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Volumn 97, Issue 2, 2013, Pages 741-749

Cytoplasmic expression, antibody production, and characterization of the novel zinc finger protein 637

Author keywords

Anti zfp637 specific antibody; Cytoplasmic expression; Oxidative stress; Recombinant protein; Zfp637

Indexed keywords

ANTIBODY PRODUCTION; BACTERIAL CULTURES; CELL LINES; CELL NUCLEUS; CYTOPLASMIC EXPRESSION; DNA-BINDING PROTEIN; ENZYME LINKED IMMUNOSORBENT ASSAY; ESCHERICHIA COLI BL21; EXPRESSION LEVELS; EXPRESSION SYSTEM; FUSION PROTEINS; GENE TRANSCRIPTIONS; GLUTATHIONE-S-TRANSFERASE; IMMUNOHISTOCHEMISTRY; NIH-3T3 CELLS; POLYCLONAL ANTIBODY; PROTEIN FAMILY; STRUCTURAL CHARACTERIZATION; TIME-DEPENDENT; WESTERN BLOTTING; ZFP637; ZINC FINGER MOTIFS; ZINC FINGER PROTEIN;

EID: 84873989922     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-012-4235-5     Document Type: Article
Times cited : (3)

References (33)
  • 1
    • 38049055294 scopus 로고    scopus 로고
    • Impaired liver regeneration in Nrf2 knockout mice: Role of ROS-mediated insulin/IGF-1 resistance
    • 10.1038/sj.emboj.7601950 10.1038/sj.emboj.7601950 1:CAS:528: DC%2BD1cXksVGqug%3D%3D
    • Beyer TA, Xu W, Teupser D, Auf dem Keller U, Bugnon P, Hildt E, Thiery J, Kan YW, Werner S (2008) Impaired liver regeneration in Nrf2 knockout mice: role of ROS-mediated insulin/IGF-1 resistance. EMBO J 27:212-223. doi: 10.1038/sj.emboj.7601950
    • (2008) EMBO J , vol.27 , pp. 212-223
    • Beyer, T.A.1    Xu, W.2    Teupser, D.3    Auf Dem Keller, U.4    Bugnon, P.5    Hildt, E.6    Thiery, J.7    Kan, Y.W.8    Werner, S.9
  • 2
    • 77956481419 scopus 로고    scopus 로고
    • Protein solubility and differential proteomic profiling of recombinant Escherichia coli overexpressing double-tagged fusion proteins
    • 10.1186/1475-2859-9-63 10.1186/1475-2859-9-63
    • Cheng CH, Lee WC (2010) Protein solubility and differential proteomic profiling of recombinant Escherichia coli overexpressing double-tagged fusion proteins. Microb Cell Fact 9:63. doi: 10.1186/1475-2859-9-63
    • (2010) Microb Cell Fact , vol.9 , pp. 63
    • Cheng, C.H.1    Lee, W.C.2
  • 3
    • 0033589826 scopus 로고    scopus 로고
    • New fusion protein systems designed to give soluble expression in Escherichia coli
    • 10.1002/(SICI)1097-0290(19991120)65:4<382: AID-BIT2>3.0.CO;2-I 10.1002/(SICI)1097-0290(19991120)65:4<382: AID-BIT2>3.0.CO;2-I 1:CAS:528:DyaK1MXmslGktr8%3D
    • Davis GD, Elisee C, Newham DM, Harrison RG (1999) New fusion protein systems designed to give soluble expression in Escherichia coli. Biotechnol Bioeng 65:382-388. doi:10.1002/(SICI)1097-0290(19991120)65:4<382::AID- BIT2>3.0.CO;2-I
    • (1999) Biotechnol Bioeng , vol.65 , pp. 382-388
    • Davis, G.D.1    Elisee, C.2    Newham, D.M.3    Harrison, R.G.4
  • 4
    • 0030254558 scopus 로고    scopus 로고
    • HIV-I protease. Cloning, expression, and purification
    • 10.1007/BF02785692 10.1007/BF02785692 1:CAS:528:DyaK2sXit1ykt7w%3D
    • Dergousova NI, Amerik AY, Volynskaya AM, Rumsh LD (1996) HIV-I protease. Cloning, expression, and purification. Appl Biochem Biotechnol 61:97-107. doi: 10.1007/BF02785692
    • (1996) Appl Biochem Biotechnol , vol.61 , pp. 97-107
    • Dergousova, N.I.1    Amerik, A.Y.2    Volynskaya, A.M.3    Rumsh, L.D.4
  • 5
    • 27744565594 scopus 로고    scopus 로고
    • In vivo misregulation of genes involved in apoptosis, development and oxidative stress in mice lacking both functional Werner syndrome protein and poly(ADP-ribose) polymerase-1
    • 10.1093/hmg/ddi362 10.1093/hmg/ddi362
    • Deschênes F, Massip L, Garand C, Lebel M (2005) In vivo misregulation of genes involved in apoptosis, development and oxidative stress in mice lacking both functional Werner syndrome protein and poly(ADP-ribose) polymerase-1. Hum Mol Genet 14:3293-3308. doi: 10.1093/hmg/ddi362
    • (2005) Hum Mol Genet , vol.14 , pp. 3293-3308
    • Deschênes, F.1    Massip, L.2    Garand, C.3    Lebel, M.4
  • 6
    • 29244442950 scopus 로고    scopus 로고
    • Simplified screening for the detection of soluble fusion constructs expressed in E. coli using a modular set of vectors
    • 10.1186/1475-2859-4-34 10.1186/1475-2859-4-34
    • Dümmler A, Lawrence A, de Marco A (2005) Simplified screening for the detection of soluble fusion constructs expressed in E. coli using a modular set of vectors. Microb Cell Fact 4:34. doi: 10.1186/1475-2859-4-34
    • (2005) Microb Cell Fact , vol.4 , pp. 34
    • Dümmler, A.1    Lawrence, A.2    De Marco, A.3
  • 7
    • 0027212498 scopus 로고
    • Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins
    • 10.1006/abio.1993.1170 10.1006/abio.1993.1170 1:CAS:528: DyaK3sXkt1equ7Y%3D
    • Frangioni JV, Neel BG (1993) Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins. Anal Biochem 210:179-187. doi: 10.1006/abio.1993.1170
    • (1993) Anal Biochem , vol.210 , pp. 179-187
    • Frangioni, J.V.1    Neel, B.G.2
  • 8
    • 79952199366 scopus 로고    scopus 로고
    • Purification of proteins fused to glutathione S-transferase
    • 10.1007/978-1-60761-913-0-14 10.1007/978-1-60761-913-0-14 1:CAS:528:DC%2BC3cXhsFaitrvE
    • Harper S, Speicher DW (2011) Purification of proteins fused to glutathione S-transferase. Methods Mol Biol 681:259-280. doi: 10.1007/978-1-60761-913-0-14
    • (2011) Methods Mol Biol , vol.681 , pp. 259-280
    • Harper, S.1    Speicher, D.W.2
  • 9
    • 0027112232 scopus 로고
    • Affinity purification of insoluble recombinant fusion proteins containing glutathione-S-transferase
    • 10.1002/bit.260390805 10.1002/bit.260390805 1:CAS:528:DyaK38XitlWhurw%3D
    • Hartman J, Daram P, Frizzell RA, Rado T, Benos DJ, Sorscher EJ (1992) Affinity purification of insoluble recombinant fusion proteins containing glutathione-S-transferase. Biotechnol Bioeng 39:828-832. doi: 10.1002/bit.260390805
    • (1992) Biotechnol Bioeng , vol.39 , pp. 828-832
    • Hartman, J.1    Daram, P.2    Frizzell, R.A.3    Rado, T.4    Benos, D.J.5    Sorscher, E.J.6
  • 10
    • 0036830462 scopus 로고    scopus 로고
    • The p53-activated gene, PAG608, requires a zinc finger domain for nuclear localization and oxidative stress-induced apoptosis
    • 10.1074/jbc.M203594200 10.1074/jbc.M203594200 1:CAS:528: DC%2BD38XotF2gtbg%3D
    • Higashi Y, Asanuma M, Miyazaki I, Haque ME, Fujita N, Tanaka K, Ogawa N (2002) The p53-activated gene, PAG608, requires a zinc finger domain for nuclear localization and oxidative stress-induced apoptosis. J Biol Chem 277:42224-42232. doi: 10.1074/jbc.M203594200
    • (2002) J Biol Chem , vol.277 , pp. 42224-42232
    • Higashi, Y.1    Asanuma, M.2    Miyazaki, I.3    Haque, M.E.4    Fujita, N.5    Tanaka, K.6    Ogawa, N.7
  • 12
    • 0032787876 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
    • 10.1110/ps.8.8.1668 10.1110/ps.8.8.1668 1:CAS:528:DyaK1MXlt1Omu7g%3D
    • Kapust RB, Waugh DS (1999) Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci 8:1668-1674. doi: 10.1110/ps.8.8.1668
    • (1999) Protein Sci , vol.8 , pp. 1668-1674
    • Kapust, R.B.1    Waugh, D.S.2
  • 13
    • 14744271625 scopus 로고
    • Protein aggregation in vitro and in vivo: A quantitative model of the kinetic competition between folding and aggregation
    • 10.1038/nbt0991-825 10.1038/nbt0991-825 1:CAS:528:DyaK3MXmt1Khtr0%3D
    • Kiefhaber T, Rudolph R, Kohler HH, Buchner J (1991) Protein aggregation in vitro and in vivo: a quantitative model of the kinetic competition between folding and aggregation. Biotechnology (N Y) 9:825-829. doi: 10.1038/nbt0991-825
    • (1991) Biotechnology (N Y) , vol.9 , pp. 825-829
    • Kiefhaber, T.1    Rudolph, R.2    Kohler, H.H.3    Buchner, J.4
  • 14
    • 79952509829 scopus 로고    scopus 로고
    • Recombinant expression, affinity purification and functional characterization of Scots pine defensin 1
    • 10.1007/s00253-010-2935-2 10.1007/s00253-010-2935-2 1:CAS:528: DC%2BC3MXhs1GhsLg%3D
    • Kovaleva V, Krynytskyy H, Gout I, Gout R (2011) Recombinant expression, affinity purification and functional characterization of Scots pine defensin 1. Appl Microbiol Biotechnol 89:1093-1101. doi: 10.1007/s00253-010-2935-2
    • (2011) Appl Microbiol Biotechnol , vol.89 , pp. 1093-1101
    • Kovaleva, V.1    Krynytskyy, H.2    Gout, I.3    Gout, R.4
  • 15
    • 14744292185 scopus 로고
    • A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm
    • 10.1038/nbt0293-187 1:CAS:528:DyaK3sXisFegsr0%3D
    • LaVallie ER, DiBlasio EA, Kovacic S, Grant KL, Schendel PF, McCoy JM (1993) A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm. Bio Technol 11:187-193. doi: 10.1038/nbt0293-187
    • (1993) Bio Technol , vol.11 , pp. 187-193
    • Lavallie, E.R.1    Diblasio, E.A.2    Kovacic, S.3    Grant, K.L.4    Schendel, P.F.5    McCoy, J.M.6
  • 16
    • 68149169901 scopus 로고    scopus 로고
    • Construction of eukaryotic expression plasmid for a novel zinc finger protein gene Zfp637 and its effect on breast carcinoma cell EMT6
    • 1:CAS:528:DC%2BD1MXhtlGhur7J 603
    • Li K, Ren JJ, Zhang J, Liu K, Qi YY, Wang XJ, Xiao HY, Lin P (2009) Construction of eukaryotic expression plasmid for a novel zinc finger protein gene Zfp637 and its effect on breast carcinoma cell EMT6. Sichuan Da Xue Xue Bao Yi Xue Ban 40:575-578, 603
    • (2009) Sichuan da Xue Xue Bao Yi Xue Ban , vol.40 , pp. 575-578
    • Li, K.1    Ren, J.J.2    Zhang, J.3    Liu, K.4    Qi, Y.Y.5    Wang, X.J.6    Xiao, H.Y.7    Lin, P.8
  • 19
    • 0028287188 scopus 로고
    • Engineering proteins to facilitate bioprocessing
    • 10.1016/0167-7799(94)90080-9 10.1016/0167-7799(94)90080-9 1:CAS:528:DyaK2cXltVKmsb8%3D
    • Nygren P-A, Stahl S, Uhlén M (1994) Engineering proteins to facilitate bioprocessing. Trends Biotechnol 12:184-188. doi: 10.1016/0167-7799(94)90080-9
    • (1994) Trends Biotechnol , vol.12 , pp. 184-188
    • Nygren, P.-A.1    Stahl, S.2    Uhlén, M.3
  • 20
    • 68249124331 scopus 로고    scopus 로고
    • The serine protease HtrA2/Omi cleaves Parkin and irreversibly inactivates its E3 ubiquitin ligase activity
    • 10.1016/j.bbrc.2009.07.079 10.1016/j.bbrc.2009.07.079 1:CAS:528:DC%2BD1MXps1Clsbw%3D
    • Park HM, Kim GY, Nam MK, Seong GH, Han C, Chung KC, Kang S, Rhim H (2009) The serine protease HtrA2/Omi cleaves Parkin and irreversibly inactivates its E3 ubiquitin ligase activity. Biochem Biophys Res Commun 387:537-542. doi: 10.1016/j.bbrc.2009.07.079
    • (2009) Biochem Biophys Res Commun , vol.387 , pp. 537-542
    • Park, H.M.1    Kim, G.Y.2    Nam, M.K.3    Seong, G.H.4    Han, C.5    Chung, K.C.6    Kang, S.7    Rhim, H.8
  • 21
    • 1642564552 scopus 로고    scopus 로고
    • The zinc finger protein Zat12 is required for cytosolic ascorbate peroxidase 1 expression during oxidative stress in Arabidopsis
    • 10.1074/jbc.M313350200 10.1074/jbc.M313350200 1:CAS:528: DC%2BD2cXitFyhurk%3D
    • Rizhsky L, Davletova S, Liang H, Mittler R (2004) The zinc finger protein Zat12 is required for cytosolic ascorbate peroxidase 1 expression during oxidative stress in Arabidopsis. J Biol Chem 279:11736-11743. doi: 10.1074/jbc.M313350200
    • (2004) J Biol Chem , vol.279 , pp. 11736-11743
    • Rizhsky, L.1    Davletova, S.2    Liang, H.3    Mittler, R.4
  • 22
    • 0037868957 scopus 로고    scopus 로고
    • Sp1 and Sp3 are oxidative stress-inducible, antideath transcription factors in cortical neurons
    • 1:CAS:528:DC%2BD3sXjslGntbs%3D
    • Ryu H, Lee J, Zaman K, Kubilis J, Ferrante RJ, Ross BD, Neve R, Ratan RR (2003) Sp1 and Sp3 are oxidative stress-inducible, antideath transcription factors in cortical neurons. J Neurosci 23:3597-3606
    • (2003) J Neurosci , vol.23 , pp. 3597-3606
    • Ryu, H.1    Lee, J.2    Zaman, K.3    Kubilis, J.4    Ferrante, R.J.5    Ross, B.D.6    Neve, R.7    Ratan, R.R.8
  • 23
    • 33748691613 scopus 로고    scopus 로고
    • The evaluation of the factors that cause aggregation during recombinant expression in E. coli is simplified by the employment of an aggregation- sensitive reporter
    • 10.1186/1475-2859-5-28 10.1186/1475-2859-5-28
    • Schultz T, Martinez L, de Marco A (2006) The evaluation of the factors that cause aggregation during recombinant expression in E. coli is simplified by the employment of an aggregation-sensitive reporter. Microb Cell Fact 5:28. doi: 10.1186/1475-2859-5-28
    • (2006) Microb Cell Fact , vol.5 , pp. 28
    • Schultz, T.1    Martinez, L.2    De Marco, A.3
  • 24
    • 4444260910 scopus 로고    scopus 로고
    • Autocatalytic processing of HtrA2/Omi is essential for induction of caspase-dependent cell death through antagonizing XIAP
    • 10.1074/jbc.M401408200 10.1074/jbc.M401408200 1:CAS:528: DC%2BD2cXntFSnsrc%3D
    • Seong YM, Choi JY, Park HJ, Kim KJ, Ahn SG, Seong GH, Kim IK, Kang S, Rhim H (2004) Autocatalytic processing of HtrA2/Omi is essential for induction of caspase-dependent cell death through antagonizing XIAP. J Biol Chem 279:37588-37596. doi: 10.1074/jbc.M401408200
    • (2004) J Biol Chem , vol.279 , pp. 37588-37596
    • Seong, Y.M.1    Choi, J.Y.2    Park, H.J.3    Kim, K.J.4    Ahn, S.G.5    Seong, G.H.6    Kim, I.K.7    Kang, S.8    Rhim, H.9
  • 25
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • 10.1016/0378-1119(88)90005-4 10.1016/0378-1119(88)90005-4 1:CAS:528:DyaL1cXlt1Ghs7g%3D
    • Smith DB, Johnson KS (1988) Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67:31-40. doi: 10.1016/0378-1119(88)90005-4
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 26
    • 0022808489 scopus 로고
    • Mr 26,000 antigen of Schistosoma japonicum recognized by resistant WEHI 129/J mice is a parasite glutathione S-transferase
    • 10.1073/pnas.83.22.8703 10.1073/pnas.83.22.8703 1:CAS:528: DyaL2sXivVCjtQ%3D%3D
    • Smith DB, Davern KM, Board PG, Tiu WU, Garcia EG, Mitchell GF (1986) Mr 26,000 antigen of Schistosoma japonicum recognized by resistant WEHI 129/J mice is a parasite glutathione S-transferase. Proc Natl Acad Sci U S A 83:8703-8707. doi: 10.1073/pnas.83.22.8703
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 8703-8707
    • Smith, D.B.1    Davern, K.M.2    Board, P.G.3    Tiu, W.U.4    Garcia, E.G.5    Mitchell, G.F.6
  • 27
    • 13644262805 scopus 로고    scopus 로고
    • Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli
    • 10.1186/1475-2859-4-1 10.1186/1475-2859-4-1
    • Sørensen HP, Mortensen KK (2005) Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli. Microb Cell Fact 4:1. doi: 10.1186/1475-2859-4-1
    • (2005) Microb Cell Fact , vol.4 , pp. 1
    • Sørensen, H.P.1    Mortensen, K.K.2
  • 28
    • 80051577496 scopus 로고    scopus 로고
    • Overexpression and purification of U24 from human herpesvirus type-6 in E. coli: Unconventional use of oxidizing environments with a maltose binding protein-hexahistine dual tag to enhance membrane protein yield
    • 10.1186/1475-2859-10-51 10.1186/1475-2859-10-51 1:CAS:528: DC%2BC3MXovVaju78%3D
    • Tait AR, Straus SK (2011) Overexpression and purification of U24 from human herpesvirus type-6 in E. coli: unconventional use of oxidizing environments with a maltose binding protein-hexahistine dual tag to enhance membrane protein yield. Microb Cell Fact 10:51. doi: 10.1186/1475-2859-10-51
    • (2011) Microb Cell Fact , vol.10 , pp. 51
    • Tait, A.R.1    Straus, S.K.2
  • 29
    • 0042193601 scopus 로고    scopus 로고
    • Protein aggregation in recombinant bacteria: Biological role of inclusion bodies
    • 10.1023/A:1025024104862 10.1023/A:1025024104862 1:CAS:528: DC%2BD3sXmtVems74%3D
    • Villaverde A, Carrió MM (2003) Protein aggregation in recombinant bacteria: biological role of inclusion bodies. Biotechnol Lett 25:1385-1395. doi: 10.1023/A:1025024104862
    • (2003) Biotechnol Lett , vol.25 , pp. 1385-1395
    • Villaverde, A.1    Carrió, M.M.2
  • 30
    • 79959657492 scopus 로고    scopus 로고
    • Optimizing HIV-1 protease production in Escherichia coli as fusion protein
    • 10.1186/1475-2859-10-53 10.1186/1475-2859-10-53
    • Volontè F, Piubelli L, Pollegioni L (2011) Optimizing HIV-1 protease production in Escherichia coli as fusion protein. Microb Cell Fact 10:53. doi: 10.1186/1475-2859-10-53
    • (2011) Microb Cell Fact , vol.10 , pp. 53
    • Volontè, F.1    Piubelli, L.2    Pollegioni, L.3
  • 31
    • 33751537479 scopus 로고    scopus 로고
    • Stability of plasmid and expression of a recombinant gonadotropin- releasing hormone (GnRH) vaccine in Escherichia coli
    • 10.1007/s00253-006-0547-7 10.1007/s00253-006-0547-7 1:CAS:528: DC%2BD28Xht1Gnu7jK
    • Xu J, Li W, Wu J, Zhang Y, Zhu Z, Liu J, Hu Z (2006) Stability of plasmid and expression of a recombinant gonadotropin-releasing hormone (GnRH) vaccine in Escherichia coli. Appl Microbiol Biotechnol 73:780-788. doi: 10.1007/s00253-006-0547-7
    • (2006) Appl Microbiol Biotechnol , vol.73 , pp. 780-788
    • Xu, J.1    Li, W.2    Wu, J.3    Zhang, Y.4    Zhu, Z.5    Liu, J.6    Hu, Z.7
  • 32
    • 55649112043 scopus 로고    scopus 로고
    • High-level expression and characterization of an anti-VEGF165 single-chain variable fragment (scFv) by small ubiquitin-related modifier fusion in Escherichia coli
    • 10.1007/s00253-008-1655-3 10.1007/s00253-008-1655-3 1:CAS:528: DC%2BD1cXhtlaqsbnP
    • Ye T, Lin Z, Lei H (2008) High-level expression and characterization of an anti-VEGF165 single-chain variable fragment (scFv) by small ubiquitin-related modifier fusion in Escherichia coli. Appl Microbiol Biotechnol 81:311-317. doi: 10.1007/s00253-008-1655-3
    • (2008) Appl Microbiol Biotechnol , vol.81 , pp. 311-317
    • Ye, T.1    Lin, Z.2    Lei, H.3
  • 33
    • 76549115938 scopus 로고    scopus 로고
    • MCP-1 causes cardiomyoblast death via autophagy resulting from ER stress caused by oxidative stress generated by inducing a novel zinc-finger protein, MCPIP
    • 10.1042/BJ20090976 10.1042/BJ20090976 1:CAS:528:DC%2BC3cXhtVKhs7Y%3D
    • Younce CW, Kolattukudy PE (2010) MCP-1 causes cardiomyoblast death via autophagy resulting from ER stress caused by oxidative stress generated by inducing a novel zinc-finger protein, MCPIP. Biochem J 426:43-53. doi: 10.1042/BJ20090976
    • (2010) Biochem J , vol.426 , pp. 43-53
    • Younce, C.W.1    Kolattukudy, P.E.2


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