Hitrap deae sepharose ff

Manufactured by GE Healthcare

HiTrap DEAE Sepharose FF is a pre-packed, ready-to-use column for ion exchange chromatography. It is designed for fast and easy purification of biomolecules, such as proteins and enzymes, from complex mixtures. The column contains DEAE (diethylaminoethyl) Sepharose, a strong anion exchange medium, which enables the efficient capture and separation of negatively charged molecules.

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Lab products found in correlation

Hitrap, by Cytiva (1 mentions) Q5 site directed mutagenesis kit, by New England Biolabs (1 mentions) T7 rna polymerase, by Thermo Fisher Scientific (1 mentions)

Spelling variants of this product

DEAE-Sepharose (35 citations) HiTrap DEAE FF (17 citations) DEAE-Sepharose FF (10 citations) HiTrap DEAE (5 citations) HiTrap DEAE Sepharose (3 citations)

3 protocols using hitrap deae sepharose ff

Purification of Recombinant Equ c 1 Allergen

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Example 3

Recombinant Equ c 1 wt and the mutants were purified with a three-step chromatography procedure. The first step was an anion-exchange chromatography by a HiTrap DEAE Sepharose FF (GE Healthcare 17-5154-01) column, the second step a cationic-exchange chromatography by a HiTrap CM Sepharose FF (GE Healthcare 17-5056-01) column and the third step a size-exclusion chromatography (SEC) by a Tricorn™ Superdex™ 16/600 column (GE Healthcare). Fractions from the SEC column elution peak were analysed by a 18% Coomassie Brilliant-Blue stained SDS-PAGE showing that they were pure and homogeneous (data not shown). Elution peak fractions were pooled and concentration of the purified rEqu c 1 allergen determined by measuring A₂₈₀.

US11679152B2. Recombinant hypoallergenic Equ c 1 polypeptides for use in the immunotherapy of horse allergy (2023-06-20). Desentum Oy [FI]. Inventors: Juha Rouvinen [FI], Kristiina Takkinen [FI], Marja-Leena Laukkanen [FI], Merja Niemi [FI], Janne Jänis [FI], Jaana Haka [FI].

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Engineered S. cerevisiae Mtr4 Purification

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The S. cerevisiae Mtr4^ΔF was constructed by removing residues 667–813 and inserting a three-glycine linker using the Q5 Site-Directed Mutagenesis Kit (NEB). All Mtr4 proteins were recombinantly expressed in Escherichia coli BL21-CodonPlus (DE3)-RIPL (Stratagene) using an autoinduction protocol (24 ). The purification of Mtr4 was carried out as previously described with the addition of a HiTrap DEAE Sepharose FF (GE) before gel filtration (25 (link)). RNase contamination was monitored with an RNaseAlert® kit (IDT) following heparin chromatography and at each subsequent chromatography step. Only RNase-free fractions were retained. Purified Mtr4 with 30% (v/v) glycerol was flash frozen in liquid nitrogen for storage.

Zhang N., Olsen K.J., Ball D., Johnson S.J, & D’Arcy S. (2022). Hydrogen-deuterium exchange mass spectrometry of Mtr4 with diverse RNAs reveals substrate-dependent dynamics and interfaces in the arch. Nucleic Acids Research, 50(7), 4042-4053.

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In vitro Transcription and Purification of tRNA i Met

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tRNA_i^Met is similar to the native tRNA_i^Met sequence from S. cerevisiae with a CCA cap and poly(A) sequence on the 3′ end. The sequence also includes non-native 5′ and 3′ cloning artifacts. The tRNA_i^Met was generated using in vitro transcription with T7 RNA polymerase (ThermoFisher Scientific) on a plasmid linearized after the tRNA_i^Met sequence. The tRNA_i^Met was purified under non-denaturing conditions as previously described (26 (link)). Briefly, the transcription reaction was loaded onto HiTrap DEAE Sepharose FF (GE) and the tRNA_i^Met eluted off using a NaCl gradient. All other RNAs were synthesized commercially (Integrated DNA Technologies, Inc.).

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