Hiprep heparin

Manufactured by GE Healthcare

The HiPrep Heparin is a lab equipment product used for the purification and separation of biomolecules. It is a resin-based chromatography column that utilizes heparin as the ligand, enabling the capture and separation of various proteins, enzymes, and other biomolecules based on their affinity for heparin.

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Lab products found in correlation

Ni nta agarose, by Qiagen (2 mentions) Superdex 200, by GE Healthcare (2 mentions) Hiprep, by Cytiva (2 mentions)

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Heparin (8 citations)

2 protocols using hiprep heparin

Purification of S. aureus RNAP Holoenzyme

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S. aureus RNAP core enzyme was prepared from E. coli strain BL21(DE3) (Invitrogen/ThermoFisher) transformed with plasmids pCOLADuet-Sau-BC, pACYCDuet-Sau-H10-A, and pCDFDuet-Sau-Z, using polyethylenimine precipitation, ammonium sulfate precipitation, immobilized-metal-ion affinity chromatography on Ni-NTA agarose (Qiagen), and cation-exchange chromatography on HiPrep Heparin (GE Healthcare); S. aureus σ^A was prepared from E. coli strain BL21(DE3) transformed with pET21a-Sau-H6-sigA, using immobilized-metal-ion affinity chromatography on Ni-NTA agarose (Qiagen) and gel-filtration chromatography on Superdex 200 (GE Healthcare); and S. aureus RNAP core enzyme and S. aureus σ^A were combined to yield S. aureus RNAP σ^A holoenzyme, as in Srivastava et al., 2011 (link).

Maffioli S.I., Zhang Y., Degen D., Carzaniga T., Gatto G.D., Serina S., Monciardini P., Mazzetti C., Guglierame P., Candiani G., Chiriac A.I., Facchetti G., Kaltofen P., Sahl H.G., Dehò G., Donadio S, & Ebright R.H. (2017). Antibacterial nucleoside-analog inhibitor of bacterial RNA polymerase. Cell, 169(7), 1240-1248.e23.

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Purification of S. aureus RNAP Holoenzyme

Cited 1 time

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S. aureus RNAP core enzyme was prepared by co-expression of genes for S. aureus RNAP β' subunit, RNAP β subunit, N-terminally decahistidine-tagged RNAP α subunit, and RNAP ω subunit in E. coli, followed by cell lysis, polyethylenimine precipitation, ammonium sulfate precipitation, immobilized-metal-ion affinity chromatography on Ni-NTA agarose (Qiagen), and cation-exchange chromatography on HiPrep Heparin (GE Healthcare), as in Maffioli et al., 2017 (link).
S. aureus σ^A was prepared by expression of a gene for N-terminally hexahistidine-tagged S. aureus σ^A in E. coli, followed by cell lysis, immobilized-metal-ion affinity chromatography on Ni-NTA agarose (Qiagen), and gel-filtration chromatography on Superdex 200 (GE Healthcare), as in Maffioli et al., 2017 (link). S. aureus RNAP σ^A holoenzyme was prepared by combination of S. aureus RNAP core enzyme and S. aureus σ^A, as in Maffioli et al., 2017 (link).

Lin W., Das K., Degen D., Mazumder A., Duchi D., Wang D., Ebright Y.W., Ebright R.Y., Sineva E., Gigliotti M., Srivastava A., Mandal S., Jiang Y., Liu Y., Yin R., Zhang Z., Eng E.T., Thomas D., Donadio S., Zhang H., Zhang C., Kapanidis A.N, & Ebright R.H. (2018). STRUCTURAL BASIS OF TRANSCRIPTION INHIBITION BY FIDAXOMICIN (LIPIARMYCIN A3). Molecular cell, 70(1), 60-71.e15.

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