Protein expression vector and utilization thereof

Details Protein expression vector and utilization thereof Protein expression vector and utilization thereof

2006-04-18

2006-04-18

Prouty, Rebecca E. (Department: 1652)

Chemistry: molecular biology and microbiology

Vector, per se

C435S348000, C435S325000, C435S252300, C435S069100

Reexamination Certificate

active

07029909

ABSTRACT:
A protein expression vector containing (a) a nucleotide sequence encoding an IgG(κ) or a trypsin secretory signal peptide, (b) a nucleotide sequence encoding a polyhistidine amino acid sequence, (c) a nucleotide sequence encoding an amino acid sequence comprising amino acid residues 36–40 of SEQ ID NO:19 (Asp-Asp-Asp-Asp-Lys), which is cleavable by an enterokinase, and (d) a cloning site into which a nucleotide sequence encoding a target protein can be inserted, wherein (a), (b), (c) and (d) are assembled within the vector in the order recited.

REFERENCES:
patent: 10179169 (1998-07-01), None
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Invitrogen 1997 Catalog, pp. 12 and 37.
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Chubet, Richard et al; “Vectors for Expression and secretion of FLAG epitope-tagged proteins in mammalian cells”;Biotechniques, vol. 20, No. 1, pp. 136-141; 1996.
Hosfield, T. et al; “Versatile epitope tagging vector for gene expression in mammalian cells”;Biotechniques; vol. 25, No. 2, pp. 306-309; 1998.
Morganti. L. et al; “Production and characterization of biologically active Ala-Ser-(His)-6-lle-Glu-Gly-Arg-human prolactin (tag-hpRL) secreted in the periplasmic space of Escherichia coli”;Biotechnology and Applied Biochemistry; vol. 23, No. 1, pp. 67-75, 1996.
Morganti, L. et al; “Synthesis and characterization of recombinant authentic human prolactin secreted intothe periplasmic space of Escherichia Coli”;Biotechnology and Applied Biochemistry; vol. 27; No. 1, pp. 63-70, 1998.
Nilsson, J. et al; “Affinity fusion strategies of detection, purification, and immobilization of recombinant proteins”;Protein Expression and Purification, vol. 11, No. 1, pp. 1-16, 1997.

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