Abstract: Human antibodies, preferably recombinant human antibodies, that specifically bind to human tumor necrosis factor ? (hTNF?) are disclosed. These antibodies have high affinity for hTNF? (e.g., Kd=10?8 M or less), a slow off rate for hTNF? dissociation (e.g., Koff=10?3 sec?1 or less) and neutralize hTNF? activity in vitro and in vivo. An antibody of the invention can be a full-length antibody or an antigen-binding portion thereof. The antibodies, or antibody portions, of the invention are useful for detecting hTNF? and for inhibiting hTNF? activity, e.g., in a human subject suffering from a disorder in which hTNF? activity is detrimental. Nucleic acids, vectors and host cells for expressing the recombinant human antibodies of the invention, and methods of synthesizing the recombinant human antibodies, are also encompassed by the invention.

Abstract: Human antibodies, preferably recombinant human antibodies, that specifically bind to human tumor necrosis factor ? (hTNF?) are disclosed. These antibodies have high affinity for hTNF? (e.g., Kd=10?8 M or less), a slow off rate for hTNF? dissociation (e.g., Koff=10?3 sec?1 or less) and neutralize hTNF? activity in vitro and in vivo. An antibody of the invention can be a full-length antibody or an antigen-binding portion thereof. The antibodies, or antibody portions, of the invention are useful for detecting hTNF? and for inhibiting hTNF? activity, e.g., in a human subject suffering from a disorder in which hTNF? activity is detrimental. Nucleic acids, vectors and host cells for expressing the recombinant human antibodies of the invention, and methods of synthesizing the recombinant human antibodies, are also encompassed by the invention.

Abstract: Specific binding members comprising human antibody antigen binding domains specific for human transforming growth factor beta (TGF?) bind specifically isoforms TGF?2 and TGF?1 or both, preferentially compared with TGF?3. Specific binding members may be isolated and utilized in the treatment of disease, particularly fibrotic disease and also immune/inflammatory diseases. Therapeutic utility is demonstrated using in vitro and in vivo models. Full sequence and binding information is provided, including epitope sequence information for particularly advantageous specific binding member which binds the active form of TGF?2, neutralizing its activity, but does not bind the latent member.