Polypeptides capable of forming antigen binding structures...

Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues – Blood proteins or globulins – e.g. – proteoglycans – platelet...

Reexamination Certificate

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

C530S387100, C530S387300, C530S388100, C530S388200, C435S007250, C424S141100, C424S153100, C536S023530

Reexamination Certificate

active

07429647

ABSTRACT:
Polypeptides capable of forming antigen binding structures specific for Rhesus D antigens include the sequences indicated in the FIGS.1ato16b. The obtained polypeptides, being Fab fragments, MAY be used directly as an active ingredient in pharmaceutical and diagnostic compositions. The Fab and their DNA sequences can also be used for the preparation of complete recombinant Anti-Rhesus D antibodies. Useful in pharmaceutical and diagnostic compositions.

REFERENCES:
patent: 2 127 434 (1984-04-01), None
patent: WO 91/07492 (1991-05-01), None
Barbas III et al., “Combinatorial Immunoglobulin Libraries on the Surface of Phage (Phabs): Rapid Selection of Antigen-Specific Fabs,”Methods: A Comparison to Methods in Enzymology, Apr. 1991; pp. 119-124, vol. 2, No. 2, Academic Press, Inc.
Chérif-Zahar et al., “Molecular cloning and protein structure of a human blood group Rh polypeptide,”Proc. Natl. Acad. Sci. USA, Aug. 1990, pp. 6243-6247, vol. 87.
Crawford et al., “Production of Human Monoclonal Antibody to Rhesus D Antigen,”The Lancet, Feb. 19, 1983, pp. 386-388, vol. 1, No. 8321.
Dziegiel et al., “Phage display used for gene cloning . . . ,” J. Immunology Methods, 1995, pp. 7-19, vol. 182.
Dziegiel et al., “Recombinant Antibody Against the Erythrocyte Antigen, Rhesus D,” Abstract No. T513,Journal of Cellular Biochemistry, Feb. 26-Apr. 17, 1994, p. 212, Supplement 18D, Wiley-Liss.
Hughes-Jones, “Human Monoclonal Antibodies and Haemolytic Disease of the Newborn,”British Journal of Haematology, Nov. 1988, pp. 263-265, vol. 70, No. 3, Blackwell Scientific Publications.
Issitt, “Genetics of the Rh blood group system: some current concepts,”Medical Laboratory Sciences, 1988, pp. 395-404, vol. 45, Blackwell Scientific Publications.
Kozbor et al., “The production of monoclonal antibodies from human lymphocytes,”Immunology Today, 1983, pp. 72-79, 1983, vol. 4, No. 3, Elsevier Science Publishers B.V.
Le Van Kim et al., “Molecular cloning and primary structure of the human blood group RhD polypeptide,”Proc. Natl. Acad. Sci. USA, Nov. 1992, pp. 10925-10929, vol. 89.
Marks et al., “Human Antibody Fragments Specific . . . ,” Biotechnology, 1993, pp. 1145-1149, vol. 11.
Mouro et al., “Rearrangements of the Blood Group RhD Gene Associated with the DVICategory Phenotype,”Blood, Feb. 15, 1994, pp. 1129-1135, vol. 83, No. 4, The American Society of Hematology.
Paradis et al., “Protective Effect of the Membrane Skeleton on the Immunologic Reactivity of the Human Red Cell Rh0(D) Antigen,”The Journal of Immunology, Jul. 1, 1986, pp. 240-244, vol. 137, No. 1, The American Association of Immunologies.
Persson et al., “Generation of diverse high-affinity human monoclonal antibodies by repertoire cloning,”Proc. Natl. Acad. Sci. USA, Mar. 1991, pp. 2432-2436, vol. 88.
Race et al. (Eds.),Blood Groups in Man, 1975, Table of Contents Only, Blackwell Scientific Publications.
Selinger, “Immunoprophylaxis for rhesus disease—expensive but worth it?”British Journal of Obstetrics and Gynaecology, Jun. 1991, pp. 509-512, vol. 98, No. 6, Blackwell Scientific Publications.
Siegel et al., “Expression and Characterization of Recombinant Anti-Rh(D) . . . ,” Blood, 1994, pp. 2334-2344, vol. 83.
Siegel et al., “Isolation of Human Anti-Red Blood Cell Antibodies by Repertoire Cloning,”Annals New York Academy of Sciences, Sep. 29, 1995, pp. 547-558, vol. 764, New York Academy of Sciences, USA.
Sziegiel et al., J. of Cellular Biochemistry, Feb. 26-Apr. 17, 1994. front page only.
Tippett et al., “The Rh Antigen D: Partial D Antigens and Associated Low Incidence Antigens,”Vox Sanguinis, Feb. 1996, pp. 123-131, vol. 70, S. Karger AG, Basel.
Vogel et al., “Human anti-IgE antibodies by repertoire cloning,”Eur. J. Immunol., May 1994, pp. 1200-1207, vol. 24, VCH Verlagsgesellschaft mbH, Weinheim.
Williamson et al., “Human monoclonal antibodies against a plethora of viral pathogens from single combinatorial libraries,”Proc. Natl. Acad. Sci. USA, May 1993, pp. 4141-4145, vol. 90.
Zebedee et al., “Human combinatorial antibody libraries to hepatitis B surface antigen,”Proc. Natl. Acad. Sci. USA, Apr. 1992, pp. 3175-3179, vol. 89.
Clackson et al., “Making Antibody Fragments Using Phage Display Libraries,”Nature352:624-28 (1991).
Griffiths, “Production of Human Antibodies Using Bacteriophage,”Curr Opin Immunol5(2):263-7 (1993)—(abstract only).
Dziegiel et al., “Phage Display Use for Gene Cloning of Human Recombinant Antibody Against the Erythrocyte Surface Antigen, Rhesus D,”J. of Immunological Methods, 182:7-19 (1995).
Marks et al., “Human Antibody Fragments Specific for Human Blood Group Antigens from a Phage Display Library,”Bio/Technology11:1145-1149 (1993).
Slegel et al., “Expression and Characterization of Recombinant Anti-Rh(D) Antibodies on Filamentous Phage: A Model System for Isolating Human Red Blood Cell Antibodies by Repertoire Cloning,”Blood83(8):2334-2344 (1994).

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Polypeptides capable of forming antigen binding structures... does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Polypeptides capable of forming antigen binding structures..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Polypeptides capable of forming antigen binding structures... will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-3978502

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.