Hitrap sp sepharose ff

Manufactured by GE Healthcare

Sourced in United Kingdom

HiTrap SP Sepharose FF is a strong cation exchange chromatography medium designed for the purification of proteins, peptides, and other biomolecules. It consists of highly cross-linked agarose beads with covalently coupled sulfopropyl (SP) functional groups. The medium provides high-resolution separation and excellent recovery of target molecules.

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Lab products found in correlation

6530 accurate mass q tof lc ms, by Agilent Technologies (1 mentions) Kta pure system, by GE Healthcare (1 mentions) Microflex lrf instrument, by Bruker (1 mentions) Viia7, by Thermo Fisher Scientific (1 mentions) Hitrap sp hp, by GE Healthcare (1 mentions) Nanovue plus spectrophotometer, by GE Healthcare (1 mentions) Viia 7 real time pcr system, by Thermo Fisher Scientific (1 mentions)

Close spelling variants of this product

HiTrap SP Sepharose FF 5 ml HiTrap SP Sepharose FF column HiTrap SP FF SP Sepharose FF Sepharose SP (HiTrap, HiTrap SP SP Sepharose

2 protocols using hitrap sp sepharose ff

Isotopic Labeling of Tau Proteins

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Isotopic labelling of Tau and Tau-F5 was performed by growing recombinant BL21 (DE3) in minimal growth medium supplemented with ¹⁵N NH₄Cl. The first purification step was performed by heating the bacterial protein extract for 15 min at 75 °C. The ¹⁵N Tau protein and ¹⁵N Tau[165–245] were recovered in the soluble fraction after centrifugation at 15,000 g for 30 min. The ¹⁵N Tau protein and ¹⁵N Tau-F5 were purified by cation exchange chromatography in 50 mM phosphate buffer pH 6.3, 1 mM EDTA (5 ml Hitrap SP Sepharose FF, General Electric Healthcare, Little Chalfont, United Kingdom). The pooled fractions from the chromatography purification step were transferred to ammonium bicarbonate by desalting on a 15/60 Hiprep desalting column (G25 resin, General Electric Healthcare) and lyophilized. The His-SH3 protein was purified on Ni-NTA resin, according to the manufacturer’s protocol.

Sottejeau Y., Bretteville A., Cantrelle F.X., Malmanche N., Demiaute F., Mendes T., Delay C., Alves Dos Alves H., Flaig A., Davies P., Dourlen P., Dermaut B., Laporte J., Amouyel P., Lippens G., Chapuis J., Landrieu I, & Lambert J.C. (2015). Tau phosphorylation regulates the interaction between BIN1’s SH3 domain and Tau’s proline-rich domain. Acta Neuropathologica Communications, 3, 58.

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Protein Purification and Characterization

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Chromatography was conducted using an ÄKTA Pure system from GE Healthcare Life Sciences (Piscataway, NJ), and the results were analyzed with the UNICORN Control System. HiTrap SP HP, HiTrap SP Sepharose FF, HiTrap ConA 4B, and HiLoad^® 26/600 Superdex^® 75 pg columns for protein purification were from GE Healthcare Life Sciences.
Protein concentrations were determined with a NanoVue Plus spectrophotometer from GE Healthcare Life Sciences by absorbance at 280 nm using Beer’s law, ε = 0.53 mL·mg^–1·cm^–1, and the molecular mass of the unglycosylated protein.
Differential scanning fluorimetry (DSF),^{39 (link)} which requires the monitoring of fluorescence during thermal denaturation, was performed with a ViiA 7 Real-Time PCR system from Applied Biosystems (Foster City, CA). Denaturation data were obtained with ViiA 7 version 2.0 software and analyzed further with Protein Thermal Shift version 1.4 software, both from Applied Biosystems.
The intact molecular mass of RNase 1 glycoforms was determined by MALDI–TOF mass spectrometry using a microflex LRF instrument from Bruker (Billerica, MA) and by ESI mass spectrometry using a 6530 Accurate-Mass Q-TOF LC/MS from Agilent (Santa Clara, CA).

Ressler V.T, & Raines R.T. (2019). Consequences of the Endogenous N-Glycosylation of Human Ribonuclease 1. Biochemistry, 58(7), 987-996.

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