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           Search results for: Mouse Anti-Human TNF-alpha TNF Antibodies    

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#23324801   2013/09/18 Save this To Up

Covalently dimerized Camelidae antihuman TNFa single-domain antibodies expressed in yeast Pichia pastoris show superior neutralizing activity.

Antagonists of tumor necrosis factor alpha (TNFa) have revolutionized the treatment of selected inflammatory diseases. Recombination Camelidae variable heavy-chain domain-only TNFa antibodies (anti-TNF-VHH) have been developed to antagonize the action of human and murine TNFa. Here, we describe a strategy to obtain functional covalent dimer anti-TNF-VHH molecules with the C-terminal fusion of human IgG1 Fc domain named anti-TNF-VHH-Fc. The resulting fusion proteins were separately expressed by use of the pET28a vector in Escherichia coli ((Ec)) strain BL21 and the pPICZaA vector in Pichia pastoris ((Pp)) strain GS115, then purified by protein A affinity resin. Fc-engineered anti-(Ec)TNF-VHH-Fc was about 40 kDa and anti-(Pp)TNF-VHH-Fc was about 43 kDa. Monomeric VHH was also cloned and expressed in E. coli strain BL21, with the molecular weight of about 18 kDa. Enzyme-linked immunosorbent assay and L929 cell cytotoxicity assay demonstrated that the fusion protein anti-(Pp)TNF-VHH-Fc blocked TNFa activity more effectively than either anti-(Ec)TNF-VHH-Fc or monomeric anti-(Ec)TNF-VHH protein. We suggest that efficient disulfide bond formation using the P. pastoris expression system improves the covalent dimer anti-TNF-VHH-Fc neutralizing activity.

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#21309681   2011/08/11 Save this To Up

E-selectin is a viable route of infection for polymer-coated adenovirus retargeting in TNF-α-activated human umbilical vein endothelial cells.

E-selectin is an attractive endothelial cell surface marker in inflammation and cancer.

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#7511636   1994/05/04 Save this To Up

Leukocyte recruitment into human skin transplanted onto severe combined immunodeficient mice induced by TNF-alpha is dependent on E-selectin.

In order to study the in vivo role of E-selectin in human inflammation, we have developed a model in which human skin is transplanted onto severe combined immunodeficient (SCID) mice. The grafted skin closely resembles normal skin and retains its human vasculature. After intradermal injection of rTNF-alpha, human E-selectin was rapidly up-regulated on dermal microvessels, with significant expression (determined immunohistochemically) at 1 h postinjection and maximum expression at 2 h postinjection. To study the functional role of E-selectin, a murine Ab against human E-selectin (mAb HEL 3/2) was developed that inhibited the in vitro adhesion of both human U937 cells and murine 32D cells to TNF-alpha-stimulated human endothelial cells. After intradermal injection of TNF-alpha, large numbers of murine leukocytes migrated into the grafts within 2 h. Intravenous injection of the antihuman E-selectin mAb 3/2 completely inhibited murine white blood cell (WBC) transmigration into the skin grafts, but an isotype-matched control Ab that also bound to human endothelium had no effect. Antihuman E-selectin mAb 3/2 was also able to inhibit the migration of i.v. 51Cr-labeled human neutrophils. These findings demonstrate that E-selectin is important in early white blood cell adhesion events and is required for TNF-alpha-induced white blood cell transmigration in the human/SCID mouse chimeric model.

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