Method for producing antibody fragments

Organic compounds -- part of the class 532-570 series – Organic compounds – Carbohydrates or derivatives

Reexamination Certificate

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Details

C536S023100, C536S023500, C435S440000, C435S463000, C435S320100

Reexamination Certificate

active

10122434

ABSTRACT:
An expression library comprising a repertoire of nucleic acid sequences cloned from a non-immunised source, each nucleic acid sequence encoding at least part of a variable domain of a heavy chain derived from an immunoglobulin naturally devoid of light chains (VHH) wherein the extent of sequence variability in the library is enhanced compared to the corresponding naïve expression library by introducing mutations in one or more of the complementarity determining regions (CDRs) of the nucleic acid sequences or by generating alternative combinations of CDR and framework sequences not naturally present in the naïve library repertoire. Also disclosed is the use of such a library in preparing antibodies, more particularly antibody fragments.

REFERENCES:
patent: 584421 (1994-03-01), None
patent: WO 9425591 (1994-11-01), None
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Aujame et al. (1997), “High affinity human antibodies by phage display,”Human Antibodies8(4):155-168.
Davies et al. (1995), “Antibody VH domains as small recognition units,” Bio/Technology 13(5):457-479.
Finnern et al. (1995), “Molecular characteristics of anti-self antibody fragments against neutrophil cytoplasmic antigens from human V gene phage display libraries,” Clin Exp Immunol 102(3):566-574.
Ghahroudi et al. (1997), “Selection and identification of single domain antibody fragments from camel heavy-chain antibodies,” FEBS Lett 414:521-526.
Hoogenboom et al. (1998), “Antibody phage display technology and its applications,” Immunotechnology 4:1-20.
Nguyen et al. (1998), “The specific variable domain of camel heavy-chain antibodies is encoded in the germline,” J Mol Biol 275:413-418.

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