using Fiji software78 (link).
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2

His-Tagged Protein Purification by FPLC

Check if the same lab product or an alternative is used in the 5 most similar protocols
Affinity purification was carried out on an ÄKTA Purifier 10 FPLC
system (GE healthcare). Cleared cell lysate (4-6 mL) was passed through a 0.22
µm PES filter (TechnoPlasticProducts) and loaded on a HisTrap™ HP
column (1 mL, Cytiva) equilibrated with 20 mM TRIS-HCl pH 7.5 containing 250 mM
NaCl and 40 mM imidazole. The column was washed with 10 column volumes of the
same buffer and bound proteins were eluted over a gradient of 10 mL to a final
concentration of 500 mM imidazole. Elution of proteins was monitored by
absorption at 215 and 280 nm and 1 mL fractions were collected. Based on
SDS-PAGE gel band pattern, fractions containing purified protein were pooled and
imidazole concentration was reduced by 20-fold dilution in buffer without
imidazole followed by volume reduction with an Amicon Ultra-4 spin filter tube
(3 kDa, Merck).
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3

His-Tagged Protein Purification by FPLC

Check if the same lab product or an alternative is used in the 5 most similar protocols
Affinity purification was carried out on an ÄKTA Purifier 10 FPLC
system (GE healthcare). Cleared cell lysate (4-6 mL) was passed through a 0.22
µm PES filter (TechnoPlasticProducts) and loaded on a HisTrap™ HP
column (1 mL, Cytiva) equilibrated with 20 mM TRIS-HCl pH 7.5 containing 250 mM
NaCl and 40 mM imidazole. The column was washed with 10 column volumes of the
same buffer and bound proteins were eluted over a gradient of 10 mL to a final
concentration of 500 mM imidazole. Elution of proteins was monitored by
absorption at 215 and 280 nm and 1 mL fractions were collected. Based on
SDS-PAGE gel band pattern, fractions containing purified protein were pooled and
imidazole concentration was reduced by 20-fold dilution in buffer without
imidazole followed by volume reduction with an Amicon Ultra-4 spin filter tube
(3 kDa, Merck).
+ Open protocol
+ Expand
4

Time-lapse Imaging of Bacterial Cell Dynamics

Check if the same lab product or an alternative is used in the 5 most similar protocols
Leaf245 was grown in R-2A+M broth and the supernatant was concentrated
200-fold with an Amicon Ultra-4 spin filter tube (100 kDa, Merck). Leaf374 grown
on R-2A+M agar was resuspended in PBS pH7.4 (10 mM
Na2HPO4, 1.8 mM KH2PO4, 137 mM NaCl,
2.7 mM KCl), spotted on a LB agar pad and dried. The concentrated supernatant of
Leaf 245 was added (10 μL) and imaging was started one minute later.
Phase contrast images were acquired on a Zeiss Axio Observer Z1 inverted
microscope (Carl Zeiss AG) equipped with an EC Plan-Neofluar 100x/1.3 objective.
Images were taken every 20 seconds over the course of 20 minutes and combined to
a time lapse video using Fiji software78 (link).
+ Open protocol
+ Expand

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