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Proteomepurify 2

Manufactured by R&D Systems
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Sourced in France

ProteomePurify 2 is a laboratory instrument designed for the purification of proteins. It utilizes advanced chromatographic techniques to isolate and concentrate target proteins from complex biological samples.

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Lab products found in correlation

Vivaspin 4, by Sartorius (1 mentions) Bradford assay, by Bio-Rad (1 mentions)

4 protocols using proteomepurify 2

1

Immunodepletion of Albumin and IgG

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The two most abundant plasma proteins, albumin and IgG, were removed
from the RBC supernatants using serum protein immunodepletion resins (Proteome
Purify 2, R&D Systems, Inc., Minneapolis, MN) according to
manufacturer’s protocol. Briefly, 600 μg of RBC supernatants was
mixed with 1 mL of suspended immunodepletion resin and incubated on rotary
shaker at room temperature for 30 minutes. After the incubation period, the
immunodepletion resin was transferred into the upper chamber of a
0.22-μm filter unit (Corning Costar Spin-X, Sigma Aldrich) and
centrifuged for 2 minutes at 2000 × g. The protein
concentrations were determined by a Brad-ford protein assay before and after
removal of the top two plasma proteins.
D’Alessandro A., Dzieciatkowska M., Hill R.C, & Hansen K.C. (2016). Supernatant protein biomarkers of red blood cell storage hemolysis as determined through an absolute quantification proteomics technology. Transfusion, 56(6), 1329-1339.
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2

Serum Proteome Profiling of Exercised Mice

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Sera were collected from 3 resting or 3 exercised WT mice, and were pooled. High abundance serum proteins, albumin and IgG were removed from pooled serum samples using Proteome Purify 2 (MIDR002–020, R&D systems) according to the manufacturer’s protocol. Mass spectrometry analysis was performed in the Northwestern Proteomics Core Facility.
Kuramoto K., Liang H., Hong J.H, & He C. (2023). Exercise-activated hepatic autophagy via the FN1-α5β1 integrin pathway drives metabolic benefits of exercise. Cell metabolism, 35(4), 620-632.e5.
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3

Depletion of Albumin and IgG

Cited 1 time
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Albumin and IgG, were removed from the plasma samples using serum protein immunodepletion resins (Proteome Purify2, R&D Systems, Inc., Minneapolis, MN) as published.29 (link),30 Because of the intentional removal of albumin and immunoglobulins these proteins are obviated from further analysis.
Banerjee A., Silliman C.C., Moore E.E., Dzieciatskowa M., Kelher M., Sauaia A., Jones K., Chapman M.P., Gonzalez E., Moore H.B., D’Alessandro A., Peltz E., Huebner B.E., Einerson P., Chandler J., Ghasabayan A, & Hansen K. (2018). Systemic Hyperfibrinolysis after Trauma: A Pilot study of Targeted Proteomic Analysis of Superposed Mechanisms in Patient Plasma. The journal of trauma and acute care surgery, 84(6), 929-938.
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4

Ultrafiltration and Albumin Depletion

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Culture supernatants of day 6, 12, and 18 were pooled and three aliquots of 2 mL each were concentrated using ultrafiltration (MWCO 5 kDa, Vivaspin4; Sartorius, Dourdan, France) over 1 hr at 4000× g at 4 °C. Buffer was exchanged twice by adding 3 mL of PBS, and centrifugation, as described above. For specific depletion of albumin, 180 µg of proteins were incubated with antibody-coated sepharose beads (Proteome purify 2; R&D systems, Lille, France) for one hour at 4 °C, with subsequent filtration using the spin-filter devices contained in the kit to obtain the Albumin-depleted fraction. Bound albumin was eluted from the resin with 500 µL of 200 mM Glycine, pH 2.8 and protein concentrations were estimated before and after depletion by using a Bradford assay (Bio-Rad). A total of 45 µg of depleted sample was digested in-solution, as described for the intracellular proteome, using a trypsin-to-protein ratio of 1:90.
Tascher G., Burban A., Camus S., Plumel M., Chanon S., Le Guevel R., Shevchenko V., Van Dorsselaer A., Lefai E., Guguen-Guillouzo C, & Bertile F. (2019). In-Depth Proteome Analysis Highlights HepaRG Cells as a Versatile Cell System Surrogate for Primary Human Hepatocytes. Cells, 8(2), 192.
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