Ultra centrifugal filter unit

Manufactured by Merck Group

Sourced in United States

The Ultra-centrifugal filter unit is a laboratory device used for the separation and concentration of macromolecules, such as proteins, nucleic acids, and other biomolecules, from complex solutions. The device utilizes centrifugal force to drive the sample through a semi-permeable membrane, allowing the desired molecules to be retained while smaller components pass through.

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Lab products found in correlation

Food scan lab 78810, by Foss (1 mentions) Tecnai 12 spirit g2 biotwin transmission electron microscope, by Thermo Fisher Scientific (1 mentions) Sw32ti rotor, by Beckman Coulter (1 mentions) Carbon coated copper grid, by Electron Microscopy Sciences (1 mentions)

5 protocols using ultra centrifugal filter unit

Meat Water Holding Capacity Measurement

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The WHC of each meat sample was measured in duplicate using the procedure as described by Hoa et al. [15 (link)]. Briefly, after grinding using a mini grinder (Hanil Co., Chungcheongnam-do, Korea), an aliquot (0.5 g) of meat was taken and placed in a 2 mL ultra-centrifugal filter unit, which was then inserted into an ultra-centrifugal filter device (Millipore Corp., Bedford, MA, USA). After heating for 20 min at 80 °C in a water bath, the samples were cooled at 4 °C for 10 min and then centrifuged at 2000× g for 10 min. The initial weight of the ultracentrifugal filter unit before cooking and its weight with the cooked sample were recorded to determine the water loss. Also, the total moisture and fat contents in each fresh meat sample, determined by using a Food Scan Lab 78810 (Foss Tecator Co., Ltd., Hillerod, Denmark), were used to determine its WHC. Finally, the WHC was calculated using the equation developed by Laakkonen et al. [16 (link)] as follows:

WHC = \frac{Total moisture content (%) - Moisture loss {(%)}^{1)}}{Total moisture content} \times 100

^{1)} Moisture loss (%) = \frac{W 1 - W 2}{S \times {FF}^{2)}} \times 100

^{2)} FF = 1 - \frac{Total fat content}{10}

W1: Weight of sample and centrifugal filter unit before heating. W2: Weight of sample and centrifugal filter unit after heating and centrifuging. S: Sample weight. ²⁾ FF: Fat factor; 1: Constant.

Hoa V.B., Song D.H., Seol K.H., Kang S.M., Kim H.W., Bae I.S., Kim E.S., Park Y.S, & Cho S.H. (2023). A Comparative Study on the Meat Quality, Taste and Aroma Related Compounds between Korean Hanwoo and Chikso Cattle. Foods, 12(4), 805.

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Measuring Water Holding Capacity in Muscle

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The WHC of the muscle samples was measured following the procedure as described in our previous study [21 (link)] and by Han et al [22 (link)] with minor modifications. Briefly, after chopping and grinding using a mini grinder, approximately 0.51 g of each sample was taken and placed in a 2 mL ultra-centrifugal filter unit, inserted into an ultra-centrifugal filter device (Millipore Corp., Bedford, MA, USA), and then heated in an 80°C pre-heated water bath for 20 min. The heated samples were cooled at room temperature for 10 min and then centrifuged at 2,000×g for 10 min at 4°C. After centrifugation, the weight of ultra-centrifugal filter unit containing the cooked sample was recorded to determine the water loss. Each sample was analyzed in duplicates and the WHC percentage was calculated as a ratio of moisture to the water loss.

Hoa V.B., Seong P.N., Cho S.H., Kang S.M., Kim Y.S., Moon S.S., Choi Y.M., Kim J.H, & Seol K.H. (2019). Quality characteristics and flavor compounds of pork meat as a function of carcass quality grade. Asian-Australasian Journal of Animal Sciences, 32(9), 1448-1457.

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Recombinant ALKBH5 Protein Purification

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Human ALKBH5 CDS region was subcloned into pET28a. The plasmid was transformed into BL21 (DE3) competent E. coli cells. Expression of ALKBH5 protein was induced by 0.1 mM IPTG at 16°C for 16 h. Purification of recombinant ALKBH5 was performed as follows. Briefly, E.coli cell pellet containing ALKBH5 was lysed in cell lysis buffer (500 mM NaCl, 50 mM Tris, pH 7.4, 20 mM imidazole). Clear cell lysate containing soluble proteins was loaded to Ni-NTA agarose beads and eluted by washing buffer (500 mM NaCl, 50 mM Tris, pH 7.4, 300 mM imidazole). Eluted proteins were concentrated by Ultra Centrifugal Filter Unit (Millipore) and applied to size exclusion chromatography. Purified ALKBH5 protein was further concentrated and was qualified by SDS-PAGE electrophoresis.

Li J., Zhou J., Xia Y., Rui Y., Yang X., Xie G., Jiang G, & Wang H. (2023). Rolling circle extension-assisted loop-mediated isothermal amplification (Rol-LAMP) method for locus-specific and visible detection of RNA N6-methyladenosine. Nucleic Acids Research, 51(9), e51.

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Serum-free Conditioned Media Concentration

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LL/2 cells were plated in 10 cm dishes at a concentration of 10 × 10⁵ cells/mL in serum‐free DMEM for 24 h. Conditioned media (CM) was concentrated using a 10 kDa cut‐off Ultra Centrifugal Filter Unit (Millipore Sigma, Burlington, MA).

Widner D.B., Liu C., Zhao Q., Sharp S., Eber M.R., Park S.H., Files D.C, & Shiozawa Y. (2021). Activated mast cells in skeletal muscle can be a potential mediator for cancer‐associated cachexia. Journal of Cachexia, Sarcopenia and Muscle, 12(4), 1079-1097.

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Concentrating ZIKV and VLPs for Electron Microscopy

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Samples were concentrated in preparation for electron microscopy. A virus stock of ZIKV PRVABC59 was concentrated using an ultra-centrifugal filter unit (MilliporeSigma, Burlington, MA, USA) with a 100 kDa cutoff. To concentrate VLPs produced by vIND-ZIKV (D4W), Vero cells grown in T-175 culture flasks to near confluency were infected at an MOI of 5. After 1 h, cells were washed and overlaid with D-MEM supplemented with 2.5% FBS. After cells were incubated for 2 days at 37 °C, the supernatant was clarified by centrifugation at 500

\times

g for 10 min at 4 °C, transferred (~ 24 ml) to a conical tube containing 6 ml cold 40% PEG-8000, and incubated overnight at 4 °C. The supernatant/PEG mixture was loaded onto a SW 32 Ti Rotor (Beckman Coulter) and centrifuged at 9100 rpm for 30 min at 4 °C. The pellet was resuspended in 200 µl 10 mM Tris (pH 8.0) buffer. Concentrated ZIKV and VLPs were fixed in 2% glutaraldehyde for 15 min. Fixed samples (3 µl) were then deposited onto plasma-cleaned carbon-coated copper grids (Electron Microscopy Sciences, Hatfield, PA, USA) and incubated for 2 min. The grids were then washed with 0.5% uranyl acetate and air dried. Grids were imaged with a FEI Tecnai 12 G2 Spirit BioTWIN transmission electron microscope at the University of Connecticut Biosciences Electron Microscopy Laboratory.

Jasperse B., O’Connell C.M., Wang Y, & Verardi P.H. (2021). Single dose of a replication-defective vaccinia virus expressing Zika virus-like particles is protective in mice. Scientific Reports, 11, 6492.

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