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streptactin xt magnetic beads  (IBA Lifesciences)


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    Structured Review

    IBA Lifesciences streptactin xt magnetic beads
    Streptactin Xt Magnetic Beads, supplied by IBA Lifesciences, used in various techniques. Bioz Stars score: 95/100, based on 76 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/strep+beads/MagStrep+Strep-Tactin+XT+beads/bio_rxiv__64898__2026__05__05__723063-203-21-25
    Average 95 stars, based on 76 article reviews
    streptactin xt magnetic beads - by Bioz Stars, 2026-09
    95/100 stars

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    Related Articles

    Incubation:

    Article Title: Single-molecule identification of full-length proteins with single-amino-acid resolution using nanopores
    Article Snippet: .. The lysed cells were centrifuged (14000xg, 20 min, 4 °C) and the supernatant was incubated with Strep beads (Strep-Tactin® MacroPrep® resin from IBA Lifesciences) for 4 hours at 4 °C with agitation. ..

    Article Title: A minimum module for positioning the Chromosomal Passenger Complex at the cell center for cytokinesis
    Article Snippet: Eluted protein was further purified by size exclusion chromatography (SEC) using Superose 6 Increase 10/300 GL column (Cytiva, 29-0915-96) in buffer containing 50 mM Potassium Phosphate pH 8.0, 500 mM NaCl, 10% (v/v) glycerol, 100 μM ATP, 10 mM 2-Mercaptoethanol, 4 mM DTT, and 0.15% (v/v) Tween-20. .. Peak fractions were incubated with PreScission protease overnight at 4°C followed by incubation with Strep beads (Strep-Tactin Sepharose, IBA LifeSciences, 2-1201-010 and 2-1250-010) for 2-3 h at 4°C. .. Bound protein was eluted in buffer containing 50 mM Potassium Phosphate pH 8.0, 500 mM NaCl, 10% (v/v) glycerol, 100 μM ATP, 10 mM 2-Mercaptoethanol, 4 mM DTT, 0.15% (v/v) Tween-20 supplemented with 10 mM d-Desthiobiotin (Sigma-Aldrich, D1411).

    Article Title: Foot-and-mouth disease virus non-structural protein 2B downregulates the RLR signaling pathway via degradation of RIG-I and MDA5
    Article Snippet: Whole-cell lysates (WCL) were obtained after lysis with protease inhibitor cocktail- and phosphatase inhibitor cocktail (Sigma)-containing radioimmunoprecipitation assay (RIPA) lysis buffer (50 mM Tris-HCl, 150 mM NaCl, 0.5% sodium deoxycholate, 1% IGEPAL, 1 mM NaF, 1 mM Na3VO4) and sonication with a sonicator (Sonics). .. The WCLs were pre-cleared with Sepharose 6B (GE Life Sciences) at 4°C for 2 h. The pre-cleared whole cell lysates were incubated overnight with 2 μg target protein antibodies, 50% slurry of glutathione-conjugated Sepharose (GST) beads (Amersham Biosciences) or Strep beads (IBA Life Sciences) with agitation at 4°C. ..

    Enzyme-linked Immunosorbent Assay:

    Article Title: The CARD8 T60 variant associates with NLRP1 and negatively regulates its activation
    Article Snippet: .. The reagents used include Human IL-1β ELISA kit (BD Biosciences, 557953), anti-FLAG antibody (Sigma, F1804), anti-Strep (Biolegend, 688202), anti-GAPDH (ABclonal, AC002), anti-His (Sangon Biotech, D191001), anti-GFP (Abmart, M20004M), FLAG Beads (Sigma, A2220), Strep Beads (IBA, 2-1208-025), Z-VAD-FMK (APExBio, A1902), Val-boroPro (TargetMol, T4042), Disuccinimidyl suberate (DSS) (PIERCE, 21555). ..

    Article Title: CARD8 negatively regulates NLRP1 inflammasome activation level by interaction with NLRP1
    Article Snippet: .. The reagents used include Human IL-1β ELISA kit (BD Biosciences, 557953), anti-FLAG antibody (Sigma, F1804), anti-Strep (Biolegend, 688202), anti-GAPDH (ABclonal, AC002), anti-His (Sangon Biotech, D191001), anti-GFP (Abmart, M20004M), FLAG Beads (Sigma, A2220), Strep Beads (IBA, 2-1208-025), Z-VAD-FMK (APExBio, A1902), Val-boroPro (TargetMol, T4042), Disuccinimidyl suberate (DSS) (PIERCE, 21555). ..

    Homogenization:

    Article Title: C9orf72-catalyzed GTP loading of Rab39A enables HOPS-mediated membrane tethering and fusion in mammalian autophagy.
    Article Snippet: .. After homogenization in resuspension buffer (20mMTris-HCl, pH 7.5, 150mM NaCl, 1mM TECP, 0.5% NP-40 and protease inhibitor) and centrifugation (48,380 × g, 45min at 4 °C), the Flag affinity gel (Sigma) or Strep beads (IBA) were used to bind proteins in supernatant. ..

    Protease Inhibitor:

    Article Title: C9orf72-catalyzed GTP loading of Rab39A enables HOPS-mediated membrane tethering and fusion in mammalian autophagy.
    Article Snippet: .. After homogenization in resuspension buffer (20mMTris-HCl, pH 7.5, 150mM NaCl, 1mM TECP, 0.5% NP-40 and protease inhibitor) and centrifugation (48,380 × g, 45min at 4 °C), the Flag affinity gel (Sigma) or Strep beads (IBA) were used to bind proteins in supernatant. ..

    Centrifugation:

    Article Title: C9orf72-catalyzed GTP loading of Rab39A enables HOPS-mediated membrane tethering and fusion in mammalian autophagy.
    Article Snippet: .. After homogenization in resuspension buffer (20mMTris-HCl, pH 7.5, 150mM NaCl, 1mM TECP, 0.5% NP-40 and protease inhibitor) and centrifugation (48,380 × g, 45min at 4 °C), the Flag affinity gel (Sigma) or Strep beads (IBA) were used to bind proteins in supernatant. ..

    Article Title: The non-canonical poly(A) polymerase FAM46C promotes erythropoiesis.
    Article Snippet: The post-transcriptional regulation of mRNA is a crucial component of gene expression.. The disruption of this process has detrimental effects on the normal development and gives rise to various diseases.. Searching for novel post-transcriptional regulators and exploring their roles are essential for understanding development and disease.

    other:

    Article Title: O -GlcNAc modification of leucyl-tRNA synthetase 1 integrates leucine and glucose availability to regulate mTORC1 and the metabolic fate of leucine
    Article Snippet: After washing five times with Buffer W (Strep Tag Washing Buffer, IBA Life Sciences, #2-1003-100), strep-bound proteins were eluted with buffer BXT (D-Desthiobiotin Buffer E, IBA Life Sciences, #2-1000-025).



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    Western blot (A) and silver-stained gel (B) show the purification fractions of the WT control (WT/WT), bait/WT experiment (bait/WT), and bait control (bait/bait), all crosslinked with 0.2% (w/v) FA. The fractions loaded are lysate (L) (1 μL), flowthrough (FT) (1 μL), wash steps 1 (W1) and 3 (W3) (8 μL), eluate (E) (4 μL), and residue (R) (4 μL). The Chameleon ® Due Pre-Stained protein marker was used for molecular weight reference. The position of the signals for PycA (127.72 kDa) and SigA-TS (45.9 kDa) is marked on the right side. PycA is a biotinylated protein and thus is purified unspecifically by the <t>MagStrep</t> beads.
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    Western blot (A) and silver-stained gel (B) show the purification fractions of the WT control (WT/WT), bait/WT experiment (bait/WT), and bait control (bait/bait), all crosslinked with 0.2% (w/v) FA. The fractions loaded are lysate (L) (1 μL), flowthrough (FT) (1 μL), wash steps 1 (W1) and 3 (W3) (8 μL), eluate (E) (4 μL), and residue (R) (4 μL). The Chameleon ® Due Pre-Stained protein marker was used for molecular weight reference. The position of the signals for PycA (127.72 kDa) and SigA-TS (45.9 kDa) is marked on the right side. PycA is a biotinylated protein and thus is purified unspecifically by the <t>MagStrep</t> beads.
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    Western blot (A) and silver-stained gel (B) show the purification fractions of the WT control (WT/WT), bait/WT experiment (bait/WT), and bait control (bait/bait), all crosslinked with 0.2% (w/v) FA. The fractions loaded are lysate (L) (1 μL), flowthrough (FT) (1 μL), wash steps 1 (W1) and 3 (W3) (8 μL), eluate (E) (4 μL), and residue (R) (4 μL). The Chameleon ® Due Pre-Stained protein marker was used for molecular weight reference. The position of the signals for PycA (127.72 kDa) and SigA-TS (45.9 kDa) is marked on the right side. PycA is a biotinylated protein and thus is purified unspecifically by the <t>MagStrep</t> beads.
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    IBA Lifesciences streptactin agarose beads
    Panel a: Co-expressed BrxB Aci , BrxC Aci 1-551 and strep-tagged PglZ Aci were affinity purified by <t>streptactin</t> chromatography followed by SEC (left trace). All three proteins remain associated through this purification scheme (SDS PAGE, right). Panel b: Mass photometry analyses of the purified BrxB Aci :PglZ Aci dimeric complex (‘B:Z’) incubated with either BrxC Aci 1-551 and ATPψS (gray) or BrxC Aci (E269Q) 1-551 and ATP (orange). The predicted mass of the B:Z complex is 122 kDa and that of the C 1-551 monomer is 66 kDa. Complexes consistent with B:Z:(C 1-551 ) 1 and B:Z:(C 1-551 ) 2 stoichiometries are observed. Panel c: X-ray crystallographic structure of a complex consisting of dimeric BrxC Aci (E269Q) 1-551 , full-length BrxB Aci and PglZ Aci 1-98 . The BrxC-BrxC interface and the BrxB-BrxC interface (boxes and insets) involve comparable residues that bind a single copy of ATP between the corresponding protein subunits.
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    Panel a: Co-expressed BrxB Aci , BrxC Aci 1-551 and strep-tagged PglZ Aci were affinity purified by <t>streptactin</t> chromatography followed by SEC (left trace). All three proteins remain associated through this purification scheme (SDS PAGE, right). Panel b: Mass photometry analyses of the purified BrxB Aci :PglZ Aci dimeric complex (‘B:Z’) incubated with either BrxC Aci 1-551 and ATPψS (gray) or BrxC Aci (E269Q) 1-551 and ATP (orange). The predicted mass of the B:Z complex is 122 kDa and that of the C 1-551 monomer is 66 kDa. Complexes consistent with B:Z:(C 1-551 ) 1 and B:Z:(C 1-551 ) 2 stoichiometries are observed. Panel c: X-ray crystallographic structure of a complex consisting of dimeric BrxC Aci (E269Q) 1-551 , full-length BrxB Aci and PglZ Aci 1-98 . The BrxC-BrxC interface and the BrxB-BrxC interface (boxes and insets) involve comparable residues that bind a single copy of ATP between the corresponding protein subunits.
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    IBA Lifesciences streptactin beads
    Panel a: Co-expressed BrxB Aci , BrxC Aci 1-551 and strep-tagged PglZ Aci were affinity purified by <t>streptactin</t> chromatography followed by SEC (left trace). All three proteins remain associated through this purification scheme (SDS PAGE, right). Panel b: Mass photometry analyses of the purified BrxB Aci :PglZ Aci dimeric complex (‘B:Z’) incubated with either BrxC Aci 1-551 and ATPψS (gray) or BrxC Aci (E269Q) 1-551 and ATP (orange). The predicted mass of the B:Z complex is 122 kDa and that of the C 1-551 monomer is 66 kDa. Complexes consistent with B:Z:(C 1-551 ) 1 and B:Z:(C 1-551 ) 2 stoichiometries are observed. Panel c: X-ray crystallographic structure of a complex consisting of dimeric BrxC Aci (E269Q) 1-551 , full-length BrxB Aci and PglZ Aci 1-98 . The BrxC-BrxC interface and the BrxB-BrxC interface (boxes and insets) involve comparable residues that bind a single copy of ATP between the corresponding protein subunits.
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    Image Search Results


    Western blot (A) and silver-stained gel (B) show the purification fractions of the WT control (WT/WT), bait/WT experiment (bait/WT), and bait control (bait/bait), all crosslinked with 0.2% (w/v) FA. The fractions loaded are lysate (L) (1 μL), flowthrough (FT) (1 μL), wash steps 1 (W1) and 3 (W3) (8 μL), eluate (E) (4 μL), and residue (R) (4 μL). The Chameleon ® Due Pre-Stained protein marker was used for molecular weight reference. The position of the signals for PycA (127.72 kDa) and SigA-TS (45.9 kDa) is marked on the right side. PycA is a biotinylated protein and thus is purified unspecifically by the MagStrep beads.

    Journal: Bio-protocol

    Article Title: TIE-UP-SIN: A Method for Enhanced Identification of Protein–Protein Interactions

    doi: 10.21769/BioProtoc.5663

    Figure Lengend Snippet: Western blot (A) and silver-stained gel (B) show the purification fractions of the WT control (WT/WT), bait/WT experiment (bait/WT), and bait control (bait/bait), all crosslinked with 0.2% (w/v) FA. The fractions loaded are lysate (L) (1 μL), flowthrough (FT) (1 μL), wash steps 1 (W1) and 3 (W3) (8 μL), eluate (E) (4 μL), and residue (R) (4 μL). The Chameleon ® Due Pre-Stained protein marker was used for molecular weight reference. The position of the signals for PycA (127.72 kDa) and SigA-TS (45.9 kDa) is marked on the right side. PycA is a biotinylated protein and thus is purified unspecifically by the MagStrep beads.

    Article Snippet: MagStrep ® Strep-Tactin ® XT beads (IBA Lifesciences, catalog number: 2-5090-010) 14.

    Techniques: Western Blot, Staining, Purification, Control, Residue, Marker, Molecular Weight

    Panel a: Co-expressed BrxB Aci , BrxC Aci 1-551 and strep-tagged PglZ Aci were affinity purified by streptactin chromatography followed by SEC (left trace). All three proteins remain associated through this purification scheme (SDS PAGE, right). Panel b: Mass photometry analyses of the purified BrxB Aci :PglZ Aci dimeric complex (‘B:Z’) incubated with either BrxC Aci 1-551 and ATPψS (gray) or BrxC Aci (E269Q) 1-551 and ATP (orange). The predicted mass of the B:Z complex is 122 kDa and that of the C 1-551 monomer is 66 kDa. Complexes consistent with B:Z:(C 1-551 ) 1 and B:Z:(C 1-551 ) 2 stoichiometries are observed. Panel c: X-ray crystallographic structure of a complex consisting of dimeric BrxC Aci (E269Q) 1-551 , full-length BrxB Aci and PglZ Aci 1-98 . The BrxC-BrxC interface and the BrxB-BrxC interface (boxes and insets) involve comparable residues that bind a single copy of ATP between the corresponding protein subunits.

    Journal: bioRxiv

    Article Title: Competing forms of protein-protein association and DNA binding exhibited by BrxC from the BREX phage restriction system

    doi: 10.64898/2026.04.09.717308

    Figure Lengend Snippet: Panel a: Co-expressed BrxB Aci , BrxC Aci 1-551 and strep-tagged PglZ Aci were affinity purified by streptactin chromatography followed by SEC (left trace). All three proteins remain associated through this purification scheme (SDS PAGE, right). Panel b: Mass photometry analyses of the purified BrxB Aci :PglZ Aci dimeric complex (‘B:Z’) incubated with either BrxC Aci 1-551 and ATPψS (gray) or BrxC Aci (E269Q) 1-551 and ATP (orange). The predicted mass of the B:Z complex is 122 kDa and that of the C 1-551 monomer is 66 kDa. Complexes consistent with B:Z:(C 1-551 ) 1 and B:Z:(C 1-551 ) 2 stoichiometries are observed. Panel c: X-ray crystallographic structure of a complex consisting of dimeric BrxC Aci (E269Q) 1-551 , full-length BrxB Aci and PglZ Aci 1-98 . The BrxC-BrxC interface and the BrxB-BrxC interface (boxes and insets) involve comparable residues that bind a single copy of ATP between the corresponding protein subunits.

    Article Snippet: Streptactin agarose beads (IBA Lifesciences Inc., cat # 2-1250-002) were prepared by pipetting 12 μl of a 50% slurry into a 0.6 ml Eppendorf tube and centrifuged at 2000 x g for 1 min.

    Techniques: Affinity Purification, Chromatography, Purification, SDS Page, Incubation

    Panel a, left: Co-expression of BrxB Aci , strep-tagged PglZ Aci and full-length BrxC Aci demonstrates co-elution of all three subunits by streptactin affinity purification (WC: Whole cell lysate; Sol: filtered soluble lysate; FT: affinity column flow-through). Panel a, right: The streptacin-eluted B:C:Z complex largely dissociates on SEC into BrxC Aci dimers and the B Aci :Z Aci complex. Panel b: Low resolution cryo-EM analysis of particles corresponding to a complex between a BrxC Aci 1-551 -BrxB Aci fusion (teal and red cartoon elements, respectively) and a separate full-length PglZ Aci subunit (blue cartoon) produces a density envelope that agrees closely with a generated predictive model of a BrxC 1-551 -BrxB:PglZ dimer, with the complex held together via interactions between separate ends of each PglZ subunit. Panel c: ATPase assays of BrxB Aci :PglZ Aci and indicated BrxC Aci constructs, comparing each protein alone, or incubated together at 1 µM concentration.

    Journal: bioRxiv

    Article Title: Competing forms of protein-protein association and DNA binding exhibited by BrxC from the BREX phage restriction system

    doi: 10.64898/2026.04.09.717308

    Figure Lengend Snippet: Panel a, left: Co-expression of BrxB Aci , strep-tagged PglZ Aci and full-length BrxC Aci demonstrates co-elution of all three subunits by streptactin affinity purification (WC: Whole cell lysate; Sol: filtered soluble lysate; FT: affinity column flow-through). Panel a, right: The streptacin-eluted B:C:Z complex largely dissociates on SEC into BrxC Aci dimers and the B Aci :Z Aci complex. Panel b: Low resolution cryo-EM analysis of particles corresponding to a complex between a BrxC Aci 1-551 -BrxB Aci fusion (teal and red cartoon elements, respectively) and a separate full-length PglZ Aci subunit (blue cartoon) produces a density envelope that agrees closely with a generated predictive model of a BrxC 1-551 -BrxB:PglZ dimer, with the complex held together via interactions between separate ends of each PglZ subunit. Panel c: ATPase assays of BrxB Aci :PglZ Aci and indicated BrxC Aci constructs, comparing each protein alone, or incubated together at 1 µM concentration.

    Article Snippet: Streptactin agarose beads (IBA Lifesciences Inc., cat # 2-1250-002) were prepared by pipetting 12 μl of a 50% slurry into a 0.6 ml Eppendorf tube and centrifuged at 2000 x g for 1 min.

    Techniques: Expressing, Co-Elution Assay, Affinity Purification, Affinity Column, Cryo-EM Sample Prep, Generated, Construct, Incubation, Concentration Assay