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Journal articles on the topic 'HyperCells'

Author: Grafiati
Published: 6 September 2023

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1

Learmonth, RP. "Hypercell." Biochemical Education 22, no. 2 (April 1994): 97–99. http://dx.doi.org/10.1016/0307-4412(94)90094-9.

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2

Williams, R. A. D. "HyperCell 1996." Trends in Biochemical Sciences 22, no. 4 (April 1997): 141. http://dx.doi.org/10.1016/s0968-0004(97)84079-0.

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3

LEVENSON, THOMAS. "Taming the Hypercello." Sciences 34, no. 4 (July 8, 1994): 15–17. http://dx.doi.org/10.1002/j.2326-1951.1994.tb03769.x.

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4

Gleiser, P. M., and F. A. Tamarit. "Dynamical properties of the hypercell spin-glass model." Physical Review E 57, no. 2 (February 1, 1998): 1410–15. http://dx.doi.org/10.1103/physreve.57.1410.

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5

Sansom, Clare. "HyperCELL 1996 — CD-ROM for MacIntosh and Windows." Biochemical Education 25, no. 2 (April 1997): 100. http://dx.doi.org/10.1016/s0307-4412(97)88292-1.

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6

Yu, Tian, Jonathan Hull, Andrea Ruiz, Ashwini Bhat, and Amar Basu. "Expediting antibody discovery using Bioelectronica’s HypercellTM platform." Journal of Immunology 204, no. 1_Supplement (May 1, 2020): 86.36. http://dx.doi.org/10.4049/jimmunol.204.supp.86.36.

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Abstract Antibody-based drugs have been successful in a range of therapeutic categories. However, generating monoclonal antibodies is time-consuming and expensive. A common approach is Hybridoma technology, which overcomes the short life-span of IgG-secreting plasma B cells in vitro. However, many plasma B cells are lost due to the low efficiency of hybridoma cell fusion (typically <10%). Direct single B cell screening strategies have emerged to bypass hybridoma fusion and recombinatorial display, coupled with the generation of recombinant monoclonal antibodies through mammalian expression systems. Obtaining expression systems with the required productivity, specificity and stability for clinical or commercial use requires screening millions of cells and thousands of clones. Bioelectronica’s HypercellTM platform is an emerging technology used throughout antibody discovery and cell-line development to identify and isolate single, high-antibody secreting cells from large pools (~10,000,000 cells) in short periods (ca. 48 hrs). This scalable “electrofluidic” sorting system reduces time and cost by integrating antigen-detection reagents and real-time computer vision analysis to expedite single cell sorting. In this paper antigen-specific IgG-secreting hybridoma cells are identified and sorted by their secretion rate. The cells and reagents are encapsulated in a Polydisperse Oblate Dispersion system (PODs), incubated for 1–4 hours for signal gain, and loaded into the HypercellTM device for cell sorting. Alternatively, the mixture can be analyzed without sorting to produce single cell secretion “finger print” signatures that can help identify unique expression patterns and monitor cell line stability over culturing time.
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7

Arakawa, Tsutomu, Mutsumi Futatsumori-Sugai, Kouhei Tsumoto, Yoshiko Kita, Haruna Sato, and Daisuke Ejima. "MEP HyperCel chromatography II: Binding, washing and elution." Protein Expression and Purification 71, no. 2 (June 2010): 168–73. http://dx.doi.org/10.1016/j.pep.2009.11.004.

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8

McCann, Karl B., Yvonne Vucica, John Wu, and Joseph Bertolini. "Use of mep HyperCel for polishing of human serum albumin." Journal of Chromatography B 969 (October 2014): 241–48. http://dx.doi.org/10.1016/j.jchromb.2014.08.029.

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9

Elsamanoudi, Ahmed, Mohamed R. AbdAllah, and Haytham M. Elbadrawy. "Parametric Hypercell Mechanism for Adaptive Building Skin: A Case Study in New Administrative Capital, Egypt." Civil Engineering and Architecture 10, no. 7 (December 2022): 3046–70. http://dx.doi.org/10.13189/cea.2022.100719.

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10

Arakawa, Tsutomu, Masao Tokunaga, Takuya Maruyama, and Kentaro Shiraki. "Two Elution Mechanisms of MEP Chromatography." Current Protein & Peptide Science 20, no. 1 (November 9, 2018): 28–33. http://dx.doi.org/10.2174/1389203718666171117105132.

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MEP (mercapto-ethyl-pyridine) HyperCel is one of the hydrophobic charge induction chromatography (HCIC) resins. Under normal operation, proteins are bound to the MEP resin at neutral pH, at which MEP is not charged, mostly via hydrophobic interaction. MEP has a pyridine group, whose pK is 4.8, and hence is positively charged at acidic pH range. Based on the binding mechanism (i.e., hydrophobic interaction) and the induced positive charge at acidic pH, there may be two ways to elute the bound proteins. One way is to bring the pH down to protonate both MEP resin and the bound protein, leading to charge repulsion and thereby elution. Another way is to use hydrophobic interaction modifiers, which are often used in hydrophobic interaction chromatography, to reduce hydrophobic interaction. Here, we summarize such two possible elution approaches.
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11

Thangavel, C., R. Bhagwat, H. Li, and L. Bradbury. "High-Throughput Purification of Polyhistidine Tagged Proteins in AcroPrepTM Multi-well Filter Plates Using IMAC HyperCelTM." Journal of Proteomics & Bioinformatics S2, no. 01 (July 2008): 224. http://dx.doi.org/10.4172/jpb.s1000163.

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12

Pezzini, J., C. Cabanne, R. Gantier, V. N. Janakiraman, and X. Santarelli. "A comprehensive evaluation of mixed mode interactions of HEA and PPA HyperCel™ chromatographic media." Journal of Chromatography B 976-977 (January 2015): 68–77. http://dx.doi.org/10.1016/j.jchromb.2014.11.020.

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13

G., Arun Govind, Agamudi Shivasankaran Kamalanathan, Mookambeswaran Arunachalam Vijayalakshmi, and Krishnan Venkataraman. "Efficient purification of Apolipoprotein A1 (ApoA1) from plasma by HEA HyperCel™: An alternative approach." Journal of Chromatography B 1073 (January 2018): 104–9. http://dx.doi.org/10.1016/j.jchromb.2017.12.016.

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14

Pezzini, J., C. Cabanne, J. W. Dupuy, R. Gantier, and X. Santarelli. "A study on the nature of interactions of mixed-mode ligands HEA and PPA HyperCel using phenylglyoxal modified lysozyme." Journal of Chromatography B 960 (June 2014): 209–13. http://dx.doi.org/10.1016/j.jchromb.2014.04.046.

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15

Ravichandran, R., Venkatesh Padmanabhan, M. A. Vijayalakhsmi, and N. S. Jayaprakash. "Studies on recovery of lactoferrin from bovine colostrum whey using mercapto ethyl pyridine and phenyl propyl amine HyperCel™ mixed mode sorbents." Biotechnology and Bioprocess Engineering 20, no. 1 (February 2015): 148–56. http://dx.doi.org/10.1007/s12257-014-0408-7.

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16

"Teaching cell biology with hypercell." Biochemical Education 22, no. 2 (April 1994): 96. http://dx.doi.org/10.1016/0307-4412(94)90092-2.

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17

Wrzosek, Katarzyna, Michal Gramblička, Darina Tóthová, Monika Antošová, and Milan Polakovič. "Impact of ionic strength on adsorption capacity of chromatographic particles employed in separation of monoclonal antibodies." Chemical Papers 64, no. 4 (January 1, 2010). http://dx.doi.org/10.2478/s11696-010-0019-5.

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AbstractThe influence of ionic strength on the adsorption capacity of seven commercial adsorbents used in downstream processing of monoclonal antibodies was examined. Affinity (MabSelect, Poros 50A High Capacity, ProSep-vA High Capacity), hydrophobic charge-induction (MEP HyperCel), and cation exchange adsorbents (FractoGel EMD SE Hicap (M), SP Sepharose Fast Flow, Ceramic HyperD F) were used to study the adsorption of polyclonal human immunoglobulin G at optimal pH values. The ionic strength, adjusted by sodium chloride concentrations in the range of 0–225 mM, strongly decreased the adsorption capacity of the cation exchangers. Equilibrium data were described in the form of the dependence of the ratio of protein concentrations in the solid and liquid phases on the total concentration of cation counter ions. They were successfully fitted and interpreted through a stoichiometric ion-exchange model.
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