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#fab-tacs #gravity column # T cell #hCD3
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#Cell isolation #FABian® #Non-magnetic Cell Separation #Strep-Tactin APC #FABian #hCD14 FABian #6-5000-001 #6-6100-260 #6-6017-001
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#Cell Staining #MHC I Streptamers® #CD8+ T cell #Flow Cytometry
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#Cell Separation #Fab-TACS® #Non-magnetic Cell Separation
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#Cell Staining #MHC I Streptamers® #CD8+ T cell #Cell Therapy #Immuno Therapy #Personalized Therapy
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#Cell Staining #MHC I Streptamers® #CD8+ T cell #Cell Therapy #Immuno Therapy #Personalized Therapy
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#Cell sorting #Strep-Tactin®XT DY-488
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#Cell Separation #Fab-TACS® #Fab-TACS #CD8 #TACS #Fab-Strep
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#Cell Staining #MHC I Streptamers® #CD8+ T cell #Graft-Versus-Host
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#Cell Staining #MHC I Streptamers® #CD8+ T cell #Cell Therapy #Immuno Therapy #Personalized Therapy
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#Cell Staining #MHC I Streptamers® #CD8+ T cell #Cell Therapy #Immuno Therapy #Personalized Therapy #Peptide for stimulation of T-cells # StrepMan #Magnetic Beads #D-Biotin #Strep-Tactin PE #Strep-Tactin APC #Peptide for stimulation of T-cells #6-5650-065 #6-5510-050 #6-0219-001 #6-5000-001
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#T Cell Stimulation & expansion #Fab Streptamers® #CD3/CD28 Streptamers
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#Cell Staining #MHC I Streptamers® #CD8+ T cell
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#T cell stimulation #Streptamer® #CD3/CD28 Streptamers®
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#Cell Staining #MHC I Streptamers® #CD8+ T cell #Cell Therapy #Immuno Therapy #Personalized Therapy
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#Cell Staining #MHC I Streptamers® #CD8+ T cell #Dendritic Cells
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#Twin-Strep-tag #Strep-Tactin XT Superflow high capacity cartridge #Twin-Strep-Tag Capture Kit #2-4370-000 #2-4026-001
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#Cell Separation #Fab Streptamers® #CD8+ T cell #Reversible Streptamers® preserve T cell receptor expression of CD8+ T cells
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#Cell Staining #MHC I Streptamers® #CD8+ T cell #Signalling
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#Strep-Tactin Superflow column #Strept-Tactin APC backbone #CD3/CD28 Streptamers #6-2010-005 #2-4011-005 #6-5010-001 #6-8900-000
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#Cell Staining #MHC I Streptamers® #CD8+ T cell #Dendritic Cells
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#Cell Staining #MHC I Streptamers® #CD8+ T cell
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#Cell Separation #Fab-TACS®
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#Cell Separation #Fab Streptamers® #CAR T cell enrichment
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#Cell Staining #MHC I Streptamers® #CD8+ T cell #Dendritic Cells
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#Cell Staining #MHC I Streptamers® #CD8+ T cell #Cell Therapy #Immuno Therapy #Personalized Therapy
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#Cell Staining #MHC I Streptamers® #CD8+ T cell
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#Cell Separation #Fab-TACS®
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#Cell Staining #MHC I Streptamers® #CD8+ T cell
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#Cell isolation #FABian®
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#Cell Staining #MHC I Streptamers® #CD8+ T cell #Flow Cytometry
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#Cell Staining #MHC I Streptamers® #CD8+ T cell
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#Cell isolation #FABian®
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#Cell Staining #MHC I Streptamers® #CD8+ T cell #Immune Status
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#Cell Staining #MHC I Streptamers® #CD8+ T cell #Cell Therapy #Immuno Therapy #Personalized Therapy
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#Cell Staining #MHC I Streptamers® #CD8+ T cell #T cell receptor affinity
In the following publication Mühlberger et al. used our Fab-TACS® columns and the adapter to separate cells loaded with superparamagnetic iron oxide nanoparticles (SPIONs) from unbound SPIONs. The authors replaced the Fab-Streps supplied with our kits with a desthiobiotinylated anti-mouse CD90.2 antibody, which can also be eluted with biotin. This approach allowed them to successfully separate magnetic cells from magnetic particles with an antibody of their choice.
For detailed information view the publication here. #Cell Separation #Fab-TACS®#gravity column #adapter
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#Cell Separation #Fab-TACS® #Serial positive enrichment #multiparameter cell sorting
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#Cell Staining #MHC I Streptamers® #CD8+ T cell
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#Cell Staining #MHC I Streptamers® #CD8+ T cell #Vaccines
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#Cell Staining #MHC I Streptamers® #CD8+ T cell #Cord blood
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#Cell Staining #MHC I Streptamers® #CD8+ T cell #Cell Therapy #Immuno Therapy #Personalized Therapy
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#Cell Staining #MHC I Streptamers® #CD8+ T cell #Cell Therapy #Immuno Therapy #Personalized Therapy
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#Cell Staining #MHC I Streptamers® #CD8+ T cell
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#Cell Staining #MHC I Streptamers® #CD8+ T cell
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#Cell Staining #MHC I Streptamers® #CD8+ T cell #Clinical Monitoring
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#Cell Separation #Fab Streptamers® #CD3/CD28 Streptamers® #preserve proliferation capacity and functional
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#Cell Staining #MHC I Streptamers® #CD8+ T cell #Cell Therapy #Immuno Therapy #Personalized Therapy
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#Cell Staining #MHC I Streptamers® #CD8+ T cell #Cell Therapy #Immuno Therapy #Personalized Therapy
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#Cell Staining #MHC I Streptamers® #CD8+ T cell #Cell Therapy #Immuno Therapy #Personalized Therapy
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#Cell Separation #MHC I Streptamers® # #Antigen-specific T cell isolation
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#Cell Staining #MHC I Streptamers® #CD8+ T cell #Immune Status
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#Twin-Strep-tag #Strep-Tactin XT #MagStrep "type3" XT beads
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#Cell Staining #MHC I Streptamers® #CD8+ T cell #TIL - Tumor infiltrating Lymphocyte
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#Cell Staining #MHC I Streptamers® #CD8+ T cell #Cell Therapy #Immuno Therapy #Personalized Therapy
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#Cell Staining #MHC I Streptamers® #CD8+ T cell #Vaccines
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#Cell Staining #MHC I Streptamers® #CD8+ T cell #Cell Therapy #Immuno Therapy #Personalized Therapy
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#Cell Staining #MHC I Streptamers® #CD8+ T cell #Vaccines
#Western blot #MagStrep ‘type3’ XT beads #2-4090-010
Ananthaswamy et al. took advantage of our BioLock biotin blocking solution prior to Strep-Tactin® protein purification of Twin-Strep-tagged gp140, the external part of the HIV gp160 glycoprotein spike. For antigenicity studies of gp140, an ELISA was performed in our Strep-Tactin® coated microplate.
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#Strep-tag #Twin-Strep-tag #Strep-Tactin #Strep-Tactin® coated microplate #Cryo-EM Structure #BioLock #biotin blocking solution #2-0205-050 #2-0205-050 #2-1501-001
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#protein interactions #AP-MS map
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#ELISA #Western blot #StrepMAB-classic #Strep-Tag II #Strep-Tactin-coated microtitre plate #pEXPR-IBA103 #Strep-Tactin Superflow high-capacity slurry #StrepMAB-Classic HRP #2-1507-001 #2-1501-001 #2-1209-101 #2-1509-001
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#Cell Separation #Fab-TACS®
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#Gravity flow Strep-Tactin® Sepharose® column #Gravity flow Strep-Tactin®XT Superflow® column #2-1202-001 #2-4011-005
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#Membrane protein
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#Immobilization
Chen and colleagues analyzed unknown functions of the large 5’ untranslated region of a virulence factor encoding gene of the human pathogen Streptococcus pyogenes. Within their studies, they made use of our StrepMAB-Classic antibody for western blot analysis. An in vivo pull-down assay was carried out using our MagStrep “type3” beads to bind protein and RNA molecules.
For detailed information view the publication here. #co-immunoprecipitation #Pull-down assay #Western blot #StrepMAB-Classic #MagStrep "type3" XT beads #2-1507-001 #2-4010-002
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#Pull-down assay #Strep-Tactin
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#Pull Down Assay
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#Membrane protein
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#Western blot #MagStrep (Strep-Tactin) type 3 XT magnetic beads #2-4090-002
Yeliseev and colleagues made use of our products for purification of a structurally intact difficult-to-express human cannabinoid receptor CB2 for following high resolution structural studies. During their experiments, they compared i.a. the binding capacities of our Strep-Tactin®XT Superflow® with MagStrep “type3” XT beads. Additionally, the affinity of Twin-Strep-tagged CB2 to Strep-Tactin®XT was analyzed by binding experiments with surface plasmon resonance showing convenient results achieved through Strep-tag® technology.
For detailed information view the publication here. #Immobilization #Strep-Tactin®XT #Surface plasmon resonance #MagStrep "type3" XT beads #Strep-Tactin®XT Superflow® resin #50 % suspension #2-4010-002
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#Mammalian Expression #Strep-tag®
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#Protein Purification #Strep-Tactin® Superflow® #high capacity
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#Detection #Strep-tag® #Antibody
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#Cloning vectors #Twin-Strep-tag® #Strep-tag® #Recombinant Protein Expression
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#Detection #Strep-tag® #Antibody
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#Detection #Strep-tag® #Antibody
Seesuay and co-workers explored potential treatment strategies against Ebola virus disease focusing on cell-penetrable human single-chain antibodies (HuscFvs). In doing so, they have used our Biotin blocking buffer and Strep-Tactin® HRP for a co-immunoprecipitation assay between a Strep-tagged HuscFvs antibody and the Ebola virus VP35 protein. Additionally, the researchers accomplished western blot detection of HuscFvs-R9 with a corresponding substrate with the aid of our Strep-Tactin® AP. For intracellular localization of the protein HuscFvs via confocal immunofluorescence microscopy, our StrepMAB-Immo DY-488 antibody was applied.
#Detection #Strep-tag® #Antibody Immunoprecipitation #Western blot #Immunostaining #StrepMAB-Immo DY-488 #Biotin blocking buffer #Strep-Tactin®-HRP conjugate #Strep-Tactin® AP conjugate #2-1564-050 #2-0205-050 #2-1502-001
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#Detection #Strep-tag® #Antibody
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#Detection #Strep-Tactin® #Conjugates
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#Detection #Strep-tag® #Antibody
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#Cloning & Transfection #Strep-tag® #pASK-IBA vectors
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#Immobilization #Strep-Tactin®XT #SPR measurements
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#Immobilization #Strep-Tactin®XT #SPR measurements
Gordon et al. used our MagStrep "type3" XT beads in combination with our Strep-Tactin®XT Elution Buffer (BXT) for efficient purification of several Twin-Strep-tagged SARS-CoV-2 proteins in an affinity purification-mass spectrometry approach and were thereby able to discover protein-protein interactions with human proteins among which potential druggable targets were identified.
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#SARS-CoV-2 #Research tools for COVID-19 #Protein:protein interaction #MagStrep "type3" XT beads #Buffer BXT #2-4010-002 #2-1042-025
Wang et al. stably produced the spike ectodomain of different Betacoronavirus species in the Drosphila S2 cell line and purified the recombinant proteins with the help of our Strep-Tactin® Sepharose®. In the course of the study, our StrepMAB-Classic antibody and its HRP conjugate were used as isotype control in the production of a human monoclonal antibody and for concurrent validation of an ELISA analysis demonstrating the antibody binding to SARS CoV-2 spike antigens.
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#SARS-CoV-2 #Research tools for COVID-19 #Protein purification #ELISA #StrepMAB-Classic #HRP #Strep-Tactin® Sepharose® 50% suspension #2-1507-001 #2-4010-002
The spike (S) proteins of SARS-CoV-2 that mediate membrane fusion and host cell entry, contain several host-derived sugars, so called glycans. These glycoproteins provide fundamental features of viral biology, as they play key roles in protein folding and immune evasion. Watanabe and colleagues could reveal the glycan structures of a recombinant SARS-CoV-2 S protein. The researchers expressed Twin-Strep-tagged versions of the SARS-CoV-2 S protein in HEK cells and purified them from cell supernatants using Strep-Tactin®. Then they combined mass spectrometric and cryo-EM analyses to determine how the glycans cover distinct regions of the virus spike surface. With this site-specific glycan signature of the SARS-CoV-2 spike, the research team improved the understanding of viral biology with major implications for vaccine development.
For detailed information view the publication here. #SARS-CoV-2 #Research tools for COVID-19
Wang et al. stably produced the spike ectodomain of different Betacoronavirus species in the Drosphila S2 cell line and purified the recombinant proteins with the help of our Strep-Tactin® Sepharose®. In the course of the study, our StrepMAB-Classic antibody and its HRP conjugate were used as isotype control in the production of a human monoclonal antibody and for concurrent validation of an ELISA analysis demonstrating the antibody binding to SARS CoV-2 spike antigens.
For detailed information view the publication here. #SARS-CoV-2 #Research tools for COVID-19
Romero Pastrana and colleagues worked on expression vectors for extracellular protein production with Lactococcus lactis as host. For protein purification, our Strep-Tactin® Sepharose® 50% suspension was applied, and for detection of strep-tagged proteins, our StrepMAB-Classic antibody was used as primary antibody in western blot analysis. An ELISA approach was carried out on Strep-Tactin® coated microplates to detect specific human IgGs, which bind to the strep-tagged staphylococcal proteins.
For detailed information view the publication here.#Western blot #ELISA #Strep-Tactin® Sepharose® 50% suspension #StrepMAB-Classic #Strep-Tactin® coated microplates #2-4010-002 #2-1507-001 #2-1501-001
AlSalmi and colleagues worked on the HIV-1 envelope trimer and therein focused on the role of the exposed part, gp140, and its potential role in vaccine development. By simply tagging their protein of interest with a Strep-tag®II and the use of Strep-Tactin® beads after application of our BioLock biotin blocking solution, the researchers succeeded in the capture of nearly homogeneous gp140 directly from the culture supernatant. For an ELISA approach, our Strep-Tactin® coated microplates were coated with the gp140 trimers to discriminate between different cleavage variants. Western blot analysis was conducted with the aid of our StrepMAB-Classic HRP conjugate.
For detailed information view the publication here.#ELISA #Western blot #Strep-Tactin® coated microplate #Strep-Tactin® resin #BioLock biotin blocking solution #StrepMAB-Classic HRP #2-1501-001 #Strep-Tactin® resin #2-0205-050 2-0205-050 #2-1507-001
To characterize the enzyme CoA-acylating prenal dehydrogenase originate from Aquincola tertiaricarbonis (AtPDH), Becher et al. used our pASG-IBA43 vector for cloning of the respective gene of wild type AtPDH and different variants. For expression of these proteins, our chemically competent E. coli TOP10 cells were transformed with pASG-IBA43 carrying the respective genes.
For detailed information view the publication here.#Competent E. coli TOP10 #pASG-IBA43 #5-1600-020 #5-4000-001
To gain insights into the physiopathological function, Zafar et al. copurified the cellular prion protein along with its interaction partners using Strep Tactin® Superflow®. The researchers made use of StarGate® transfer/combinatorial cloning with our vectors for mammalian expression, pENTRY-IBA and pESG-IBA, and further implemented the StrepMAB-Classic antibody and its HRP conjugate in immunoblot analysis as primary or secondary antibody, respectively.
For detailed information view the publication here.#Western blot #StrepMAB-Classic #StrepMAB-Classic #HRP #Strep-Tactin® Superflow® 50% suspension #pENTRY-IBA #pESG-IBA #2-1507-001 #2-1507-001 #2-1206-025#5-4091-001 #5-4400-001
Terfrüchte and co-workers utilized our GFP-Strep-tag®II control protein as positive control for the biochemical characterization of nanobodies and their GFP binding activity in an ELISA.
For detailed information view the publication here.#ELISA #GFP-Strep-tag control protein #2-1006-005
Peng et al. were able to observe significantly higher T cell responses in severe as compared to mild cases of COVID-19 in recovered patients and succeeded in identification of six immunodominant epitope groups. Further, a higher proportion of specific CD8+ T cell responses has been reported in mild disease. During their research, our StrepMAB-Classic antibody was used for coating of immunoplates for a following ELISA.
For detailed information view the publication here.#ELISA #SARS-CoV 2 #StrepMAB-Classic #2-1507-001
Krieger et al. packed columns with our Strep-Tactin® Sepharose® 50% suspension for purification of RNA-binding HBV core antigens after expression in HEK-293 cells. The strep-tagged proteins were eluted from the columns with a buffer supplemented with our desthiobiotin.
For detailed information view the publication here.#Desthiobiotin #Strep-Tactin® Sepharose® 50% suspension #2-1000-001 #2-4010-002
Schäfer and co-workers aimed to explore the complement system regulator FHR-3 and its role in autoimmune diseases. Therefore, they used our Strep-Tactin® Sepharose® columns for purification of recombinant FHR-3 protein and purity was controlled by western blotting with our StrepMAB-Classic antibody. To analyze the interaction with C3b, an ELISA was performed, and the binding was screened with our StrepMAB-Classic antibody conjugated with HRP.
For detailed information view the publication here.#Western blot #StrepMAB-Classic #StrepMAB-Classic #HRP #Gravity flow Strep-Tactin® Sepharose® column# #2-1507-001 #2-1507-001 #2-1202-001
To fuse the M13 phage coat protein pIX with Strep-tag®II for targeted immobilization with the wished orientation of the phages, Tong and colleagues applied our StarGate® cloning system, including pENTRY-IBA51 into which the gene of interest is cloned (donor) and here, an anhydrotetracycline inducible pASG-IBA4 vector encoding an ompA signal for periplasmic secretion (acceptor).
For detailed information view the publication here.#pENTRY #pASG-IBA4 #5-4091-001 #5-4000-001
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#Magnetic Microbeads #MHC I Strep #Strep-PE #Fab Streptamer for MB #Peptide for stimulation of T-cells #6-5510-050 #MHC I Strep #6-5000-001
Tausch and colleagues successfully generated a functional recombinant Haemolysin BL enterotoxin complex from Bacillus cereus exploiting our integrated Strep-tag® system: after cloning the corresponding sequences into our pASK-IBAplus vectors well established for expression in E. coli, efficient purification of the target on Strep-Tactin® Sepharose® was confirmed via immunoblotting with our StrepMAB-Classic antibody.
For detailed information view the publication here.#Western blot #StrepMAB-Classic #Strep-Tactin® Sepharose® 50% suspension #pASK-IBA #2-1507-001 #2-4010-002 #2-1321-000
Investigating the role of Gadd45β protein in inflammatory bowel disease, Hwang and colleagues performed a pull-down assay with our Strep-Tactin® Sepharose® followed by western blot analysis using our StrepMAB-Classic antibody.
For detailed information view the publication here.#Pull-down assay #Western blot #StrepMAB-Classic #Strep-Tactin® Sepharose® 50% suspension #2-1507-001 #2-4010-002
To produce monoclonal antibodies against Rift Valley fever virus proteins, Jäckel et al. made use of our StarGate® cloning strategy: nucleocapsid proteins were obtained by cloning the respective genes into our pPSG-IBA43 vector for bacterial production (acceptor) via our pENTR-IBA51 vector (donor).
For detailed information view the publication here.#pENTRY #pPSG-IBA43 #StarGate cloning Kit #5-4091-001
#Buffer IS #Biotin #Strep-Tactin #Magnetic Microbeads #MHC I Strep #Strep-PE #6-5602-050 #6-0219-001 #Strep-Tactin #6-5510-050 #MHC I Strep #6-5000-001
For the identification of possible interaction partners of the fatty acid 2-hydroxylase (FA2H) involved in neurodegenerative diseases, Hardt and colleagues used an integrated approach of quantitative mass spectrometry with formaldehyde cross-linking and proximity biotinylation. To create the best possible preconditions, they generated a Twin-Strep-tagged FA2H by cloning the gene of interest firstly into our pENTRY-IBA51 vector and subsequently into the pESG-IBA108 vector for mammalian expression. Efficient purification was carried out on our Strep-Tactin® Macroprep® resin and western blot analysis performed with the aid of Strep-Tactin® HPR conjugate.
For detailed information view the publication here.#pENTRY-IBA51#pESG-IBA108 #Strep-Tactin Macroprep beads #StrepTactin HRP conjugate #5-4091-001 #5-4400-001 #2-1505-010 #2-1502-001
#StrepMan #Magnetic Beads #Buffer IS #6-5650-065 #6-5510-050 #6-5602-050
Progranulin (PGRN) has an important function in the brain and plays a critical role in maintaining lysosome functionality, thereby influencing the likelihood of occurrence of neurogenerative diseases. In this study, Holler and colleagues successfully verified the expression of the Strep-tagged target by immunoblotting with the StrepMAB-Immo antibody and purified PGRN with our Strep-Tactin®XT Superflow® resin.
For detailed information view the publication here.#Western blot #Strep-Tactin®XT Superflow® resin #StrepMAB-Immo #2-4010-002 #2-1517-001
In order to better understand the avidity in multivalent protein interactions and its role in disorder-based allostery, Sørensen and co-workers used our Strep-Tactin®XT Superflow® columns for purification of several fusion proteins containing disordered linker regions. In addition, our StrepMAB-Immo antibody was applied for the capture of strep-tagged proteins in a surface plasmon resonance (SPR) analysis.
For detailed information view the publication here.#Surface plasmon resonance #StrepMAB-Immo #Gravity flow Strep-Tactin®XT Superflow® column #2-1517-001 #2-4011-005
Ortega et al. tested different parameters for efficient recombinant protein expression and purification using their specially developed vector suite. In doing so, they received high purity in a single step using our Twin-Strep-tag® system for protein purification from Drosophila melanogaster cell culture in combination with our BioLock biotin blocking solution and our Strep-Tactin®XT Superflow® column.
For detailed information view the publication here.#BioLock #Gravity flow Strep-Tactin®XT Superflow® column #2-0205-050 #2-4011-005
Maidorn and colleagues generated two new nanobodies for the detection of synaptic proteins. For antigen purification our Twin-Strep-Tag® was fused to the respective proteins. To identify binders during phage display, the Twin-Strep-tagged antigens were immobilized to our MagStrep "type3" XT beads and used for a pull-down assay. After washing, retained phages were eluted using Strep-Tactin®XT Elution Buffer (BXT).
For detailed information view the publication here.#Pull-down assay #MagStrep "type3" XT beads #Buffer BXT #2-4010-002 #2-1042-025
Scholl et al. used our pASK-IBA3 and -IBA5 vectors for either N- or C-terminal fusion of the Strep-tag®II to a recombinant phosphoenolpyruvate carboxylase and global signal transduction protein PII, followed by purification with our Strep-Tactin® Superflow columns. To elucidate complex formation of the targets under different conditions, an in-batch pull-down assay using our MagStrep “type3” XT beads was performed and bound proteins were eluted using our Buffer BXT.
For detailed information view the publication here.#Pull-down assay #MagStrep "type3" XT beads#Gravity flow Strep-Tactin Superflow high cap. col. #pASK-IBA3 -IBA5 #Buffer XT #2-4010-002 #2-1209-001#2-1321-000 #2-1045-250
To identify interactors of a kinase regulator of plant immune response, Giska and co-workers performed a tandem affinity purification combining our Twin-Strep-tag® with a FLAG-tag coupled to mass spectrometric analysis. Upon detection of a protein phosphatase as important interactor, the enzyme was produced in E. coli via our pASK-IBA3C vector, purified with our Strep-Tactin® Macroprep® and the interaction was further underpinned in a pull-down assay utilizing MagStrep "type3" XT beads. The presence of the respective Strep-tagged proteins was verified by western blot deploying our StrepMAB-Classic HRP conjugate.
For detailed information view the publication here.#Pull-down assay #Western blot #MagStrep "type3" XT beads #Strep-Tactin® MacroPrep® #Pask iba3 plus #StrepMAB-Classic HRP conjugate #2-4010-002 #2-1505-010 #2-1321-000 #2-1507-001
Satapathy et al. demonstrate the utility of IBA’s MEXi system for mammalian expression of fully functional heavily post-translationally modified and structurally complex proteins, enabling the comprehensive analysis of structure-function relationships of difficult-to-express, low abundant or even secreted targets. After protein production using MEXi-293E cells in combination with our specially prepared transfection and culture media, they were able to obtain highly pure and functional mammalian chaperone clusterin upon elution from the Strep-Tactin®XT Superflow® high capacity cartridge. As compared to prior expression and purification strategies, the researchers report a more than six times substantial increase in yield directly from human plasma cultures, deploying a straightforward single-step chromatography protocol. Further, they made use of the integrated Strep-tag® toolbox by applying our StrepMAB-Classic antibody and Strep-Tactin® HRP conjugate for detection by cell staining as well as western blotting.
For detailed information view the publication here.#Mexi cells #CM and TM media #Streptactin-XT Superflow high capacity cartridge #StrepMAB-Classic# #2-6001-001 #2-6010-010 #2-6011-010 #2-4025-001 #2-1507-001
Hausjell and colleagues tested different yeasts for the recombinant production of the abundant but hard-to-express protein superfamily of cytochromes P450. For this purpose, they made use of our StarGate® cloning system with the pENTRY-IBA51 vector for the first and pYSG-IBA103 for the second step. Our competent E. coli TOP10 cells were used for first plasmid cloning steps prior to transformation of the respective yeast strain.
For detailed information view the publication here.#competent E. coli TOP10 #pENTRY #pYSG-IBA103 #5-1600-020 #5-4091-001 #5-4600-001
For detailed information view the publication here.
#ELISA #Western blot #Surface plasmon resonance #pDSG expression vector #Strep-tactin affinity chromatography #Strep-Tactin XT coated microplate #2-1501-001
Read how Wrobel et al. compare the spike glycoproteins of SARS-CoV-2 and closely related bat virus RaTG13 to uncover the virus emergence. Here, our protein purification products were exploited to optimize yield and purity by pretreatment of the expression culture with BioLock Biotin blocking solution before binding of the Twin-Strep-tag® fusion proteins to Strep-Tactin®XT and elution with with Buffer BXT.
For detailed information view the publication here.#BioLock #Strep-Tactin®XT Superflow® resin #Buffer BXT #2-0205-050 #2-4010-002 #2-1042-025
See how Barinka et al. used a variety of our products: For protein purification they utilized our Strep-Tactin® Sepharose® columns and eluted their protein by addition of our desthiobiotin. Strep-Tactin® AP was deployed in ELISA screening to identify Anticalin candidates targeting the prostate-specific membrane antigen. For both immunofluorescence microscopy and analysis by flow cytometry, cells were immobilized for staining with our StrepMAB-Immo as primary antibody.
For detailed information view the publication here.#ELISA #Immunostaining #Flow cytometry #StrepMAB-Immo #Desthiobiotin #Strep-Tactin® AP conjugate #Gravity flow Strep-Tactin® Sepharose® column #2-1517-001 #2-1000-001 #2-1502-001 #2-1202-001
To access the feasibility of amber codon suppression for large and complex multidomain proteins, Heil et al. purified a Strep-tagged fusion protein with the aid of our Strep-Tactin® column and afterwards utilized our StrepMAB-Classic antibody as primary antibody for a quantitative western blot to read out incorporation efficiency of non-canonical amino acids.
For detailed information view the publication here.#Western blot #StrepMAB-Classic #Strep-Tactin® column #2-1507-001 #Strep-Tactin® column
Muschallik et al. worked on the stereoselective characteristics of the (R,R)-butane-2,3-diol dehydrogenase.
For detailed information view the publication here.#Strep-Tactin® MacroPrep® #pASG #2-1505-010 #5-4000-001
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#Strep-Tactin PE + APC #CD3 Fab-TACS human #Peptide for stimulation of T-cells #6-5000-001 #6-3201-004 #Peptide for stimulation of T-cells
Röhlen and colleagues present insights in the field of biosensor systems for both tricarboxylic acids as well as organic and volatile fatty acids. The researchers for instance worked on a hybrid biosensor system based on a bi-enzymatic detection principle. For expression of the proteins of choice, first our pENTRY vector was used and sub-cloned into pASG-IBA5 carrying either a C- or N-terminal Strep-tag®II. Following expression, our Strep-Tactin® MacroPrep® resin was used for protein purification exploiting the mild elution with desthiobiotin.
For detailed information view the publication here.#Desthiobiotin #ENTRY vector #pASG-IBA5 #Strep-Tactin® MacroPrep® #2-1000-001 #5-4091-001 #5-4000-001 #2-1505-010
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#Strep-Tactin®XT DY-649 #2-1568-050 #Flow cytometry
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#Strep-Tactin XT #Strep-Tactin #Strep-tag #Twin-Strep-tag
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#Fab-TACS #CD4 #TACS #Fab-Strep
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#streptamer #strep-tactin #strep-tactin PE #streptactin PE #strep-tactin APC #streptactin APC #B cells #antigen-specific B cells
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#cellisolation #cellstaining #mhc I Streptamer #tcells
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#cellisolation #Fab-TACS #tcells #gravitycolumns
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#Strep-Tactin®XT DY-649 conjugate #Twin-Strep-tag® #protein interactions #microscopy #fluorescent dyes #internal tag #2-1568-050
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#Twin-Strep-tag® Capture Kit #surface plasmon resonance #SPR #immobilization #pull-down assay
