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Cobalt talon resin

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Cobalt-TALON resin is a high-performance affinity chromatography resin designed for the purification of polyhistidine-tagged proteins. It utilizes cobalt ions immobilized on a resin matrix to selectively bind and capture target proteins containing polyhistidine tags. The resin provides efficient protein capture and easy on-column elution, making it a useful tool for researchers and scientists working with recombinant proteins.

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Lab products found in correlation

Superdex 200 increase, by GE Healthcare (4 mentions) Cobalt talon resin, by Takara Bio (4 mentions) Hrv 3c protease, by Thermo Fisher Scientific (3 mentions) Freestyle 293 f cells, by Thermo Fisher Scientific (1 mentions) Superose 6 increase 10 300 column, by GE Healthcare (1 mentions)

4 protocols using cobalt talon resin

1

Recombinant Influenza Hemagglutinin Expression

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rHA “head” and rHA full length soluble ectodomains (FLsE) constructs were cloned into pFastBac vector for insect cell expression (Hi5 cells) or pVRC vector for mammalian expression (293F or 293S cells). All constructs were confirmed by DNA sequencing at the DNA Sequencing Core Facility at Dana Farber Cancer Institute. For biolayer interferometry (BLI) and crystallography the HA1 head constructs contained a HRV 3C-cleavable C-terminal His6X tag or SBP-His8Xtag. The HA FLsE constructs used in ELISA assays contained a thrombin or HRV 3C-cleavable C-terminal foldon tag with either a His6X or SBP-His8Xtag. All constructs were purified from supernatants by passage over Cobalt-TALON resin (Takara) followed by gel filtration chromatography on Superdex 200 Increase (GE Healthcare) in 10 mM Tris-HCl, 150 mM NaCl at pH 7.5. Affinity tags were removed using HRV 3C protease (ThermoScientific) and the protein repurified using Cobalt-TALON resin to remove the protease, tag and non-cleaved protein.
Bajic G., Maron M.J., Adachi Y., Onodera T., McCarthy K.R., McGee C.E., Sempowski G.D., Takahashi Y., Kelsoe G., Kuraoka M, & Schmidt A.G. (2019). Influenza antigen engineering focuses immune responses to a subdominant but broadly protective viral epitope. Cell host & microbe, 25(6), 827-835.e6.
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2

SARS-CoV-2 RBD Recombinant Protein

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SARS-2 RBD (GenBank; MN975262.1) was cloned into pVRC vector for mammalian expression (FreeStyle 293F or Expi293F suspension cells). The construct contains a human rhinovirus 3C-cleavable carboxy (C)-terminal streptavidin-binding peptide-His8× tag. Supernatants were harvested 5 d post-transfection and passaged directly over Cobalt-TALON resin (Takara) followed by size exclusion chromatography on Superdex 200 Increase (GE Healthcare) in 1× phosphate-buffered saline. Typical yields from FreeStyle 293F cells are approximately 9 mg l−1 culture. Affinity tags were removed using human rhinovirus 3 C protease (Thermo Fisher Scientific) and the protein was repurified using Cobalt-TALON resin to remove the protease, tag and non-cleaved protein. RBD sequence and purification validation are provided in Supplementary Fig. 1.
Norman M., Gilboa T., Ogata A.F., Maley A.M., Cohen L., Busch E.L., Lazarovits R., Mao C.P., Cai Y., Zhang J., Feldman J.E., Hauser B.M., Caradonna T.M., Chen B., Schmidt A.G., Alter G., Charles R.C., Ryan E.T, & Walt D.R. (2020). Ultrasensitive high-resolution profiling of early seroconversion in patients with COVID-19. Nature Biomedical Engineering, 4(12), 1180-1187.
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3

Production and Purification of SARS-CoV-2 Spike Proteins

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The SARS-CoV-2 ectodomain constructs were produced and purified as described previously (Wrapp et al., 2020b (link)). Plasmids encoding Spike-2P and HexaPro (Hsieh et al., 2020 (link)) were transiently transfected in FreeStyle 293F cells (Thermo Fisher) using Turbo293 (SpeedBiosystems). The cultures were collected on Day 6 post transfection. The cells were separated from the medium by centrifugation. Protein were purified from filtered cell supernatants by StrepTactin resin (IBA) and additionally by size exclusive chromatography using Superose 6 10/300 increase column (GE Healthcare) in 2mM Tris pH 8, 200mM NaCl, 0.02% NaN3. SARS-CoV-2 NTD was produced as previously described (Zhou et al., 2020b (link)). SARS-CoV RBD and MERS-CoV Spike RBD were cloned into pVRC8400 vector for mammalian expression (FreeStyle 293F or Expi293F suspension cells). The construct contains an HRV 3C-cleavable C-terminal SBP-8xHis tag. Supernatants were harvested 5 days post-transfection and passaged directly over Cobalt-TALON resin (Takara) followed by size exclusion chromatography on Superdex 200 Increase (GE Healthcare) in 1x PBS. Typical yields from FreeStyle 293F cells are approximately 50 mg/liter culture. Affinity tags can be removed using HRV 3C protease (ThermoScientific) and the protein repurified using Cobalt-TALON resin to remove the protease, tag and non-cleaved protein.
Li D., Edwards R.J., Manne K., Martinez D.R., Schäfer A., Alam S.M., Wiehe K., Lu X., Parks R., Sutherland L.L., Oguin TH I.I.I., McDanal C., Perez L.G., Mansouri K., Gobeil S.M., Janowska K., Stalls V., Kopp M., Cai F., Lee E., Foulger A., Hernandez G.E., Sanzone A., Tilahun K., Jiang C., Tse L.V., Bock K.W., Minai M., Nagata B.M., Cronin K., Gee-Lai V., Deyton M., Barr M., Von Holle T., Macintyre A.N., Stover E., Feldman J., Hauser B.M., Caradonna T.M., Scobey T.D., Rountree W., Wang Y., Moody M.A., Cain D.W., DeMarco C.T., Denny T.N., Woods C.W., Petzold E.W., Schmidt A.G., Teng I.T., Zhou T., Kwong P.D., Mascola J.R., Graham B.S., Moore I.N., Seder R., Andersen H., Lewis M.G., Montefiori D.C., Sempowski G.D., Baric R.S., Acharya P., Haynes B.F, & Saunders K.O. (2021). In vitro and in vivo functions of SARS-CoV-2 infection-enhancing and neutralizing antibodies. Cell, 184(16), 4203-4219.e32.
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4

Recombinant Influenza Hemagglutinin Constructs

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rHA1 “head” and rHA full length soluble ectodomains (FLsE) constructs were cloned into pFastBac vector for insect cell expression (Hi5 cells) or pVRC vector for mammalian expression (HEK293F cells). HAs were derived from the following templates: A/America black duck/New Brunswick/00464/2010 (H4N6) (GenBank: AGG81749.1) and A/mallard/Wisconsin/10OS3941/2010 (H14N6) (GenBank: AGE03043) (Table S3). All constructs were confirmed by DNA sequencing at the DNA Sequencing Core Facility at Dana Farber Cancer Institute. For biolayer interferometry (BLI) and crystallography the HA1 head constructs contained an HRV 3C-cleavable C-terminal His6X tag or SBP-His8Xtag. The HA FLsE constructs used in ELISA assays contained a thrombin or HRV 3C-cleavable C-terminal foldon tag with either a His6X or SBP-His8Xtag. All constructs were purified from supernatants by passage over Cobalt-TALON resin (Takara) followed by gel filtration chromatography on Superdex 200 Increase (GE Healthcare) in 10 mM Tris-HCl, 150 mM NaCl at pH 7.5. For BLI and crystallography the tags were removed using HRV 3C protease (ThermoScientific) and the protein repurified using Cobalt-TALON resin to remove the protease, tag and non-cleaved protein.
Bajic G., Maron M.J., Caradonna T.M., Tian M., Mermelstein A., Fera D., Kelsoe G., Kuraoka M, & Schmidt A.G. (2020). Structure-guided molecular grafting of a complex broadly neutralizing viral epitope. ACS infectious diseases, 6(5), 1182-1191.
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