Sf9 insect cells

Name: Sf9 insect cells
Brand: Expression Systems
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Sf9 insect cells are a commonly used cell line derived from the fall armyworm, Spodoptera frugiperda. They are a versatile tool for the expression of recombinant proteins in a eukaryotic system. Sf9 cells are known for their high growth rate and ability to perform post-translational modifications, making them a suitable choice for the production of complex proteins.

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Sf9 insect cells are commercially available from Expression Systems and can be purchased through authorized distributors. A price range of $249.00 to $558.00 is typical for these cells.

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72 protocols using «sf9 insect cells»

Recombinant Human Copper Transporter 1 Expression

2025

The expression of hCtr1 was described in detail in our previous publications [3 (link),22 (link)]. In short, wild-type (WT) hCtr1 was generated by PCR amplification and inserted into a modified pFastBac (pK503-9) vector with an N-terminal FLAG tag. To produce baculovirus for hCtr1 expression, recombinant bacmid DNA was extracted and transfected into Sf9 insect cells (Expression Systems, LLC, Davis, CA, USA) using Cellfectin II Reagent (Thermo Fisher, Airport City, IL, USA), following the Bac-to-Bac instruction manual (Thermo Fisher, Airport City, IL, USA). The cells were cultured at 27 °C for three days and then harvested and re-suspended in a buffer containing 400 mM NaCl, 10% glycerol, and 20 mM HEPES (Sigma-Aldrich, Rehovot, IL, USA) at pH 7.4. After lysis, the resulting pellet was re-suspended in a buffer containing 1.5% Triton X-100, 200 mM NaCl, 10% glycerol, and 20 mM HEPES (pH 7.4) and incubated overnight at 4 °C. After incubation, the suspension was centrifuged again at 40,000 rpm for 40 min. The supernatant was supplemented with 3 mM CaCl₂ and loaded onto an anti-FLAG M1 agarose affinity gel column (Sigma-Aldrich, Rehovot, IL, USA) overnight at 4 °C, pre-equilibrated with TBS buffer (150 mM NaCl, 50 mM Tris-HCl, pH 7.4). Finally, the column was washed with TBS buffer and eluted with a buffer containing 5 mM EDTA.
To prepare the Cu(II)-NTA solution, 10 mM Cu(II) was combined with 10 mM NTA and mixed overnight. Subsequently, 240 µM Cu(II)-NTA was added to 120 µM purified hCtr1 solution and incubated overnight at 4 °C.
The addition of Cu(I) was performed as follows: concentrated Cu(I) solution (30 mM) was first prepared using Tetrakis(acetonitrile)copper(I) hexafluorophosphate (Sigma-Aldrich, Rehovot, IL, USA) dissolved in dry acetonitrile (HPLC grade) under anaerobic conditions. The Cu(I) solution was then added at different volumes to 120 µM hCtr1 monomer to give 1:1 Cu(I):hCtr1, 3:1 Cu(I):hCtr1, 5:1 Cu(I):hCtr1 ratios. Twenty percent glycerol was added to all samples.

Peleg S., Meron S., Shenberger Y., Hofmann L., Gevorkyan-Airapetov L, & Ruthstein S. (2025). Exploring the Gating Mechanism of the Human Copper Transporter, hCtr1, Using EPR Spectroscopy. Biomolecules, 15(1), 127.

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GTPγS Binding Assay for FPR2

2024

The GTPγS binding assay was conducted using cell membranes overexpressing FPR2 and purified G_i heterotrimer, following our previously reported method (47 (link)). Briefly, Sf9 insect cells (ExpressionSystems) were infected with baculovirus expressing FPR2. The cells were collected by centrifugation at 8000 g for 10 min after 48 h. For ³⁵S-GTPγS binding analysis, ∼200 μg/ml of human FPR2 cell membrane was incubated with 200 nM purified G_i protein for 20 min on ice in buffer containing 20 mM HEPES, pH 7.5, 150 mM NaCl, 5 mM MgCl₂, 3 μg/ml BSA, 0.1 μM TCEP, and 5 μM GDP. Next, 25 μl FPR2-G_i mix was transferred to 225 μl reaction buffer containing 20 mM HEPES, pH 7.5, 150 mM NaCl, 5 mM MgCl₂, 3 μg/ml BSA, 0.1 μM TCEP, 1 μM GDP, 35 pM ³⁵S-GTPγS (PerkinElmer) and ligands (LXA₄ and 15-oxo-LXA₄-Me at 2 μM, WKYMVm (Tocris) at 5 μM). After an additional 15 min incubation at 25°C, the reaction was terminated by adding 6 ml of cold wash buffer containing 20 mM HEPES, pH 7.5, 150 mM NaCl, and 5 mM MgCl₂, and filtering through glass fiber prefilters (Millipore Sigma,). After washing 4 times with 6 ml cold buffer, the filters were incubated with 5 ml of CytoScint liquid scintillation cocktail (MP Biomedicals) and counted on a Beckman LS6500 scintillation counter.

Koudelka A., Buchan G.J., Cechova V., O’Brien J.P., Stevenson E.R., Uvalle C.E., Liu H., Woodcock S.R., Mullett S.J., Zhang C., Freeman B.A, & Gelhaus S.L. (2024). Lipoxin A4 yields an electrophilic 15-oxo metabolite that mediates FPR2 receptor-independent anti-inflammatory signaling. Journal of Lipid Research, 66(1), 100705.

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Production of MBP-3C-Mlp1(17-1,137)-His6 Fusion Protein

2024

MBP-3C-Mlp1(17-1,137)-His 6 was produced using baculovirus expression vector system. To generate V0 baculovirus stock, EMBacY bacmid harbouring the open reading frame of MBP-3C-Mlp1(17-1,137)-His 6 was transfected into Sf9 insect cells (Expression Systems). The recombinant fusion protein was expressed in Hi5 insect cells (Expression Systems) at 27 °C. The insect biomass was collected 3 days after proliferation arrest and flash frozen in liquid nitrogen.

Stankunas E, & Köhler A. (2024). Docking a flexible basket onto the core of the nuclear pore complex. Nature cell biology.

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Corresponding organizations : Max Perutz Labs, Vienna Biocenter, Medical University of Vienna

Baculovirus-Mediated Insect Cell Protein Expression

2024

The DNA constructs used in this study are listed in Table S2. For recombinant insect cell expression, the biGBac 75 (link) vector system was used. All protein sequences are numbered according to the canonical sequence entry in UniProt. Recombinant bacmids were generated from the plasmids in Table S2 using MAX Efficiency DH10Bac competent cells (Thermo Fisher Scientific) and transfected into Sf9 insect cells (Thermo Fisher Scientific) with Cellfectin II Reagent (Thermo Fisher Scientific) to generate a P1 baculovirus stock. P1 baculovirus was amplified in adherent Sf9 insect cells to generate P2 and P3 stocks, and the P3 virus was used to infect Tni suspension insect cell culture (Expression Systems) for protein expression.

Cai S.W., Takai H., Zaug A.J., Dilgen T.C., Cech T.R., Walz T, & de Lange T. (2024). POT1 recruits and regulates CST-Polα/primase at human telomeres. Cell, 187(14).

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Corresponding organizations : Rockefeller University, University of Colorado Boulder, Howard Hughes Medical Institute

GTPγS Binding Assay for FPR2 and Gαi

2024

The GTPγS binding assay was conducted using cell membranes overexpressing FPR2 and purified G_i heterotrimer, following our previously reported method (49 (link)). Briefly, Sf9 insect cells (ExpressionSystems) were infected with baculovirus expressing FPR2. The cells were collected by centrifugation at 8000 x g for 10 min after 48 hr. For ³⁵S-GTPγS binding analysis, ~200 µg/mL of human FPR2 cell membrane was incubated with 200 nM purified G_i protein for 20 min on ice in buffer containing 20 mM HEPES, pH 7.5, 150 mM NaCl, 5 mM MgCl₂, 3 μg/mL BSA, 0.1 μM TCEP, and 5 μM GDP. Next, 25 μL FPR2-G_i mix was transferred to 225 μL reaction buffer containing 20 mM HEPES, pH 7.5, 150 mM NaCl, 5mM MgCl₂, 3 μg/mL BSA, 0.1 μM TCEP, 1 μM GDP, 35 pM ³⁵S-GTPγS (Perkin Elmer) and ligands (LXA₄ and 15-oxo-LXA₄-Me at 2 μM, WKYMVm (Tocris) at 5 μM). After additional 15 min incubation at 25 °C, the reaction was terminated by adding 6 mL of cold wash buffer containing 20 mM HEPES, pH 7.5, 150 mM NaCl and 5mM MgCl₂, and filtering through glass fiber prefilters (Millipore Sigma,). After washing 4 times with 6 mL cold wash buffer, the filters were incubated with 5 mL of CytoScint liquid scintillation cocktail (MP Biomedicals) and counted on a Beckman LS6500 scintillation counter.

Koudelka A., Buchan G.J., Cechova V., O’Brien J.P., Liu H., Woodcock S.R., Mullett S.J., Zhang C., Freeman B.A, & Gelhaus S.L. (2024). Lipoxin A4 yields an electrophilic 15-oxo metabolite that mediates FPR2 receptor-independent anti-inflammatory signaling. bioRxiv.

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Corresponding organizations : University of Pittsburgh

Top 5 most cited protocols using «sf9 insect cells»

Purification of Human σ1 Receptor

Cited 4 times

The human σ₁ receptor was cloned into pFastbac1 with an amino-terminal hemagglutinin signal sequence followed by a FLAG epitope tag and a 3C protease cleavage site. Following proteolytic digest to remove the FLAG tag, the resulting protein is identical to the wild-type receptor with the exception of an amino terminal protease site scar, comprising the sequence “GPGS”. This receptor construct was expressed in Sf9 insect cells (Expression Systems) using the FastBac baculovirus system (ThermoFisher) according to the manufacturer’s instructions. Infection was performed when cells reached a density of 4 × 10⁶ cells/mL, and flasks were shaken at 27 °C for two days prior to harvest.
Cells were harvested by centrifugation and frozen at −80 °C until purification. For both PD144418 and 4-IBP-bound receptors, 1 μM of ligand was added in all purification steps. After thawing frozen cell paste, cells were lysed by osmotic shock in 20 mM HEPES pH 7.5, 2 mM magnesium chloride, and 1:100,000 (v:v) benzonase nuclease (Sigma Aldrich). Lysed cells were centrifuged at 20,000 rpm in a Sorvall RC 5C Plus centrifuge with an SS-34 rotor for 15 minutes. The receptor was then extracted using a glass dounce tissue grinder in a solubilization buffer containing 250 mM NaCl, 20 mM HEPES pH 7.5, 20% (v/v) glycerol, 1% (w/v) lauryl maltose neopentyl glycol (LMNG; Anatrace), and 0.1% (w/v) cholesterol hemisuccinate (CHS; Steraloids). Samples were stirred for 2 hr at 4 °C, and then centrifuged as before for 20 min. Next, samples were filtered on a glass microfiber filter. The filtered supernatant containing solubilized receptor was supplemented with 2 mM calcium chloride and loaded by gravity flow onto 5 mL anti-FLAG antibody affinity resin. The resin was washed extensively, first in 50 mL of buffer containing 100 mM NaCl, 20 mM HEPES pH 7.5, 2 mM calcium chloride, 0.2% glycerol, 0.1% LMNG, and 0.01% CHS, and then in 50 mL of buffer containing 100 mM NaCl, 20 mM HEPES pH 7.5, 2 mM calcium chloride, 0.02% glycerol, 0.01% LMNG, and 0.001% CHS. The receptor was eluted in the same buffer supplemented with 5 mM EDTA and 0.2 mg/mL FLAG peptide in lieu of calcium. 3C protease was added (1:100 w:w) and incubated with the receptor at 4 °C overnight.
The receptor was further purified by size exclusion chromatography (SEC) on a Sephadex S200 column (GE Healthcare) in buffer containing 0.01% LMNG, 0.001% CHS, 100 mM NaCl, 20 mM HEPES pH 7.5, and 1 μM of ligand. The receptor was biochemically pure but consistently ran as a high molecular weight oligomer during SEC. Following preparative SEC, the protein was concentrated to 20 –30 mg/mL and flash frozen with liquid nitrogen in aliquots of 8 –9 μL. Samples were stored at −80°C until use for crystallography. Purity and monodispersity of crystallographic samples was evaluated by SDS-PAGE and analytical SEC, respectively (Extended Data Figure 1).

Schmidt H.R., Zheng S., Gurpinar E., Koehl A., Manglik A, & Kruse A.C. (2016). Crystal structure of the human σ1 receptor. Nature, 532(7600), 527-530.

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Corresponding organizations : Harvard University, Stanford University

Recombinant Expression and Purification of KCTD-GABA Receptor Complexes

Cited 3 times

Human KCTD12 and KCTD16 genes were synthesized (Integrated DNA Technologies). KCTD12 (residues 32–131) and KCTD16 (residues 23–124) BTB domains were cloned into a pET28a expression vector (EMD Millipore) for the expression of an N-terminal His₆-SUMO fusion protein or an untagged version in Escherichia coli strain BL21(DE3). KCTD12 (residues 200–325) and KCTD16 (residues 158–279) H1 domain were cloned into the multiple cloning site 1 of pETduet-1 vector (EMD Millipore) and expressed with an N-terminal His₆-SUMO tag followed by 3C protease site. All human GABA_B2 C-terminal truncations were cloned into the same vector with an N-terminal His₆-GST or His₆-SUMO fusion protein followed by 3C protease site and were expressed in BL21(DE3) E. coli. KCTD12 (residues 32–325) and KCTD16 (residues 21–279) constructs containing both BTB and H1 domains were cloned into the vector pVL1393 vector (Expression Systems) and protein was expressed using baculovirus infection of Sf9 insect cells (Expression Systems) according the manufacturer’s protocols. These constructs were expressed with an N-terminal His₆-GST fusion protein followed by a 3C protease site. Human Gα_q was cloned into pVL1393 without tags. Human Gβ₁γ₂ heterodimer was modified to include an N-terminal His6 tag on the Gβ subunit and a C68S point mutation in Gγ, which eliminates the lipid modification site. A bicistronic vector based on pVL1392 was used to prepare baculovirus encoding both subunits. All point mutations and deletions were introduced by the QuikChange method.
Plasmids encoding untagged KCTD16 BTB and His₆-GST-tagged GABA_B2 fragment were co-transformed into E. coli BL21(DE3) strain. Bacteria were cultured in LB medium supplemented with 50 μg ml⁻¹ ampicillin and 50 μg ml⁻¹ kanamycin at 37 °C to an OD₆₀₀ value of 0.8, and protein expression was induced by the addition of 0.5 mM isopropyl 1-thio-β-D-glucopyranoside followed by shaking overnight at 18 °C. Cells were harvested by centrifugation, resuspended in buffer A (50 mM Tris-HCl, pH 8.0, 250 mM NaCl and 25 mM Imidazole) and lysed by sonication. His-GST-GABA_B2 fragment in complex with KCTD16_BTB was purified from clarified lysate by Ni-NTA affinity chromatography. Resin was washed with buffer A and protein then eluted with buffer B (50 mM Tris-HCl, pH 8.0, 250 mM NaCl and 250 mM Imidazole). The eluted fraction was incubated with 3C protease overnight to cleave His6-GST tag. Protein solution was diluted three-fold by 20 mM HEPES-NaOH, pH 7.6 and loaded onto a Q sepharose column (GE Healthcare). The flow-through was collected, concentrated and further purified by size exclusion chromatography (SEC) Superdex S200 10/300 equilibrated in storage buffer (10 mM HEPES-NaOH pH 7.6, and 150 mM NaCl). Protein expression and nickel affinity purification for His₆-SUMO-tagged KCTD12 H1 was performed as described above. After tag cleavage by 3C protease, the protein sample was concentrated and purified on a Superdex S200 10/300 size exclusion column equilibrated in storage buffer.
His₆-GST-tagged KCTD12 32–325 or KCTD16 21–279 was expressed in Sf9 insect cell cultures using the BestBac baculovirus system (Expression Systems). Infection was performed when cells reached a density of 3 × 10⁶ cell per mL and flasks were shaken at 27 °C for 36 hours before harvest. Cells were harvested by centrifugation and lysed in buffer A using a glass dounce tissue grinder. Protein was purified by Ni-NTA gravity flow chromatography followed by glutathione agarose bead affinity purification (GE Healthcare). The protein was further purified by Superdex S200 10/300 equilibrated in storage buffer. His6-tagged Gβ₁ and Gγ₂ (C68S mutant) were expressed in Sf9 insect cells using the BestBac system (Expression Systems) as described above. Purification was performed as previously reported^{23 (link)}.
For KCTD12_H1/Gβ₁γ₂ complex assembly and purification, individually purified KCTD12 H1 and Gβ₁γ₂ proteins were mixed in a 1:1.2 molar ratio and then incubated at room temperature for 30 min. Excess Gβ₁γ₂ was separated from KCTD12 H1/Gβ₁γ₂ complex on a Superdex S200 10/300 column in binding buffer (20 mM HEPES-NaCl pH 7.6 and 50 mM NaCl). For KCTD16 21–279/GABA_B2 876–913 complex, purified His6-SUMO-tagged GABA_B2 876–913 and His6-GST-tagged KCTD16 21–279 were mixed in a 2:1 molar ratio. The His6-SUMO tag of GABA_B2 and His6-GST tag of KCTD16 21–279 were cleaved by 3C protease at 4°C overnight. The protein complex was further purified by SEC S200 10/300 with storage buffer. For KCTD12 32–325/GABA_B2 876–913/ Gβ₁γ₂ complex, individually purified His₆-GST-tagged KCTD12 32–325, His₆-SUMO-tagged GABA_B2 876–913, and Gβ₁γ₂ were mixed in a 1:2:1.2 ratio. After tag cleavage by 3C protease the protein sample was loaded onto Superdex S200 10/300 equilibrated in binding buffer.

Zheng S., Abreu N., Levitz J, & Kruse A.C. (2019). Structural basis for KCTD-mediated rapid desensitization of GABAB signaling. Nature, 567(7746), 127-131.

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Corresponding organizations : Boston VA Research Institute, Harvard University, Cornell University

Purification of NKCC1 Transporter from Zebrafish

Cited 2 times

NKCC1 from Danio rerio was cloned into a modified pFastBac vector with an N-terminal maltose binding protein (MBP) tag and 3C protease cleavage site. This construct was expressed in Sf9 insect cells (Expression Systems, #94–001S; no further authentications were carried out and no mycoplasma contamination tests were performed for this study) using the baculovirus system. Cells were infected at a density of 3.5–4 × 10⁶ cells per ml and culture flasks were shaken at 27 °C for 60 hours. Cell pellets were frozen down at −80 °C until further use. All protein purification steps were carried out at 4 °C unless otherwise noted. Cells were lysed by osmotic shock by incubating for 30 mins in a buffer containing 20 mM Tris-HCl, pH 8.0 with 1.5 μg/ml Leupeptin, 1.5 μg/ml pepstatin A, 1mM benzamidine, and 1:500 dilution of aprotinin. The sample was then centrifuged at 39,000g for 20 min. The supernatant was discarded and the pellets were solubilized using a glass Dounce tissue homogenizer in buffer A (20mM Tris-HCl, pH 8.0, 200mM NaCl, 200mM KCl) supplemented with 1% lauryl maltose neopentyl glycol (LMNG, Anatrace), 0.01% cholesteryl hemisuccinate (CHS, Anatrace), 1.5 μg/ml Leupeptin, 1.5 μg/ml pepstatin A, 1mM benzamidine, and 1:500 dilution of aprotinin. The sample was stirred for 2.5 hours and then centrifuged at 31,000g for 45 min. The insoluble fraction was discarded and the supernatant was incubated with prewashed amylose resin for 1 hour. The resin was carefully washed to remove contaminant protein. The NKCC1 protein was cleaved from MBP by incubating with 3C protease. The sample was further purified by gel filtration (Superose 6, GE Healthcare) in buffer A with 0.06% digitonin. The peak fraction was collected and concentrated for cryo-EM.

Chew T.A., Orlando B.J., Zhang J., Latorraca N.R., Wang A., Hollingsworth S.A., Chen D.H., Dror R.O., Liao M, & Feng L. (2019). Structure and mechanism of the cation-chloride cotransporter NKCC1. Nature, 572(7770), 488-492.

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Corresponding organizations : Stanford University, Harvard University

Culturing Sf9 and HEK293T Cell Lines

Cited 1 time

Spodoptera frugiperda (Sf9) insect cells (Expression Systems) were grown in ESF 921 serum-free medium (Expression Systems) at 27 °C and 120 rpm. HEK293T cells (American Type Culture Collection) were cultured in DMEM (Life Technologies) supplemented with 10% FBS (Gibco) and maintained in a humidified chamber with 5% CO₂ at 37 °C.

Cong Z., Zhou Q., Li Y., Chen L.N., Zhang Z.C., Liang A., Liu Q., Wu X., Dai A., Xia T., Wu W., Zhang Y., Yang D, & Wang M.W. (2022). Structural basis of peptidomimetic agonism revealed by small-molecule GLP-1R agonists Boc5 and WB4-24. Proceedings of the National Academy of Sciences of the United States of America, 119(20), e2200155119.

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Corresponding organizations : Fudan University, Sir Run Run Shaw Hospital, Zhejiang University, Huazhong University of Science and Technology, National Center for Drug Screening, Shanghai Institute of Materia Medica, University of Chinese Academy of Sciences, Chinese Academy of Sciences, Institute of Deep-Sea Science and Engineering

Expression and Purification of FLAG-tagged Sigma-1 Receptor

Cited 1 time

The pFastBAC plasmid encoding for the FLAG tagged σ1R gene was kindly provided by Prof. Andrew Kruse (Harvard Medical School, Boston, MA, USA). The protein was expressed and purified according to previously described conditions [22 (link)] at the Protein Facility of Elettra Sincrotrone Trieste (Basovizza, Trieste, Italy). The bacmid was generated by transposition using E. coli DH10Bac competent cells (Invitrogen, Waltham, MA, USA). Sf9 insect cells (Expression Systems, Davis, CA, USA) were used for virus preparation and protein expression. Infection was performed at a density of 1 x 106 cells/mL and cultures were grown at 27 °C for 72 h. Cells were harvested by centrifugation, lysed by osmotic shock in 20 mM Hepes pH 7.5, 2 mM MgCl₂ and 1:100.000 (v/v) Benzonase (#E1014, Merck, Darmstad, Germany) and then centrifuged for 15′ at 47,800× g. The pellet was resuspended in solubilisation buffer (20 mM Hepes pH 7.5, 250 mM NaCl, 20% v/v glycerol, 1% w/v lauryl maltose neopentyl glycol (LMNG; Anatrace, Maumee, OH, USA), and 0.1% (w/v) cholesteryl hemisuccinate (CHS; Steraloids, Newport, RI, USA)) using a glass Dounce homogeniser. After 2 h stirring at 4 °C, samples were centrifuged for 20′ at 47,800xg. Filtered supernatant was then loaded on Anti–DYKDDDK resin (#L00432, GenScript, Nanjing, China), previously equilibrated with 20 mM Hepes pH 7.5, 100 mM NaCl, 0.2% v/v glycerol, 0.1% w/v LMNG, 0.01% w/v CHS. The resin was first washed with the same buffer used for equilibration, and washed again with a second washing buffer (20 mM Hepes pH 7.5, 100 mM NaCl, 0.02% v/v glycerol, 0.01% LMNG, 0.001% CHS). The protein was eluted with 0.2 mg/mL FLAG peptide (#RP10586-1, GenScript), and dissolved in the second washing step buffer, in three steps: E1, E2, E3. These steps differ in the time of incubation of the resin with the elution buffer (E1: no incubation; E2: 1 h incubation; E3: over-night incubation). σ1R purity was assessed by SDS–Page and Western blot (Figure 3).

Battista T., Pascarella G., Staid D.S., Colotti G., Rosati J., Fiorillo A., Casamassa A., Vescovi A.L., Giabbai B., Semrau M.S., Fanelli S., Storici P., Squitieri F., Morea V, & Ilari A. (2021). Known Drugs Identified by Structure-Based Virtual Screening Are Able to Bind Sigma-1 Receptor and Increase Growth of Huntington Disease Patient-Derived Cells. International Journal of Molecular Sciences, 22(3), 1293.

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Corresponding organizations : Institute of Molecular Biology and Pathology, National Research Council, Sapienza University of Rome, Casa Sollievo della Sofferenza, Istituti di Ricovero e Cura a Carattere Scientifico, University of Campania "Luigi Vanvitelli", Elettra-Sincrotrone Trieste S.C.p.A., University of Trento

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