Expression of functional antibody fragments

a functional antibody and fragment technology, applied in the field of functional antibody fragment production, can solve the problems of difficult control of the precise nature and proportion of the recovered antibody fragment, and the reaction involves highly toxic compounds, and achieve the effect of facilitating the preparation of homogeneous recombinan
US20050244929A1Inactive Publication Date: 2005-11-03GENENTECH INC

Patent Information

Authority / Receiving Office
US · United States
Patent Type
Applications(United States)
Current Assignee / Owner
GENENTECH INC
Publication Date
2005-11-03
Estimated Expiration
Not applicable · inactive patent

Smart Images

  • Figure 1
    Figure 1
  • Figure 2
    Figure 2
  • Figure 3
    Figure 3
Patent Text Reader

Abstract

Methods for the high yield production of antibody Fv-containing polypeptides, especially Fab′ and F(ab′)2 antibody fragments are provided. Expression of heavy and light chain Fv in a microbial secretory system is followed by recovery of Fv from the periplasm under conditions that maintain a cysteine residue as a free thiol. The free thiol is reacted with free thiol of an antibody fragment of the same or differing specificity, or with agents such as diagnostic labels or therapeutic moieties. The products offer advantages of homogeneity and purity not available through the use of known methods for preparing such derivatives.
Need to check novelty before this filing date? Find Prior Art

Description

FIELD OF THE INVENTION

[0001] This invention relates to the production of functional antibody fragments in a microbial host. BACKGROUND OF THE INVENTION

[0002] Naturally occurring antibodies (immunoglobulins) comprise two heavy chains linked together by disulfide bonds and two light chains, each light chain being linked to one of the heavy chains by disulfide bonds. Each chain has an N-terminal variable domain (VH or VL) and a constant domain at its C-terminus; the constant domain of the light chain is aligned with and disulfide bonded to the first constant domain of the heavy chain, and the light chain variable domain is aligned with the variable domain of the heavy chain. The heavy chain constant region includes (in the N- to C-terminal direction) the CH1 and hinge regions. The light chain also contains a hinge domain. Particular amino acid residues are believed to form an interface between and disulfide bond the light and heavy chain variable domains, see e.g. Chothia et al., J. ...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More