University of Texas System

Medimmune Limited

Other

Massachusetts Institute of Technology

Medimmine, LLC

Elizabeth Sally Ward

Leslie Sydnor Johnson

William Dall'Acqua

Barbara Imperiali

Cristina Zamora

William Dall'acqua

Glycan-binding proteins, and compositions thereof, are generally described, including methods of making and using such proteins. The proteins may include scaffolds based on easily evolvable DNA-binding proteins, with binding sites able to specifically bind to mono- or disaccharides, such as monosaccharide-binding determinants, disaccharide-binding determinants, more complex carbohydrates, etc. In certain aspects, a protein may be generated starting from a small DNA-binding protein, such as Sso7d. Such glycan-binding proteins may have numerous applications, including in enzyme-linked immunosorbent assays (ELISAs), glycan characterization, cell selection, flow cytometry, histology, imaging, arrays, affinity purification, enzyme-linked visualization, binding to a target for pharmaceutical purposes, etc.

Glycan-binding proteins and related compositions and methods

Embodiments of a razor for shaving are disclosed. The razor may include a water-resistant handle. The razor may also include a blade with at least one sharp edge and one edge substantially enclosed substantially by handle. The razor may also include a blade with a plurality of edges that are interchangeable and each edge of blade may vary in sharpness.

Rookie razor

The present invention provides molecules, including IgGs, non-IgG immunoglobulins, proteins and non-protein agents, that have increased in vivo half-lives due to the presence of an IgG constant domain, or a portion thereof that binds the FcRn, having one or more amino acid modifications that increase the affinity of the constant domain or fragment for FcRn. Such proteins and molecules with increased half-lives have the advantage that smaller amounts and or less frequent dosing is required in the therapeutic, prophylactic or diagnostic use of such molecules.

Molecules with extended half-lives, compositions and uses thereof

The present invention provides molecules, including IgGs, non-IgG immunoglobulin, proteins and non-protein agents, that have increased in vivo half-lives due to the presence of an IgG constant domain, or a portion thereof that binds the FcRn, having one or more amino acid modifications that increase the affinity of the constant domain or fragment for FcRn. Such proteins and molecules with increased half-lives have the advantage that smaller amounts and or less frequent dosing is required in the therapeutic, prophylactic or diagnostic use of such molecules.

Disclosed are recombinant vectors encoding immunoglobulin-like domains and portions thereof, such as antibody Fc-hinge fragments, subfragments and mutant domains with extended biological half lives. Methods of producing large quantities of such domains, heterodimers, and fusion proteins following expression by host cells are also reported. Described are antibody Fc and Fc-hinge domains, which have the same in vivo stability as intact antibodies; and domains engineered to have increased in vivo half lives. These DNA constructs and protein domains will be useful as templates for in vitro mutagenesis and high resolution structural studies; for immunization and vaccination; and for the production of recombinant antibodies or chimeric proteins with increased stability and longevity for therapeutic and diagnostic uses.

Immunoglobin-like domains with increased half lives

Variable domain murine T-cell receptor genes have been isolated and used to construct cloning and expression vectors. V , V , and single chain V -V fragments have been expressed as secreted domains in using the vectors. The domains are secreted into the culture supernatant in milligram quantities. The single domains and the single chain T-cell receptors are folded into &bgr;-pleated sheet structures similar to those of immunoglobulin variable domains. The secreted fragments may be useful for immunization to generate anti-clonotypic antibodies, in vaccination or for high resolution structural studies. The genes encoding these domains may also serve as templates for in vitro mutagenesis and improvement of affinities of the TCR fragments for their interaction with cognate peptide-MHC complexes.

Secretion of T cell receptor fragments from recombinant host cells

Variable domain murine T-cell receptor genes have been isolated and used to construct cloning and expression vectors. V , V and single chain V -V fragments have been expressed as secreted domains in using the vectors. The domains are secreted into the culture supernatant in milligram quantities. The single domains and the single chain T-cell receptors are folded into &bgr;-pleated sheet structures similar to those of immunoglobulin variable domains. The secreted fragments may be useful for immunization to generate anti-clonotypic antibodies, in vaccination or for high resolution structural studies. The genes encoding these domains may also serve as templates for in vitro mutagenesis and improvement of affinities of the TCR fragments for their interaction with cognate peptide-MHC complexes.

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Dallas, TX, United States of America

Elizabeth Sally Ward