Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P04626 (erbB-2)
 5,251 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Single-chain Fv proteins containing a COOH-terminal cysteine (sFv') were constructed by using an antidigoxin 26.10 sFv and an anti-c-erbB-2 741F8 sFv. The fully active sFv' proteins were prepared by expression in Escherichia coli as insoluble inclusion bodies, followed by in vitro refolding using glutathione redox buffers and purification. The COOH-terminal cysteines of the refolded sFv' proteins were protected by a blocking group presumed to be the glutathionyl peptide, which was easily and selectively removed by gentle reduction. Air oxidation of the reduced sFv' monomers resulted in the efficient formation of disulfide-linked sFv' homodimers, designated (sFv')2, which were stable under oxidizing conditions and relatively slow to be disrupted under reducing conditions. The (26-10-1 sFv')-(741F8-1 sFv') heterodimer was prepared and possessed dual-antigen specificity; the active bispecific (sFv')2 dimerized under native conditions, apparently as a manifestation of self-association by the 741F8 sFv' subunit. Biodistribution and imaging studies that were performed on mice bearing human SK-OV-3 tumor xenografts that express the c-erbB-2 as a cell surface antigen were reviewed. Radioiodinated 741F8-2 (sFv')2 homodimer localized to the tumors with high specificity, as evidenced by excellent tumor:normal tissue ratios. Sagittal section autoradiography of whole animals 24 h after administration of antibody species revealed that 741F8 (sFv')2 produced a stronger tumor image than comparable doses of the 741F8 Fab, monomeric sFv', and the 26-10 (sFv')2 control without the high nonspecific background distribution of the 741F8 IgG.
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PMID:Targeting c-erbB-2 expressing tumors using single-chain Fv monomers and dimers. 749 81

Monoclonal antibodies (mAbs) were modified with a photo-cross linker, sulfosuccinimidyl 2-(m-azido-o-nitrobenzamido)-ethyl-1,3'-dithiopropionate (SAND), and their efficacy in immunohistochemical staining of tissue sections was examined comparatively with that of unmodified mAbs. mAbs used were HBJ127 and SV2-61 gamma which recognized a proliferation-associated human gp125 cell surface antigen and a human c-erbB-2 protooncogene product, respectively. Both mAbs could stain relevant cancer tissue in frozen sections but not that in paraffin sections. Whereas SAND-modified mAbs intensely stained the cancer tissue in paraffin sections too, and the UV irradiation to SAND-modified mAb-treated tissue sections further increased the intensity of the staining. Scatchard plot analysis using 125I-labeled mAbs indicated that the augmentation of staining capacity by the SAND modification is due to the increase of the mAb amount capable of binding to the antigen.
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PMID:Efficient immunostaining of tissue sections with chemically modified monoclonal antibody. 769 66