E coli bl21

Manufactured by Qiagen

Sourced in Germany, United States

E. coli BL21 is a bacterial strain commonly used in molecular biology laboratories. It is a non-pathogenic strain of Escherichia coli that is optimized for recombinant protein expression. The BL21 strain is known for its high efficiency in producing target proteins and is widely used in various research and industrial applications.

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Lab products found in correlation

Escherichia coli top10, by Thermo Fisher Scientific (1 mentions) Guanidine hydrochloride, by Avantor (1 mentions) Rhtpo, by Thermo Fisher Scientific (1 mentions) Pqe 60 plasmid, by Qiagen (1 mentions) Stempro 34 sfm medium, by Thermo Fisher Scientific (1 mentions) Macs immunomagnetic absorption column separation device, by Miltenyi Biotec (1 mentions) Rpmi 1640 medium, by Thermo Fisher Scientific (1 mentions) Cd34 microbead kit, by Miltenyi Biotec (1 mentions) Pqe60, by Qiagen (1 mentions) Prep4, by Qiagen (1 mentions) Isopropyl β d 1 thiogalactopyranoside iptg, by Merck Group (1 mentions) Quick start bradford protein assay, by Bio-Rad (1 mentions) Ni nta agarose, by Qiagen (1 mentions) Ni nta, by Qiagen (1 mentions)

Spelling variants of this product

E. coli BL21(DE3) (3 citations)

4 protocols using e coli bl21

Bacterial Expression System for Viral Proteins

Cited 1 time

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Escherichia coli TOP10 (Thermo Fisher Scientific, Waltham, MA, USA) was generally used to clone genes. E. coli BL21 (Qiagen, Hilden, Germany) and M15 (Qiagen) strains were used to prepare the purified antigen for each viral capsid protein. S. cerevisiae 2805 (MATa pep4::HIS3 prb1-Δcan1 GAL2 his3 ura3-52) was the yeast strain used for heterologous expression. Yeast and bacterial strains were cultured, as previously described (So et al. 2021 (link)).

Le N.M., So K.K., Chun J, & Kim D.H. (2024). Expression of virus-like particles (VLPs) of foot-and-mouth disease virus (FMDV) using Saccharomyces cerevisiae. Applied Microbiology and Biotechnology, 108(1), 81.

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Recombinant SCF Expression in E. coli

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The PQE60 plasmid and E.Coli BL 21 were obtained from QIAGEN (Valencia, CA, USA). Isopropyl-1-thio-ß- D-galactopyranoside (IPTG) was from Bio-Basic Inc (Amherst, NY, USA) to induce recombinant SCF expression in bacteria. Guanidine Hydrochloride was from Amresco Inc (Solon, OH, USA). Urea was from Shanghai Experimental Reagent Inc (Shanghai, China). RPMI 1640 medium and STEM PRO®-34 SFM medium were from Gibco (Grand Island, NY, USA). Fetal bovine serum was from Hyclone (Logan, UT, USA). Goat-anti-mouse immunoglobulin G (IgG) conjugated with alkaline phosphatase was from Biolegend (Canada). Prestained protein molecular weight marker was from Bio-Rad (USA). Biotin conjugated goat anti-mouse-IgG was from Biolegend (San Diego, CA, USA). Mouse monoclonal antibody isotyping reagent kit and streptavidin-peroxidase was from Sigma-Aldrich (St. Louis, MO, USA). MACS immunomagnetic absorption column separation device and CD34 MicroBead Kit, was from Miltenyi Biotec (Germany). rhTPO and rhFLT-3 were from Pepro Tech (USA). Anti-human CD34 mAb conjugated with phycoerythrin was from Immunotec (Canada). Peptides were synthesized by Nanjing Genscript Inc. (Nanjing, China).

Shen B., Jiang W., Fan J., Dai W., Ding X, & Jiang Y. (2015). Residues 39-56 of Stem Cell Factor Protein Sequence Are Capable of Stimulating the Expansion of Cord Blood CD34+ Cells. PLoS ONE, 10(10), e0141485.

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Recombinant EspA, EspB, and Intimin-β Proteins

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The full nucleotide coding regions of EspA and EspB were amplified using the sets of primers pQE60-EspA and pQE60-EspB, respectively (see Key Resources Table), and then cloned into the plasmid pQE60 (QIAGEN). The plasmid p6his-Intb385 containing the DNA region encoding the extracellular C-terminal 385 amino acids of Intimin-β (6xHis-tagged-Intimin-β₃₈₅) cloned into the vector pQE32 was kindly provided by Alison D. O’Brien (Sinclair and O’Brien, 2004 (link)). The recombinant plasmids were transformed into E. coli BL21 containing the plasmid pREP4 (QIAGEN) and protein overexpression was induced by adding 1mM isopropyl β-D-1-thiogalactopyranoside (IPTG; Sigma-Aldrich) into the bacterial cultures. Recombinant proteins were purified under denaturing conditions using nickel nitrilotriacetic acid (Ni-NTA) agarose (QIAGEN), and then dialyzed in PBS 1X. Protein concentration was determined using the Quick Start Bradford Protein Assay (Bio-Rad) and the purity of the samples was analyzed by electrophoresis into 12% SDS-PAGE. Aliquots of the proteins were stored at −20°C until use.

Caballero-Flores G., Sakamoto K., Zeng M., Wang Y., Hakim J., Matus-Acuña V., Inohara N, & Núñez G. (2019). Maternal immunization confers protection to the offspring against an attaching and effacing pathogen through delivery of IgG in breast milk. Cell host & microbe, 25(2), 313-323.e4.

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High-Throughput SIRT1 Activity Assay

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The prokaryotic expression vector of truncated SIRT1(193-747AA) was constructed with SIRT1 cDNA from Prof Hou-Zao Chen (Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences & Peking Union Medical College). Then the SIRT1 recombinant was induced and purified in E.Coli Bl21(DE3) and Ni-NTA(Qiagen). The peptide substrate used in the screening model was synthesized according to p53 sequence; it was comprised of ε-acetylated lysine and a conjoined 4-methyl-7-amide-coumarin moiety (AMC) at the carboxyl terminus of the RHKK sequence. The screening method contains two enzymatic catalysis reactions. Firstly, the peptide substrate is incubated with human recombinant SIRT1 along with its cofactor NAD+. Once the acetyl group is released form the peptide, the substrate can be recognized by trypsin in the second step, following by the release of the AMC fluorescence moiety. Finally, the free fluorophore can be detected using an excitation wavelength of 360nm and an emission wavelength of 460 nm. The reactions were suited to high-throughput screening, and the assay was performed in the 96-well microplate [28] [29] [30] .

Zheng Y.C., Wang L.Z., Zhao L.J., Zhao L.J., Zhan Q.N., Ma J.L., Zhang B., Wang M.M., Wang Z.R., Li J.F., Liu Y., Chen Z.S., Shen D.D., Liu X.Q., Ren M., Lv W.L., Zhao W., Duan Y.C, & Liu H.M. (2016). 1,2,3-Triazole-Dithiocarbamate Hybrids, a Group of Novel Cell Active SIRT1 Inhibitors. Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology, 38(1).

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