Review



e coli bl21 de3 cells  (Formedium)

 
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
    • 86
      Buy from Supplier

    Structured Review

    Formedium e coli bl21 de3 cells
    (A) Structure of the MutL-MutH-DNA complex. MutL LN40 is coloured in light and dark green, MutH in purple, and the DNA in orange. (B) Structure of MutL LN40 bound to a 5′ extended single stranded DNA (PDB ID: 7P8V). In this structure, the single-stranded DNA overhang is located in the same groove as MutH in the MutL-MutH-DNA complex, indicting that MutL LN40 cannot bind MutH and DNA simultaneously. (C) Superposition of three MutL LN40 structures in different functional states: apo, ssDNA-bound, and MutH-bound. The changes in the groove between the two monomers are highlighted by helices 265–281 and 313–331. The width of the groove ranges from 14 Å in the ssDNA-bound structure (blue, PDB ID: 7P8V), to 21 Å in the apo structure (orange, PDB ID: 1B63), to 28 Å in the MutH-bound structure (green, this work. (D) Conservation analysis of MutH from H. influenzae and <t>E.</t> <t>coli</t> mapped onto the E. coli MutH structure. Highly conserved residues are shown in magenta, and lesser conserved residues in blue. The strong conservation of the DNA-binding site supports the use of the available H. influenzae MutH-DNA structure (PDB ID: 2AOR) as a structural reference for comparison with our E. coli MutL-bound MutH complex.
    E Coli Bl21 De3 Cells, supplied by Formedium, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/e+coli+bl21+de3+cells/bio_rxiv__64898__2026__04__21__719898-32-5-14?v=Formedium
    Average 86 stars, based on 1 article reviews
    e coli bl21 de3 cells - by Bioz Stars, 2026-08
    86/100 stars

    Images

    1) Product Images from "Cryo-EM structure of MutL-activated MutH"

    Article Title: Cryo-EM structure of MutL-activated MutH

    Journal: bioRxiv

    doi: 10.64898/2026.04.21.719898

    (A) Structure of the MutL-MutH-DNA complex. MutL LN40 is coloured in light and dark green, MutH in purple, and the DNA in orange. (B) Structure of MutL LN40 bound to a 5′ extended single stranded DNA (PDB ID: 7P8V). In this structure, the single-stranded DNA overhang is located in the same groove as MutH in the MutL-MutH-DNA complex, indicting that MutL LN40 cannot bind MutH and DNA simultaneously. (C) Superposition of three MutL LN40 structures in different functional states: apo, ssDNA-bound, and MutH-bound. The changes in the groove between the two monomers are highlighted by helices 265–281 and 313–331. The width of the groove ranges from 14 Å in the ssDNA-bound structure (blue, PDB ID: 7P8V), to 21 Å in the apo structure (orange, PDB ID: 1B63), to 28 Å in the MutH-bound structure (green, this work. (D) Conservation analysis of MutH from H. influenzae and E. coli mapped onto the E. coli MutH structure. Highly conserved residues are shown in magenta, and lesser conserved residues in blue. The strong conservation of the DNA-binding site supports the use of the available H. influenzae MutH-DNA structure (PDB ID: 2AOR) as a structural reference for comparison with our E. coli MutL-bound MutH complex.
    Figure Legend Snippet: (A) Structure of the MutL-MutH-DNA complex. MutL LN40 is coloured in light and dark green, MutH in purple, and the DNA in orange. (B) Structure of MutL LN40 bound to a 5′ extended single stranded DNA (PDB ID: 7P8V). In this structure, the single-stranded DNA overhang is located in the same groove as MutH in the MutL-MutH-DNA complex, indicting that MutL LN40 cannot bind MutH and DNA simultaneously. (C) Superposition of three MutL LN40 structures in different functional states: apo, ssDNA-bound, and MutH-bound. The changes in the groove between the two monomers are highlighted by helices 265–281 and 313–331. The width of the groove ranges from 14 Å in the ssDNA-bound structure (blue, PDB ID: 7P8V), to 21 Å in the apo structure (orange, PDB ID: 1B63), to 28 Å in the MutH-bound structure (green, this work. (D) Conservation analysis of MutH from H. influenzae and E. coli mapped onto the E. coli MutH structure. Highly conserved residues are shown in magenta, and lesser conserved residues in blue. The strong conservation of the DNA-binding site supports the use of the available H. influenzae MutH-DNA structure (PDB ID: 2AOR) as a structural reference for comparison with our E. coli MutL-bound MutH complex.

    Techniques Used: Functional Assay, Binding Assay, Comparison



    Similar Products

    e coli bl21 de3 competent cells  (New England Biolabs)
    99
    New England Biolabs e coli bl21 de3 competent cells
    E Coli Bl21 De3 Competent Cells, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/e+coli+bl21+de3+cells/pm42047214-247-5-11?v=New+England+Biolabs
    Average 99 stars, based on 1 article reviews
    e coli bl21 de3 competent cells - by Bioz Stars, 2026-08
    99/100 stars
    		  Buy from Supplier
    e coli bl21 de3 competent cells  (Sangon Biotech)
    86
    Sangon Biotech e coli bl21 de3 competent cells
    E Coli Bl21 De3 Competent Cells, supplied by Sangon Biotech, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/e+coli+bl21+de3+cells/pm42257678-212-0-25?v=Sangon+Biotech
    Average 86 stars, based on 1 article reviews
    e coli bl21 de3 competent cells - by Bioz Stars, 2026-08
    86/100 stars
    		  Buy from Supplier
    bl21 de3 e coli competent cells  (Sangon Biotech)
    86
    Sangon Biotech bl21 de3 e coli competent cells
    Construction of engineered E. coli strains and protein purification. (A) PCR identification of positive E. coli clones. Lanes 1–3 correspond to BL21-pET28-ST-PCV2 Cap, BL21-pET28-ST-PCV3 Cap, and BL21-pET28-SC-mi3, respectively. (B–D) Expression and purification of recombinant proteins ST-PCV2 Cap, ST-PCV3 Cap, and SC-mi3, respectively. Lanes 1–6 represent whole bacterial lysate, pellet after sonication, supernatant after sonication, Ni column flow-through, wash fraction, and purified protein, respectively. (E) Western blot validation of antigen proteins. Lanes 1, 2 correspond to ST-PCV2 Cap and ST-PCV3 Cap, respectively. (F) Endotoxin removal from recombinant protein solutions. Color intensity represents endotoxin content; numbers indicate endotoxin content (EU/mL).
    Bl21 De3 E Coli Competent Cells, supplied by Sangon Biotech, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/e+coli+bl21+de3+cells/pmc13280793-36-8-16?v=Sangon+Biotech
    Average 86 stars, based on 1 article reviews
    bl21 de3 e coli competent cells - by Bioz Stars, 2026-08
    86/100 stars
    		  Buy from Supplier
    e coli bl21 de3 cells  (Sangon Biotech)
    86
    Sangon Biotech e coli bl21 de3 cells
    Construction of engineered E. coli strains and protein purification. (A) PCR identification of positive E. coli clones. Lanes 1–3 correspond to BL21-pET28-ST-PCV2 Cap, BL21-pET28-ST-PCV3 Cap, and BL21-pET28-SC-mi3, respectively. (B–D) Expression and purification of recombinant proteins ST-PCV2 Cap, ST-PCV3 Cap, and SC-mi3, respectively. Lanes 1–6 represent whole bacterial lysate, pellet after sonication, supernatant after sonication, Ni column flow-through, wash fraction, and purified protein, respectively. (E) Western blot validation of antigen proteins. Lanes 1, 2 correspond to ST-PCV2 Cap and ST-PCV3 Cap, respectively. (F) Endotoxin removal from recombinant protein solutions. Color intensity represents endotoxin content; numbers indicate endotoxin content (EU/mL).
    E Coli Bl21 De3 Cells, supplied by Sangon Biotech, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/e+coli+bl21+de3+cells/pmc13018976-38-19-23?v=Sangon+Biotech
    Average 86 stars, based on 1 article reviews
    e coli bl21 de3 cells - by Bioz Stars, 2026-08
    86/100 stars
    		  Buy from Supplier
    hicontrol e coli bl21 de3 cells  (Lucigen Corp)
    86
    Lucigen Corp hicontrol e coli bl21 de3 cells
    Construction of engineered E. coli strains and protein purification. (A) PCR identification of positive E. coli clones. Lanes 1–3 correspond to BL21-pET28-ST-PCV2 Cap, BL21-pET28-ST-PCV3 Cap, and BL21-pET28-SC-mi3, respectively. (B–D) Expression and purification of recombinant proteins ST-PCV2 Cap, ST-PCV3 Cap, and SC-mi3, respectively. Lanes 1–6 represent whole bacterial lysate, pellet after sonication, supernatant after sonication, Ni column flow-through, wash fraction, and purified protein, respectively. (E) Western blot validation of antigen proteins. Lanes 1, 2 correspond to ST-PCV2 Cap and ST-PCV3 Cap, respectively. (F) Endotoxin removal from recombinant protein solutions. Color intensity represents endotoxin content; numbers indicate endotoxin content (EU/mL).
    Hicontrol E Coli Bl21 De3 Cells, supplied by Lucigen Corp, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/e+coli+bl21+de3+cells/pm42162590-73-10-15?v=Lucigen+Corp
    Average 86 stars, based on 1 article reviews
    hicontrol e coli bl21 de3 cells - by Bioz Stars, 2026-08
    86/100 stars
    		  Buy from Supplier
    e coli bl21 de3 plyss cells  (Thermo Fisher)
    99
    Thermo Fisher e coli bl21 de3 plyss cells
    Construction of engineered E. coli strains and protein purification. (A) PCR identification of positive E. coli clones. Lanes 1–3 correspond to BL21-pET28-ST-PCV2 Cap, BL21-pET28-ST-PCV3 Cap, and BL21-pET28-SC-mi3, respectively. (B–D) Expression and purification of recombinant proteins ST-PCV2 Cap, ST-PCV3 Cap, and SC-mi3, respectively. Lanes 1–6 represent whole bacterial lysate, pellet after sonication, supernatant after sonication, Ni column flow-through, wash fraction, and purified protein, respectively. (E) Western blot validation of antigen proteins. Lanes 1, 2 correspond to ST-PCV2 Cap and ST-PCV3 Cap, respectively. (F) Endotoxin removal from recombinant protein solutions. Color intensity represents endotoxin content; numbers indicate endotoxin content (EU/mL).
    E Coli Bl21 De3 Plyss Cells, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/e+coli+bl21+de3+cells/us12618081-1594-3-9?v=Thermo+Fisher
    Average 99 stars, based on 1 article reviews
    e coli bl21 de3 plyss cells - by Bioz Stars, 2026-08
    99/100 stars
    		  Buy from Supplier
    e coli bl21 de3 cells  (Formedium)
    86
    Formedium e coli bl21 de3 cells
    (A) Structure of the MutL-MutH-DNA complex. MutL LN40 is coloured in light and dark green, MutH in purple, and the DNA in orange. (B) Structure of MutL LN40 bound to a 5′ extended single stranded DNA (PDB ID: 7P8V). In this structure, the single-stranded DNA overhang is located in the same groove as MutH in the MutL-MutH-DNA complex, indicting that MutL LN40 cannot bind MutH and DNA simultaneously. (C) Superposition of three MutL LN40 structures in different functional states: apo, ssDNA-bound, and MutH-bound. The changes in the groove between the two monomers are highlighted by helices 265–281 and 313–331. The width of the groove ranges from 14 Å in the ssDNA-bound structure (blue, PDB ID: 7P8V), to 21 Å in the apo structure (orange, PDB ID: 1B63), to 28 Å in the MutH-bound structure (green, this work. (D) Conservation analysis of MutH from H. influenzae and <t>E.</t> <t>coli</t> mapped onto the E. coli MutH structure. Highly conserved residues are shown in magenta, and lesser conserved residues in blue. The strong conservation of the DNA-binding site supports the use of the available H. influenzae MutH-DNA structure (PDB ID: 2AOR) as a structural reference for comparison with our E. coli MutL-bound MutH complex.
    E Coli Bl21 De3 Cells, supplied by Formedium, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/e+coli+bl21+de3+cells/bio_rxiv__64898__2026__04__21__719898-32-5-14?v=Formedium
    Average 86 stars, based on 1 article reviews
    e coli bl21 de3 cells - by Bioz Stars, 2026-08
    86/100 stars
    		  Buy from Supplier

    Image Search Results


    Construction of engineered E. coli strains and protein purification. (A) PCR identification of positive E. coli clones. Lanes 1–3 correspond to BL21-pET28-ST-PCV2 Cap, BL21-pET28-ST-PCV3 Cap, and BL21-pET28-SC-mi3, respectively. (B–D) Expression and purification of recombinant proteins ST-PCV2 Cap, ST-PCV3 Cap, and SC-mi3, respectively. Lanes 1–6 represent whole bacterial lysate, pellet after sonication, supernatant after sonication, Ni column flow-through, wash fraction, and purified protein, respectively. (E) Western blot validation of antigen proteins. Lanes 1, 2 correspond to ST-PCV2 Cap and ST-PCV3 Cap, respectively. (F) Endotoxin removal from recombinant protein solutions. Color intensity represents endotoxin content; numbers indicate endotoxin content (EU/mL).

    Journal: Frontiers in Veterinary Science

    Article Title: Construction and immunogenicity evaluation of a bivalent nanoparticle based on mi3 displaying porcine circovirus type 2 and type 3 capsid proteins

    doi: 10.3389/fvets.2026.1862938

    Figure Lengend Snippet: Construction of engineered E. coli strains and protein purification. (A) PCR identification of positive E. coli clones. Lanes 1–3 correspond to BL21-pET28-ST-PCV2 Cap, BL21-pET28-ST-PCV3 Cap, and BL21-pET28-SC-mi3, respectively. (B–D) Expression and purification of recombinant proteins ST-PCV2 Cap, ST-PCV3 Cap, and SC-mi3, respectively. Lanes 1–6 represent whole bacterial lysate, pellet after sonication, supernatant after sonication, Ni column flow-through, wash fraction, and purified protein, respectively. (E) Western blot validation of antigen proteins. Lanes 1, 2 correspond to ST-PCV2 Cap and ST-PCV3 Cap, respectively. (F) Endotoxin removal from recombinant protein solutions. Color intensity represents endotoxin content; numbers indicate endotoxin content (EU/mL).

    Article Snippet: The pET28a(+) plasmid for recombinant protein expression and BL21(DE3) E. coli competent cells were purchased from Sangon Biotech (Shanghai) Co., Ltd.

    Techniques: Protein Purification, Clone Assay, Expressing, Purification, Recombinant, Sonication, Western Blot, Biomarker Discovery

    (A) Structure of the MutL-MutH-DNA complex. MutL LN40 is coloured in light and dark green, MutH in purple, and the DNA in orange. (B) Structure of MutL LN40 bound to a 5′ extended single stranded DNA (PDB ID: 7P8V). In this structure, the single-stranded DNA overhang is located in the same groove as MutH in the MutL-MutH-DNA complex, indicting that MutL LN40 cannot bind MutH and DNA simultaneously. (C) Superposition of three MutL LN40 structures in different functional states: apo, ssDNA-bound, and MutH-bound. The changes in the groove between the two monomers are highlighted by helices 265–281 and 313–331. The width of the groove ranges from 14 Å in the ssDNA-bound structure (blue, PDB ID: 7P8V), to 21 Å in the apo structure (orange, PDB ID: 1B63), to 28 Å in the MutH-bound structure (green, this work. (D) Conservation analysis of MutH from H. influenzae and E. coli mapped onto the E. coli MutH structure. Highly conserved residues are shown in magenta, and lesser conserved residues in blue. The strong conservation of the DNA-binding site supports the use of the available H. influenzae MutH-DNA structure (PDB ID: 2AOR) as a structural reference for comparison with our E. coli MutL-bound MutH complex.

    Journal: bioRxiv

    Article Title: Cryo-EM structure of MutL-activated MutH

    doi: 10.64898/2026.04.21.719898

    Figure Lengend Snippet: (A) Structure of the MutL-MutH-DNA complex. MutL LN40 is coloured in light and dark green, MutH in purple, and the DNA in orange. (B) Structure of MutL LN40 bound to a 5′ extended single stranded DNA (PDB ID: 7P8V). In this structure, the single-stranded DNA overhang is located in the same groove as MutH in the MutL-MutH-DNA complex, indicting that MutL LN40 cannot bind MutH and DNA simultaneously. (C) Superposition of three MutL LN40 structures in different functional states: apo, ssDNA-bound, and MutH-bound. The changes in the groove between the two monomers are highlighted by helices 265–281 and 313–331. The width of the groove ranges from 14 Å in the ssDNA-bound structure (blue, PDB ID: 7P8V), to 21 Å in the apo structure (orange, PDB ID: 1B63), to 28 Å in the MutH-bound structure (green, this work. (D) Conservation analysis of MutH from H. influenzae and E. coli mapped onto the E. coli MutH structure. Highly conserved residues are shown in magenta, and lesser conserved residues in blue. The strong conservation of the DNA-binding site supports the use of the available H. influenzae MutH-DNA structure (PDB ID: 2AOR) as a structural reference for comparison with our E. coli MutL-bound MutH complex.

    Article Snippet: All proteins were expressed in E. coli BL21(DE3) cells grown in 2x YT media (Formedium, UK) at 30 °C.

    Techniques: Functional Assay, Binding Assay, Comparison