Generation of Monoclonal Antibodies Against Recombinant AtSIZ1

被引:1
作者
Kim, Kangchang [2 ]
Bae, Suyoung [1 ]
Hong, Jaewoo [1 ]
Choi, Jida [1 ]
Ryoo, Soyoon [1 ]
Jhun, Hyunjhung [1 ]
Lee, Siyoung [3 ]
Her, Erk [3 ]
Hong, Kwangwon [1 ]
Kim, Soohyun [1 ]
机构
[1] Konkuk Univ, Lab Cytokine Immunol, Inst Biomed Sci & Technol, Med Immunol Ctr, Seoul 143701, South Korea
[2] Gyeongsang Natl Univ, PMBBRC, EB NCRC, Div Appl Life Sci,Brain Korea Program 21, Jinju, South Korea
[3] Konkuk Univ, Coll Med, Dept Immunol, Seoul 143701, South Korea
来源
HYBRIDOMA | 2010年 / 29卷 / 04期
关键词
SUMO E3 LIGASE; SALICYLIC-ACID; POSTTRANSLATIONAL MODIFICATIONS; POLYPEPTIDE TAGS; MODIFIER SUMO; ARABIDOPSIS; UBIQUITIN; PROTEIN; SUMOYLATION; TRANSCRIPTION;
D O I
10.1089/hyb.2010.0002
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Post-translational modifications of target proteins by small ubiquitin-like modifier (SUMO) proteins modulate many cellular processes in yeast and animals. Here we present the development of monoclonal antibodies (MAb) and polyclonal antibodies (PAb) against Arabidopsis SIZ1 (AtSIZ1) protein with high specificity. Mice were immunized with recombinant AtSIZ1 protein for generating monoclonal antibodies via the classic hybridoma production technique. Anti-AtSIZ1 MAb and PAb were able to detect endogenous AtSIZ1 in Arabidopsis wild type and its complementary line formed by transforming C-siz1-2 mutant with construct containing the AtSIZ1 gene under the control of the native promoter, but not the siz1-2 deletion mutant. These results show that these anti-AtSIZ MAbs are highly sensitive to detect endogenous AtSIZ1 and can be used for immuno-blotting and other experimental methods. The new anti-AtSIZ1 MAbs will be essential tools used to investigate the role of AtSIZ1 in plant developmental biology.
引用
收藏
页码:333 / 340
页数:8
相关论文
共 37 条
  • [1] The Arabidopsis E3 SUMO ligase SIZ1 regulates plant growth and drought responses
    Catala, Rafael
    Ouyang, Jian
    Abreu, Isabel A.
    Hu, Yuxin
    Seo, Haksoo
    Zhang, Xiuren
    Chua, Nam-Hai
    [J]. PLANT CELL, 2007, 19 (09) : 2952 - 2966
  • [2] Evolution of a signalling system that incorporates both redundancy and diversity:: Arabidopsis SUMOylation
    Chosed, Renee
    Mukherjee, Sohini
    Lois, Luisa Maria
    Orth, Kim
    [J]. BIOCHEMICAL JOURNAL, 2006, 398 (03) : 521 - 529
  • [3] SUMO-conjugating and SUMO-deconjugating enzymes from Arabidopsis
    Colby, Thomas
    Matthaei, Anett
    Boeckelmann, Astrid
    Stuible, Hans-Peter
    [J]. PLANT PHYSIOLOGY, 2006, 142 (01) : 318 - 332
  • [4] Post-translational regulation in plants employing a diverse set of polypeptide tags
    Downes, B
    Vierstra, RD
    [J]. BIOCHEMICAL SOCIETY TRANSACTIONS, 2005, 33 : 393 - 399
  • [5] MUBs, a family of ubiquitin-fold proteins that are plasma membrane-anchored by prenylation
    Downes, Brian P.
    Saracco, Scott A.
    Lee, Sang Sook
    Crowell, Dring N.
    Vierstra, Richard D.
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2006, 281 (37) : 27145 - 27157
  • [6] The 'PINIT' motif, of a newly identified conserved domain of the PIAS protein family, is essential for nuclear retention of PIAS3L
    Duval, D
    Duval, G
    Kedinger, C
    Poch, O
    Boeuf, H
    [J]. FEBS LETTERS, 2003, 554 (1-2) : 111 - 118
  • [7] Post-translational modification by the small ubiquitin-related modifier SUMO has big effects on transcription factor activity
    Gill, G
    [J]. CURRENT OPINION IN GENETICS & DEVELOPMENT, 2003, 13 (02) : 108 - 113
  • [8] SUMO: A history of modification
    Hay, RT
    [J]. MOLECULAR CELL, 2005, 18 (01) : 1 - 12
  • [9] SUMOrganization of the nucleus
    Heun, Patrick
    [J]. CURRENT OPINION IN CELL BIOLOGY, 2007, 19 (03) : 350 - 355
  • [10] SP-RING for SUMO: New functions bloom for a ubiquitin-like protein
    Hochstrasser, M
    [J]. CELL, 2001, 107 (01) : 5 - 8