Prokaryotic expression of a novel mouse pro-apoptosis protein PNAS-4 and application of its polyclonal antibodies

Brazilian Journal of Medical and Biological Research

Volumn 41, Issue 6, 2008, Pages 504-511

  Zhang, P ^a   Wang, C T ^a   Yan, F ^a   Gou, L ^a   Tong, A P ^b   Cai, F ^b   Li, Q ^b   Deng, H X ^a   Wei, Y Q ^a  

^a SICHUAN UNIVERSITY   (China)

^b SICHUAN UNIVERSITY   (China)

Author keywords

Anti mPNAS 4; Apoptosis related protein family; One step affinity purification; Polyclonal antibody

Indexed keywords

APOPTOSIS INDUCING FACTOR; DNA; GLUTATHIONE; POLYCLONAL ANTIBODY; PROTEIN PNAS 4; SEPHAROSE; UNCLASSIFIED DRUG;

ANIMAL CELL; ANIMAL TISSUE; APOPTOSIS; ARTICLE; BRAIN TISSUE; CANCER CELL CULTURE; COLON CARCINOMA; CONTROLLED STUDY; DNA DAMAGE; ELECTROSPRAY MASS SPECTROMETRY; GENE OVEREXPRESSION; IMMUNOBLOTTING; IMMUNOHISTOCHEMISTRY; IN VITRO STUDY; IN VIVO STUDY; LEWIS CARCINOMA; MOUSE; NONHUMAN; PROKARYOTE; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PURIFICATION; RABBIT; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; SEQUENCE HOMOLOGY; TEMPERATURE DEPENDENCE;

ESCHERICHIA COLI; MUS; ORYCTOLAGUS CUNICULUS; PROKARYOTA;

ANIMALS; APOPTOSIS; APOPTOSIS REGULATORY PROTEINS; BLOTTING, WESTERN; DNA, COMPLEMENTARY; ESCHERICHIA COLI; GLUTATHIONE TRANSFERASE; IMMUNOHISTOCHEMISTRY; MICE; PLASMIDS; PROKARYOTIC CELLS; RABBITS; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; XENOPUS PROTEINS;

EID: 54749115185     PISSN: 0100879X     EISSN: 1414431X     Source Type: Journal    
DOI: 10.1590/S0100-879X2008000600012     Document Type: Article

References (21)

1. Filippov V, Filippova M, Sinha D, DuerksenHughes PJ. PNAS-4: A Novel Pro-Apoptotic Gene Activated During the Early Response to DNA Damage. Proceedings of the American Association for Cancer Research. 96th Annual Meeting. Anaheim, 2005.
2. James ER, Fresco VM, Robertson LL. Glucocorticoid-induced changes in the global gene expression of lens epithelial cells. J Ocul Pharmacol Ther 2005; 21: 11-27.
3. Guo F, Li SQ, Chu YH, Huang XF, Sun LM, Li YQ, et al. High-level expression, polyclonal antibody preparation and sub-cellular localization analysis of mouse Rhox5 protein. Protein Expr Purif 2007; 54: 247-252.
4. Rautureau G, Jouvensal L, Decoville M, Locker D, Vovelle F, Schoentgen F. Cloning, high yield over-expression, purification, and characterization of CG18594, a new PEBP/RKIP family member from Drosophila melanogaster. Protein Expr Purif 2006; 48: 90-97.
5. Park HJ, Jeon JH, Kang SG, Lee JH, Lee SA, Kim HK. Functional expression and refolding of new alkaline esterase, EM2L8 from deep-sea sediment metagenome. Protein Expr Purif 2007; 52: 340-347.
6. Londer YY, Pokkuluri PR, Erickson J, Orshonsky V, Schiffer M. Heterologous expression of hexaheme fragments of a multidomain cytochrome from Geobacter sulfurreducens representing a novel class of cytochromes c. Protein Expr Purif 2005; 39: 254-260.
7. Menard LP, Lussier JG, Lepine F, Paiva de SC, Dubreuil JD. Expression, purification, and biochemical characterization of enteroaggregative Escherichia coli heat-stable enterotoxin 1. Protein Expr Purif 2004; 33: 223-231.
8. Li A, Kato Z, Ohnishi H, Hashimoto K, Matsukuma E, Omoya K, et al. Optimized gene synthesis and high expression of human interleukin-18. Protein Expr Purif 2003; 32: 110-118.
9. Voss EW Jr, Miklasz SD, Petrossian A, Dombrink-Kurtzman MA. Polyclonal antibodies specific for liganded active site (metatype) of a high affinity anti-hapten monoclonal antibody. Mol Immunol 1988; 25: 751-759.
10. Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976; 72: 248-254.
11. LaVallie ER, McCoy JM. Gene fusion expression systems in Escherichia coli. Curr Opin Biotechnol 1995; 6: 501-506.
12. Smith DB, Johnson KS. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 1988; 67: 31-40.
13. Stevens RC. Design of high-throughput methods of protein production for structural biology. Structure 2000; 8: R177-R185.
14. Guzzo CM, Yang DC. Systematic analysis of fusion and affinity tags using human aspartyl-tRNA synthetase expressed in E. coli. Protein Expr Purif 2007; 54: 166-175.
15. Kovacs-Nolan J, Sasaki E, Yoo D, Mine Y. Cloning and expression of human rotavirus spike protein, VP8, in Escherichia coli. Biochem Biophys Res Commun 2001; 282: 1183-1188.
16. Smith DB. Generating fusions to glutathione S-transferase for protein studies. Methods Enzymol 2000; 326: 254-270.
17. Lundberg M, Holmgren A, Johansson M. Human glutaredoxin 2 affinity tag for recombinant peptide and protein purification. Protein Expr Purif 2006; 45: 37-42.
18. Yan J, Yang XP, Kim YS, Joo JH, Jetten AM. RAP80 interacts with the SUMO-conjugating enzyme UBC9 and is a novel target for sumoylation. Biochem Biophys Res Commun 2007; 362: 132-138.
19. Huang X, Shi Z, Wang W, Bai J, Chen Z, Xu J, et al. Identification and characterization of a novel protein ISOC2 that interacts with p16INK4a. Biochem Biophys Res Commun 2007; 361: 287-293.
20. Quaedackers ME, van den Brink CE, van der Saag PT, Tertoolen LG. Direct interaction between estrogen receptor alpha and NF-kappaB in the nucleus of living cells. Mol Cell Endocrinol 2007; 273: 42-50.
21. Nian H, Fan C, Liao S, Shi Y, Zhang K, Liu Y, et al. RNF151, a testis-specific RING finger protein, interacts with dysbindin. Arch Biochem Biophys 2007; 465: 157-163.