Human Antibody Library | Domain Antibody Library

We are pleased to announce the availability of the Domain Antibody Phagemid library constructed by Dr Daniel Christ (formally of the MRC Laboratory of Molecular Biology, Cambridge UK and currently based at the Garvan Institute, Sydney, Australia).

 

This library offers significant advantages over the hugely successful Tomlinson I + J library introduced by us in 2002.

Applications

This artificial library of antibodies can be used to derive binders to almost any target molecule using phage display and selection. These binders can be used for the same applications as conventional monoclonal antibodies (ELISA, Western blotting, FACS, immunohistochemistry), but can be isolated in a fraction of the time and without the need for animal immunisation.

 

Phage-antibody libraries have been used successfully in hundreds of molecular biology labs worldwide to derive highly specific antibody reagents to a wide range of different proteins, peptides or small molecule compounds

Description

This library is based on a VH framework (V3-23/D47). Diversity was introduced into the antigen binding domains by PCR mutagenesis into CDR1, CDR2 and CDR3. There are many benefits to this library.

  • Produced binders to the model antigens refold without major loss of antigen-binding activity upon cooling.
  • Antibodies selected maintain antigen-binding activity after up to 25 cycles of heat denaturation, rivalling the heat resistance of thermophilic protein such as Taq polymerase.
  • Repertoire withstands heat-induced aggregation on phage.

These benefits offer a wide range of diagnostic and therapeutic research applications and can further maximise the number of binders to your antigen of interest.

Specifications

This library is supplied as a single kit containing:

  • Phagemid antibody library (~3x10 9 )
  • Helper phage KM13
  • Host strain TG1Tr
  • Optimised antibody expression strain HB2151
  • Controls: anti-beta-galactosidase & anti-bovine ubiquitin antibodies
  • detailed protocol

 

For further information and troubleshooting tips please see the  detailed protocol

 

THIS LIBRARY IS PROVIDED AS A RESEARCH TOOL AND IS NOT INTENDED TO BE USED IN DRUG DISCOVERY AS THE BASIS FOR NOVEL THERAPEUTIC AGENTS.  THE MTA UNDER WHICH THIS PRODUCT IS RELEASED SETS OUT THE RIGHTS THAT THE ORIGINATING ORGANISATION (MEDICAL RESEARCH COUNCIL) IS ABLE TO GRANT.  SHOULD YOU WISH TO COMMERCIALISE AN ANTIBODY DEVELOPED FROM THIS LIBRARY, IT IS LIKELY THAT YOU WILL REQUIRE A LICENSE FROM SEVERAL COMPANIES, AT LEAST ONE OF WHICH IS ONLY AVAILABLE TO COMMERCIAL ENTITIES, NOT ACADEMIC ORGANISATIONS.

 

Ordering details

Product Code Name Price
6001_hDAb Human Domain Antibody Constructs (DAb) £313.00
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Supporting publications

 

Niccheri, F., Real-Fernàndez, F., Ramazzotti, M., Lolli, F., Rossi, G., Rovero, P. and Degl'Innocenti, D. (2014),
J. Mol. Recognit., 27: 618–626. doi:10.1002/jmr.2386

 

Lee CM, Iorno N, Sierro F, Christ D.
Selection of human antibody fragments by phage display.
Nat Protoc. 2007;2(11):3001-8.


Dudgeon K, Famm K, Christ D.
Sequence determinants of protein aggregation in human VH domains.
Protein Eng Des Sel. 2008 Oct 28.


Famm K, Hansen L, Christ D, Winter G.
Thermodynamically stable aggregation-resistant antibody domains through directed evolution.
J Mol Biol. 2008 Feb 29;376(4):926-31.


Christ D, Famm K, Winter G.
Repertoires of aggregation-resistant human antibody domains.
Protein Eng Des Sel. 2007 Aug;20(8):413-6.

Christ D, Famm K, Winter G.
Tapping diversity lost in transformations--in vitro amplification of ligation reactions.
Nucleic Acids Res. 2006;34(16):e108.