메뉴 건너뛰기




Volumn 151, Issue 4, 2011, Pages 295-302

A simple method for production and purification of soluble and biologically active recombinant human leukemia inhibitory factor (hLIF) fusion protein in Escherichia coli

Author keywords

Fusion protein; Histidine tag; HLIF; Recombinant protein; Solubility; Stem cells

Indexed keywords

ALKALINE PHOSPHATASE ACTIVITY; BIOLOGICAL ACTIVITIES; COST EFFECTIVE; CYTOKINES; DOSE-DEPENDENT MANNER; FUSION PROTEINS; FUSION TAG; HIGH PURITY; HISTIDINE TAG; HLIF; IMMOBILIZED METAL AFFINITY CHROMATOGRAPHY; LC/MS/MS; LEUKEMIA INHIBITORY FACTORS; MOUSE EMBRYONIC STEM CELLS; N-TERMINALS; PLURIPOTENCY; RECOMBINANT PROTEIN; SIMPLE METHOD; TF-1 CELLS; USER-FRIENDLY METHODS; WESTERN BLOTS;

EID: 79951551289     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2010.12.020     Document Type: Article
Times cited : (28)

References (29)
  • 1
    • 46049098618 scopus 로고    scopus 로고
    • Expression of recombinant human epidermal growth factor in Escherichia coli and characterization of its biological activity
    • Abdull Razis A.F., Ismail E.N., Hambali Z., Abdullah M.N., Ali A.M., Mohd Lila M.A. Expression of recombinant human epidermal growth factor in Escherichia coli and characterization of its biological activity. Appl. Biochem. Biotechnol. 2008, 144:249-261.
    • (2008) Appl. Biochem. Biotechnol. , vol.144 , pp. 249-261
    • Abdull Razis, A.F.1    Ismail, E.N.2    Hambali, Z.3    Abdullah, M.N.4    Ali, A.M.5    Mohd Lila, M.A.6
  • 2
    • 0033598777 scopus 로고    scopus 로고
    • Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm
    • Bessette P.H., Aslund F., Beckwith J., Georgiou G. Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm. Proc. Natl. Acad. Sci. U. S. A. 1999, 96:13703-13708.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 13703-13708
    • Bessette, P.H.1    Aslund, F.2    Beckwith, J.3    Georgiou, G.4
  • 3
    • 0042927956 scopus 로고    scopus 로고
    • High throughput protein production for functional proteomics
    • Braun P., LaBaer J. High throughput protein production for functional proteomics. Trends Biotechnol. 2003, 21:383-388.
    • (2003) Trends Biotechnol. , vol.21 , pp. 383-388
    • Braun, P.1    LaBaer, J.2
  • 4
    • 0026305697 scopus 로고
    • Controlling basal expression in an inducible T7 expression system by blocking the target T7 promoter with lac repressor
    • Dubendorff J.W., Studier F.W. Controlling basal expression in an inducible T7 expression system by blocking the target T7 promoter with lac repressor. J. Mol. Biol. 1991, 219:45-59.
    • (1991) J. Mol. Biol. , vol.219 , pp. 45-59
    • Dubendorff, J.W.1    Studier, F.W.2
  • 7
    • 0024433304 scopus 로고
    • Production of leukemia inhibitory factor in Escherichia coli by a novel procedure and its use in maintaining embryonic stem cells in culture
    • Gearing D.P., Nicola N.A., Metcalf D., Foote S., Willson T.A., Gough N.M., Williams R.L. Production of leukemia inhibitory factor in Escherichia coli by a novel procedure and its use in maintaining embryonic stem cells in culture. Nat. Biotechnol. 1989, 7:1157-1161.
    • (1989) Nat. Biotechnol. , vol.7 , pp. 1157-1161
    • Gearing, D.P.1    Nicola, N.A.2    Metcalf, D.3    Foote, S.4    Willson, T.A.5    Gough, N.M.6    Williams, R.L.7
  • 9
    • 18844362113 scopus 로고    scopus 로고
    • Strategies for efficient production of heterologous proteins in Escherichia coli
    • Jana S., Deb J.K. Strategies for efficient production of heterologous proteins in Escherichia coli. Appl. Microbiol. Biotechnol. 2005, 67:289-298.
    • (2005) Appl. Microbiol. Biotechnol. , vol.67 , pp. 289-298
    • Jana, S.1    Deb, J.K.2
  • 10
    • 52949100181 scopus 로고    scopus 로고
    • Soluble expression of archaeal proteins in Escherichia coli by using fusion-partners
    • Kim S., Lee S.B. Soluble expression of archaeal proteins in Escherichia coli by using fusion-partners. Protein Express Purif. 2008, 62:116-119.
    • (2008) Protein Express Purif. , vol.62 , pp. 116-119
    • Kim, S.1    Lee, S.B.2
  • 12
    • 60549098614 scopus 로고    scopus 로고
    • Improving aquaporin Z expression in Escherichia coli by fusion partners and subsequent condition optimization
    • Lian J., Ding S., Cai J., Zhang D., Xu Z., Wang X. Improving aquaporin Z expression in Escherichia coli by fusion partners and subsequent condition optimization. Appl. Microbiol. Biotechnol. 2009, 82:463-470.
    • (2009) Appl. Microbiol. Biotechnol. , vol.82 , pp. 463-470
    • Lian, J.1    Ding, S.2    Cai, J.3    Zhang, D.4    Xu, Z.5    Wang, X.6
  • 13
    • 45249121799 scopus 로고    scopus 로고
    • Development of single mouse blastomeres into blastocysts, outgrowths and the establishment of embryonic stem cells
    • Lorthongpanich C., Yang S.H., Piotrowska-Nitsche K., Parnpai R., Chan A.W. Development of single mouse blastomeres into blastocysts, outgrowths and the establishment of embryonic stem cells. Reproduction 2008, 135:805-813.
    • (2008) Reproduction , vol.135 , pp. 805-813
    • Lorthongpanich, C.1    Yang, S.H.2    Piotrowska-Nitsche, K.3    Parnpai, R.4    Chan, A.W.5
  • 16
    • 0028854006 scopus 로고
    • High level expression of human leukemia inhibitory factor (LIF) from a synthetic gene in Escherichia coli and the physical and biological characterization of the protein
    • Samal B.B., Arakawa T., Boone T.C., Jones T., Prestrelski S.J., Narhi L.O., Wen J., Stearns G.W., Crandall C.A., Pope J., et al. High level expression of human leukemia inhibitory factor (LIF) from a synthetic gene in Escherichia coli and the physical and biological characterization of the protein. Biochim. Biophys. Acta 1995, 1260:27-34.
    • (1995) Biochim. Biophys. Acta , vol.1260 , pp. 27-34
    • Samal, B.B.1    Arakawa, T.2    Boone, T.C.3    Jones, T.4    Prestrelski, S.J.5    Narhi, L.O.6    Wen, J.7    Stearns, G.W.8    Crandall, C.A.9    Pope, J.10
  • 17
    • 0026416825 scopus 로고
    • Mass production of human epidermal growth factor using fed-batch cultures of recombinant Escherichia coli
    • Shimizu N., Fukuzono S., Harada Y., Fujimori K., Gotoh K., Yamazaki Y. Mass production of human epidermal growth factor using fed-batch cultures of recombinant Escherichia coli. Biotechnol. Bioeng. 1991, 38:37-42.
    • (1991) Biotechnol. Bioeng. , vol.38 , pp. 37-42
    • Shimizu, N.1    Fukuzono, S.2    Harada, Y.3    Fujimori, K.4    Gotoh, K.5    Yamazaki, Y.6
  • 18
    • 0023738918 scopus 로고
    • Production and characterization of human basic fibroblast growth factor from Escherichia coli
    • Squires C.H., Childs J., Eisenberg S.P., Polverini P.J., Sommer A. Production and characterization of human basic fibroblast growth factor from Escherichia coli. J. Biol. Chem. 1988, 263:16297-16302.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16297-16302
    • Squires, C.H.1    Childs, J.2    Eisenberg, S.P.3    Polverini, P.J.4    Sommer, A.5
  • 19
    • 0025349192 scopus 로고
    • Structural organization of the genes for murine and human leukemia inhibitory factor. Evolutionary conservation of coding and non-coding regions
    • Stahl J., Gearing D.P., Willson T.A., Brown M.A., King J.A., Gough N.M. Structural organization of the genes for murine and human leukemia inhibitory factor. Evolutionary conservation of coding and non-coding regions. J. Biol. Chem. 1990, 265:8833-8841.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8833-8841
    • Stahl, J.1    Gearing, D.P.2    Willson, T.A.3    Brown, M.A.4    King, J.A.5    Gough, N.M.6
  • 20
    • 0034665455 scopus 로고    scopus 로고
    • Design of high-throughput methods of protein production for structural biology
    • Stevens R.C. Design of high-throughput methods of protein production for structural biology. Structure 2000, 8:R177-185.
    • (2000) Structure , vol.8
    • Stevens, R.C.1
  • 21
    • 0032189925 scopus 로고    scopus 로고
    • Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins
    • Stewart E.J., Aslund F., Beckwith J. Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins. EMBO J 1998, 17:5543-5550.
    • (1998) EMBO J , vol.17 , pp. 5543-5550
    • Stewart, E.J.1    Aslund, F.2    Beckwith, J.3
  • 22
  • 23
    • 77953434949 scopus 로고    scopus 로고
    • Emerging use of stem cells in regenerative medicine
    • Teo A.K., Vallier L. Emerging use of stem cells in regenerative medicine. Biochem. J. 2010, 428:11-23.
    • (2010) Biochem. J. , vol.428 , pp. 11-23
    • Teo, A.K.1    Vallier, L.2
  • 26
    • 10644275363 scopus 로고    scopus 로고
    • Optimized expression of soluble cyclomaltodextrinase of thermophilic origin in Escherichia coli by using a soluble fusion-tag and by tuning of inducer concentration
    • Turner P., Holst O., Karlsson E.N. Optimized expression of soluble cyclomaltodextrinase of thermophilic origin in Escherichia coli by using a soluble fusion-tag and by tuning of inducer concentration. Protein Express Purif. 2005, 39:54-60.
    • (2005) Protein Express Purif. , vol.39 , pp. 54-60
    • Turner, P.1    Holst, O.2    Karlsson, E.N.3
  • 27
    • 0023943656 scopus 로고
    • Expression, renaturation and purification of recombinant human interleukin 4 from Escherichia coli
    • van Kimmenade A., Bond M.W., Schumacher J.H., Laquoi C., Kastelein R.A. Expression, renaturation and purification of recombinant human interleukin 4 from Escherichia coli. Eur. J. Biochem. 1988, 173:109-114.
    • (1988) Eur. J. Biochem. , vol.173 , pp. 109-114
    • van Kimmenade, A.1    Bond, M.W.2    Schumacher, J.H.3    Laquoi, C.4    Kastelein, R.A.5
  • 28
    • 0028793115 scopus 로고
    • Increase of solubility of foreign proteins in Escherichia coli by coproduction of the bacterial thioredoxin
    • Yasukawa T., Kanei-Ishii C., Maekawa T., Fujimoto J., Yamamoto T., Ishii S. Increase of solubility of foreign proteins in Escherichia coli by coproduction of the bacterial thioredoxin. J. Biol. Chem. 1995, 270:25328-25331.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25328-25331
    • Yasukawa, T.1    Kanei-Ishii, C.2    Maekawa, T.3    Fujimoto, J.4    Yamamoto, T.5    Ishii, S.6
  • 29
    • 77952423352 scopus 로고    scopus 로고
    • Large scale production of stem cells and their derivatives
    • Zweigerdt R. Large scale production of stem cells and their derivatives. Adv. Biochem. Eng. Biotechnol. 2009, 114:201-235.
    • (2009) Adv. Biochem. Eng. Biotechnol. , vol.114 , pp. 201-235
    • Zweigerdt, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.