PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9748318-6 1998 275, 245-253], were found to be additive and transferable to the cysteine-restored variant of the A48 scFv, thereby generating extremely stable VH domains. Cysteine 65-73 immunglobulin heavy chain variable region Homo sapiens 102-106 15157618-2 2004 For this purpose, we introduced an additional cysteine residue at the C-terminus of the scFv fragment. Cysteine 46-54 immunglobulin heavy chain variable region Homo sapiens 88-92 11162401-4 2001 The C-termini of the scFv antibody fragments contain 1-3 cysteine residues that are separated by a hydrophilic linker (GGSSGGSSGS) from the binding domain and are accessible for site-specific functionalization with thiol-reactive reagents. Cysteine 57-65 immunglobulin heavy chain variable region Homo sapiens 21-25 11162401-12 2001 Our results indicate that the P. pastoris expression system is useful for the large-scale production of cysteine-functionalized alpha-ED-B scFv antibody fragments. Cysteine 104-112 immunglobulin heavy chain variable region Homo sapiens 139-143 12121127-4 2002 In this article, we tested by quantitative biodistribtution analysis whether conjugation to TAT peptides could improve the tumor targeting properties of scFv(L19)-Cys: an engineered human antibody fragment specific for the ED-B domain of fibronectin, a marker located in the modified extracellular matrix surrounding tumor neovasculature. Cysteine 163-166 immunglobulin heavy chain variable region Homo sapiens 153-157 12121127-6 2002 However, conjugation of scFv(L19)-Cys to TAT peptides resulted in a severely reduced tumor targeting performance compared to the unconjugated antibody, as measured in murine F9 teratocarcinoma-bearing mice, after intravenous injection of the radiolabeled antibody preparations. Cysteine 34-37 immunglobulin heavy chain variable region Homo sapiens 24-28 12489850-9 2002 The scFv-cys targets the cationic liposome-DNA complex (lipoplex) to tumor cells and enhances the transfection efficiencies both in vitro and in vivo in a variety of human tumor models. Cysteine 9-12 immunglobulin heavy chain variable region Homo sapiens 4-8 11320404-2 2001 The scFv was constructed from a monoclonal antibody directed against pIgR and a cysteine residue was added at the carboxyl end to facilitate its conjugation to polylysine (polyK) via the heterobifunctional cross-linker SPDP. Cysteine 80-88 immunglobulin heavy chain variable region Homo sapiens 4-8 11320404-3 2001 ScFv-cys was expressed in Drosophila S2 cells and purified to homogeneity using conventional column chromatography. Cysteine 5-8 immunglobulin heavy chain variable region Homo sapiens 0-4 11320404-6 2001 Receptor-bearing MDCK cells were readily transfected by scFv-cys containing, pIgR directed complexes, and expression could be blocked by addition of excess human secretory component (SC), the extracellular portion of pIgR. Cysteine 61-64 immunglobulin heavy chain variable region Homo sapiens 56-60 9636161-1 1998 Antibody single-chain Fv fragment (scFv) molecules that are specific for fluorescein have been engineered with a C-terminal cysteine for a directed immobilization on a flat gold surface. Cysteine 124-132 immunglobulin heavy chain variable region Homo sapiens 35-39 9551966-9 1998 The CD8alpha-derived hinge successfully performs this task in chimeric scFv-Syk receptors regardless of its cysteine content. Cysteine 108-116 immunglobulin heavy chain variable region Homo sapiens 71-75 9637257-1 1998 A fully functional cysteine-free derivative of the intrinsically stable anti-HER2 scFv fragment hu4D5-8 was generated by replacing the disulfide forming cysteine residues in VH and VL with the amino acid combination valine-alanine in both domains. Cysteine 19-27 immunglobulin heavy chain variable region Homo sapiens 82-86 9637257-1 1998 A fully functional cysteine-free derivative of the intrinsically stable anti-HER2 scFv fragment hu4D5-8 was generated by replacing the disulfide forming cysteine residues in VH and VL with the amino acid combination valine-alanine in both domains. Cysteine 153-161 immunglobulin heavy chain variable region Homo sapiens 82-86 9026037-2 1997 Anti-CD19 scFv FVS191cys was constructed by engineering a cysteine residue at the C terminus of the V1, domain of scFv FVS191. Cysteine 58-66 immunglobulin heavy chain variable region Homo sapiens 10-14 9194170-6 1997 The double mutant scFv (Q,S) proved to be very stable in vitro: no loss of activity was observed after storage for 1 month at 4 degrees C, while the activity of scFv containing a cysteine residue in CDR-H3 decreased by more than half. Cysteine 179-187 immunglobulin heavy chain variable region Homo sapiens 18-22 9194170-6 1997 The double mutant scFv (Q,S) proved to be very stable in vitro: no loss of activity was observed after storage for 1 month at 4 degrees C, while the activity of scFv containing a cysteine residue in CDR-H3 decreased by more than half. Cysteine 179-187 immunglobulin heavy chain variable region Homo sapiens 161-165 9026037-2 1997 Anti-CD19 scFv FVS191cys was constructed by engineering a cysteine residue at the C terminus of the V1, domain of scFv FVS191. Cysteine 58-66 immunglobulin heavy chain variable region Homo sapiens 114-118 9636285-3 1995 Moreover, we have compared the redox state of ScFv fragments targeted to the secretory compartment, the cytosol and the mitochondria, and demonstrated that cysteine residues in ScFv targeted to the secretory compartments and to the mitochondria are oxidized. Cysteine 156-164 immunglobulin heavy chain variable region Homo sapiens 46-50 8965166-0 1996 Technetium-99m radiolabeling using a phage-derived single-chain Fv with a C-terminal cysteine. Cysteine 85-93 immunglobulin heavy chain variable region Homo sapiens 51-66 8575837-4 1995 The scFv was refolded in a cystine/cysteine redox buffer and purified to homogeneity using anion exchange chromatography. Cysteine 35-43 immunglobulin heavy chain variable region Homo sapiens 4-8 9636285-3 1995 Moreover, we have compared the redox state of ScFv fragments targeted to the secretory compartment, the cytosol and the mitochondria, and demonstrated that cysteine residues in ScFv targeted to the secretory compartments and to the mitochondria are oxidized. Cysteine 156-164 immunglobulin heavy chain variable region Homo sapiens 177-181 30130449-3 2018 To improve biochemical stability, cysteine residues are often engineered on the heavy- and light-chain regions of the scFv to form an intrachain disulfide bond. Cysteine 34-42 immunglobulin heavy chain variable region Homo sapiens 118-122 7628706-1 1995 To facilitate the purification and conjugation of single-chain antibodies (scFv) selected from a phage display library, we have incorporated His6, an amber stop codon and a C-terminal Cys into a surface expression vector. Cysteine 184-187 immunglobulin heavy chain variable region Homo sapiens 75-79 31733318-4 2019 MAIN METHODS: An ScFv was conjugated with superparamagnetic iron oxide (SPIO) or indocyanine green (ICG) via a linker by utilizing the reaction between cysteine and maleimide. Cysteine 152-160 immunglobulin heavy chain variable region Homo sapiens 17-21 31332748-3 2019 This is of high importance as nonspecific antibody modification often involves attachment to free cysteine or lysine amino acids which may reside in the active site, leading to reduced antigen binding.In this chapter, we outline a facile and versatile chemoenzymatic approach for production of targeted nanocarrier scFv conjugates using the bacterial trans-peptidase Sortase A (Srt A). Cysteine 98-106 immunglobulin heavy chain variable region Homo sapiens 315-319 32569010-4 2020 MATERIALS AND METHODS: We recombinantly expressed the Thy1-scFv with a carboxy-terminus cysteine residue to facilitate its thioether conjugation to the PEGylated MBs presenting with maleimide functional groups. Cysteine 88-96 immunglobulin heavy chain variable region Homo sapiens 59-63 31535232-4 2019 In this study, a novel fusion protein, ScFv-Cys containing a single chain variable fragment (ScFv) and an additional C-terminal cysteine residue, was generated at a rate of 10 mg/L of bacterial culture and purified at 95% by Ni-NTA chromatography. Cysteine 44-47 immunglobulin heavy chain variable region Homo sapiens 39-43 31535232-4 2019 In this study, a novel fusion protein, ScFv-Cys containing a single chain variable fragment (ScFv) and an additional C-terminal cysteine residue, was generated at a rate of 10 mg/L of bacterial culture and purified at 95% by Ni-NTA chromatography. Cysteine 44-47 immunglobulin heavy chain variable region Homo sapiens 93-97 31535232-4 2019 In this study, a novel fusion protein, ScFv-Cys containing a single chain variable fragment (ScFv) and an additional C-terminal cysteine residue, was generated at a rate of 10 mg/L of bacterial culture and purified at 95% by Ni-NTA chromatography. Cysteine 128-136 immunglobulin heavy chain variable region Homo sapiens 39-43 31535232-5 2019 Subsequently, the recombinant ScFv-Cys was coupled with malPEG2000-DSPE and incorporated into liposomes to generate the immunoliposomes. Cysteine 35-38 immunglobulin heavy chain variable region Homo sapiens 30-34 30352511-5 2018 Two cysteines were judiciously incorporated at the beginning of the scFv hexahistidine tag, in order to allow controlled bioconjugation of a heterobifunctional linker including a second generation maleimide (SGM), either cleavable (for monomethyl auristatin E) or noncleavable (for monomethyl auristatin F). Cysteine 4-13 immunglobulin heavy chain variable region Homo sapiens 68-72 30130449-6 2018 Structural characterization studies showed that the size variants resulted from the engineered disulfide bond on the scFv, whereby the engineered disulfide was found to be either open or unable to form an intrachain disulfide bond due to cysteinylation or glutathionylation of the cysteines. Cysteine 281-290 immunglobulin heavy chain variable region Homo sapiens 117-121 30130449-7 2018 Furthermore, the scFv engineered cysteines also formed intermolecular disulfide bonds, leading to the formation of highly stable dimers and aggregates. Cysteine 33-42 immunglobulin heavy chain variable region Homo sapiens 17-21 29737435-4 2018 The scFv monomer was linked to maleimide-DTPA via unpaired cysteine at the scFv C-terminus, followed by chelation with gadolinium (Gd). Cysteine 59-67 immunglobulin heavy chain variable region Homo sapiens 4-8 30405887-5 2018 The resulting scFv-hERG1-Cys showed much higher stability and protein yield, increased affinity and more advantageous binding kinetics, compared to the "native" anti-hERG1scFv. Cysteine 25-28 immunglobulin heavy chain variable region Homo sapiens 14-18 30405887-6 2018 The scFv-hERG1-Cys was hence chosen and characterized: it showed a good binding to the native hERG1 antigen expressed on cells, was stable in serum and displayed a fast pharmacokinetic profile once injected intravenously in nude mice. Cysteine 15-18 immunglobulin heavy chain variable region Homo sapiens 4-8 30405887-8 2018 Finally, the in vivo distribution of an Alexa Fluor 750 conjugated scFv-hERG1-Cys was evaluated both in healthy and tumor-bearing nude mice, showing a good tumor-to-organ ratio, ideal for visualizing hERG1-expressing tumor masses in vivo. Cysteine 78-81 immunglobulin heavy chain variable region Homo sapiens 67-71 30405887-9 2018 In conclusion, the scFv-hERG1-Cys possesses features which make it a suitable tool for application in cancer molecular imaging. Cysteine 30-33 immunglobulin heavy chain variable region Homo sapiens 19-23 24262918-5 2014 Moreover, scFv and scFabDeltaC antibody variants retained improved antigen binding after subcloning into the single gene encoded IgG-like formats scFv-Fc or scIgG, but lost affinity after conversion into IgGs.Only affinity maturation using the Fab-like FabDeltaC format, which does not contain the carboxy terminal cysteines, allowed successful selection of molecules with improved binding that was retained after conversion to IgG. Cysteine 315-324 immunglobulin heavy chain variable region Homo sapiens 10-14 29662239-3 2018 In transfected HEK293A cells, 3B12A scFv recapitulated the affinity of the full-length MAb to mislocalised TDP-43 with a defective nuclear localising signal and to a TDP-43 inclusion mimic with cysteine-to-serine substitution at RRM1. Cysteine 194-202 immunglobulin heavy chain variable region Homo sapiens 36-40 28643153-0 2018 A 3E8.scFv.Cys-IR800 Conjugate Targeting TAG-72 in an Orthotopic Colorectal Cancer Model. Cysteine 11-14 immunglobulin heavy chain variable region Homo sapiens 6-10 28643153-3 2018 PROCEDURES: An engineered single-chain variable fragment of 3E8 MAb (targeted to TAG-72), appending a C-terminal cysteine residue (3E8.scFv.Cys), was created and reacted with IRDye800-maleimide. Cysteine 113-121 immunglobulin heavy chain variable region Homo sapiens 135-139 28643153-3 2018 PROCEDURES: An engineered single-chain variable fragment of 3E8 MAb (targeted to TAG-72), appending a C-terminal cysteine residue (3E8.scFv.Cys), was created and reacted with IRDye800-maleimide. Cysteine 140-143 immunglobulin heavy chain variable region Homo sapiens 135-139 28643153-4 2018 3E8.scFv.Cys-IR800 identity and purity were verified by MALDI-TOF mass spectra and 800 nm detected size exclusion column HPLC. Cysteine 9-12 immunglobulin heavy chain variable region Homo sapiens 4-8 28643153-6 2018 We further evaluated the imaging ability and receptor-specific binding of 3E8.scFv.Cys-IR800 in an orthotopic LS-174 T mouse model. Cysteine 83-86 immunglobulin heavy chain variable region Homo sapiens 78-82 28643153-8 2018 A 1 nmol dose of 3E8.scFv.Cys-IR800 via intraperitoneal injection administration was sufficient to produce high tumor to background fluorescence contrast. Cysteine 26-29 immunglobulin heavy chain variable region Homo sapiens 21-25 28643153-9 2018 Blocking competition studies both in vitro and in vivo using a different blocking protein, 3E8DeltaCH2, demonstrated 3E8.scFv.Cys-IR800 binding specificity for TAG-72 antigen. Cysteine 126-129 immunglobulin heavy chain variable region Homo sapiens 121-125 28643153-10 2018 CONCLUSIONS: 3E8.scFv.Cys-IR800 shows properties useful in a clinically viable OSN agent for colorectal cancer. Cysteine 22-25 immunglobulin heavy chain variable region Homo sapiens 17-21 29067565-4 2017 The scFv, J591c-scFv, was engineered with a C-terminal cysteine. Cysteine 55-63 immunglobulin heavy chain variable region Homo sapiens 16-20 28755586-4 2017 This scFv contains 5 Cys residues: VH22 and VH92 in the variable heavy chain (VH) and VL23, VL87 and VL88 in the variable light chain (VL). Cysteine 21-24 immunglobulin heavy chain variable region Homo sapiens 5-9 28126683-3 2017 METHODS: An anti-prostate membrane antigen (PSMA) scFv with a site-specific cysteine was expressed and evaluated in a prostate cancer xenograft model by Cu-64 PET imaging. Cysteine 76-84 immunglobulin heavy chain variable region Homo sapiens 50-54 28126683-4 2017 To enhance tumor accumulation, the scFv-cys was conjugated to the co-polymer DSPE-PEG-maleimide that spontaneously assembled into a homogeneous multivalent lipid nanoparticle (LNP). Cysteine 40-43 immunglobulin heavy chain variable region Homo sapiens 35-39 29553717-4 2018 We developed two novel bioengineered scFv carrying two cysteines located (i) at the end (4D5.1-cys2) or (ii) at the beginning (4D5.2-cys2) of its hexahistidine tag. Cysteine 55-64 immunglobulin heavy chain variable region Homo sapiens 37-41 29553717-6 2018 Our data indicated that the insertion of cysteines at the beginning of the hexahistidine tag was allowed to obtain nearly 2-fold conjugation efficiency (13 scFv/NP) compared to NMs using classical maleimide. Cysteine 41-50 immunglobulin heavy chain variable region Homo sapiens 156-160 29067565-4 2017 The scFv, J591c-scFv, was engineered with a C-terminal cysteine. Cysteine 55-63 immunglobulin heavy chain variable region Homo sapiens 4-8 32481827-4 2013 The Cys and 6 x His functionalities were exploited as orthogonal reactive groups driving the scFv conjugation to MNPs. Cysteine 4-7 immunglobulin heavy chain variable region Homo sapiens 93-97 32481827-3 2013 The scFv was genetically engineered to introduce a cysteine residue inside the loop sequence bridging the VH and VL lobes of the molecule and a histidine tag at the C-terminus in the VL fragment. Cysteine 51-59 immunglobulin heavy chain variable region Homo sapiens 4-8 18790696-7 2008 Moreover, scFv mE12 was endowed with an additional cysteine residue in the linker region and applied for the generation of anti-endoglin scFv immunoliposomes capable of selectively binding to endoglin-expressing cells. Cysteine 51-59 immunglobulin heavy chain variable region Homo sapiens 10-14 22484084-6 2012 To enhance its stability and neutralizing potency, a disulfide-stabilized scFv, ds-FV57, was also derived by introduction of cysteines at V(H)44 and V(L)100. Cysteine 125-134 immunglobulin heavy chain variable region Homo sapiens 74-78 22484084-7 2012 Furthermore, the cysteine at V(L)85 of ds-FV57 was mutated to serine to construct ds-FV57(VL85Ser) in order to avoid potential mis-formed disulfide bonds which would alter the affinity of the scFv. Cysteine 17-25 immunglobulin heavy chain variable region Homo sapiens 192-196 19327975-2 2009 The scFv-cys stabilized gold NPs were used to develop a highly sensitive colorimetric immunosensor. Cysteine 9-12 immunglobulin heavy chain variable region Homo sapiens 4-8 19327975-3 2009 The scFv-cys stabilized gold NPs were characterized by UV-vis spectra, transmission electron microscope (TEM) and FTIR. Cysteine 9-12 immunglobulin heavy chain variable region Homo sapiens 4-8 19327975-4 2009 After adding the antigen rabbit IgG, the solution of scFv-cys stabilized gold NPs shows obvious visible color change from deep red to light purple due to the aggregation of the gold nanoparticles. Cysteine 58-61 immunglobulin heavy chain variable region Homo sapiens 53-57 19327975-5 2009 Based on the colorimetric aggregation of scFv-cys stabilized gold NPs, the immunosensor exhibits high sensitivity with a detection limit of 1.7 nM and good specificity. Cysteine 46-49 immunglobulin heavy chain variable region Homo sapiens 41-45 18790696-7 2008 Moreover, scFv mE12 was endowed with an additional cysteine residue in the linker region and applied for the generation of anti-endoglin scFv immunoliposomes capable of selectively binding to endoglin-expressing cells. Cysteine 51-59 immunglobulin heavy chain variable region Homo sapiens 137-141 17944370-1 2007 To constructed the recombinant human anti-rabies virus ScdsFv, cys sites were introduced into framework region (FR) of VH and VL genes which were amplified from human anti-rabies virus ScFv respectively using genetic point mutation technology. Cysteine 63-66 immunglobulin heavy chain variable region Homo sapiens 185-189 18290668-6 2008 A 42-fold improvement of detection limits using MUA/A10B scFv-RG3 (less than 0.2 nM experimentally determined) was achieved compared to A10B Fab antibody and a 5-fold improvement was observed compared to A10B scFv that was engineered with a cysteine in the linker sequence. Cysteine 241-249 immunglobulin heavy chain variable region Homo sapiens 57-61 16760193-6 2006 However, the location of the engineered cysteine in these di-scFv-c did influence PEGylation efficiency of this free thiol; higher PEGylation efficiency occurred with this cysteine in the inter-scFv linkage. Cysteine 40-48 immunglobulin heavy chain variable region Homo sapiens 61-65 17613658-5 2007 These scFv molecules were genetically modified to express an additional cysteine residue at the C-terminus allowing a defined and site-directed conjugation. Cysteine 72-80 immunglobulin heavy chain variable region Homo sapiens 6-10 16898953-6 2006 The affinity of scFv for the disintegrin/TSP1/cysteine-rich/spacer domain was determined by surface plasmon resonance analysis and the dissociation constants ranged from 3 to 254 nM. Cysteine 46-54 immunglobulin heavy chain variable region Homo sapiens 16-20 16868004-9 2006 To increase serum half-life, a branched 40 kDa PEG-polymer was coupled to the most potent GM-CSF-neutralizing scFv (3077) via an additional C-terminal cysteine. Cysteine 151-159 immunglobulin heavy chain variable region Homo sapiens 110-114 16760193-6 2006 However, the location of the engineered cysteine in these di-scFv-c did influence PEGylation efficiency of this free thiol; higher PEGylation efficiency occurred with this cysteine in the inter-scFv linkage. Cysteine 172-180 immunglobulin heavy chain variable region Homo sapiens 194-198 16192357-3 2005 We introduced a cysteine residue at the C terminus of each scFv construct to allow covalent attachment to gold-coated sensor interfaces in directed orientation. Cysteine 16-24 immunglobulin heavy chain variable region Homo sapiens 59-63 16427706-1 2006 Single chain variable fragment (scFv) molecules were selected from a synthetic phage display library then cloned into a generic vector for expression of the scFv fused to the light chain constant domain of human immunoglobulin with a C-terminal cysteine residue (scFvC(L)cys). Cysteine 245-253 immunglobulin heavy chain variable region Homo sapiens 32-36 16427706-1 2006 Single chain variable fragment (scFv) molecules were selected from a synthetic phage display library then cloned into a generic vector for expression of the scFv fused to the light chain constant domain of human immunoglobulin with a C-terminal cysteine residue (scFvC(L)cys). Cysteine 245-253 immunglobulin heavy chain variable region Homo sapiens 157-161 16427706-1 2006 Single chain variable fragment (scFv) molecules were selected from a synthetic phage display library then cloned into a generic vector for expression of the scFv fused to the light chain constant domain of human immunoglobulin with a C-terminal cysteine residue (scFvC(L)cys). Cysteine 245-248 immunglobulin heavy chain variable region Homo sapiens 32-36 16427706-1 2006 Single chain variable fragment (scFv) molecules were selected from a synthetic phage display library then cloned into a generic vector for expression of the scFv fused to the light chain constant domain of human immunoglobulin with a C-terminal cysteine residue (scFvC(L)cys). Cysteine 245-248 immunglobulin heavy chain variable region Homo sapiens 157-161 16427706-5 2006 ScFv molecules lacking the C-terminal cysteine performed poorly in similar experiments. Cysteine 38-46 immunglobulin heavy chain variable region Homo sapiens 0-4 16492049-2 2006 The method relies on the conjugation of a glutathione monolayer-protected gold cluster (MPC) with a single chain Fv antibody fragment (scFv), mutated to present an exposed cysteine residue. Cysteine 172-180 immunglobulin heavy chain variable region Homo sapiens 135-139 15679346-3 2005 The recombinant single-chain fragment variable (scFv) antibody contained a cysteine within the linker amino acid sequence used to join the scFv variable heavy and light chains. Cysteine 75-83 immunglobulin heavy chain variable region Homo sapiens 48-52 15679346-4 2005 The presence of cysteine induced the scFv construct to self-assemble as a densely packed rigid monolayer on the gold surface of a quartz crystal microbalance. Cysteine 16-24 immunglobulin heavy chain variable region Homo sapiens 37-41 15679346-8 2005 We demonstrate here that the use of scFv containing a cysteine within the scFv linker sequence (i.e., scFv-cys) for preparation of biosensor surfaces markedly increases the density of available antigen-binding sites, yielding a system that is highly selective, rapid, and capable of detecting low concentrations of antigens in complex samples. Cysteine 54-62 immunglobulin heavy chain variable region Homo sapiens 36-40 15679346-8 2005 We demonstrate here that the use of scFv containing a cysteine within the scFv linker sequence (i.e., scFv-cys) for preparation of biosensor surfaces markedly increases the density of available antigen-binding sites, yielding a system that is highly selective, rapid, and capable of detecting low concentrations of antigens in complex samples. Cysteine 54-62 immunglobulin heavy chain variable region Homo sapiens 74-78 15679346-8 2005 We demonstrate here that the use of scFv containing a cysteine within the scFv linker sequence (i.e., scFv-cys) for preparation of biosensor surfaces markedly increases the density of available antigen-binding sites, yielding a system that is highly selective, rapid, and capable of detecting low concentrations of antigens in complex samples. Cysteine 54-62 immunglobulin heavy chain variable region Homo sapiens 74-78 15679346-8 2005 We demonstrate here that the use of scFv containing a cysteine within the scFv linker sequence (i.e., scFv-cys) for preparation of biosensor surfaces markedly increases the density of available antigen-binding sites, yielding a system that is highly selective, rapid, and capable of detecting low concentrations of antigens in complex samples. Cysteine 54-57 immunglobulin heavy chain variable region Homo sapiens 36-40 15679346-8 2005 We demonstrate here that the use of scFv containing a cysteine within the scFv linker sequence (i.e., scFv-cys) for preparation of biosensor surfaces markedly increases the density of available antigen-binding sites, yielding a system that is highly selective, rapid, and capable of detecting low concentrations of antigens in complex samples. Cysteine 54-57 immunglobulin heavy chain variable region Homo sapiens 74-78 15679346-8 2005 We demonstrate here that the use of scFv containing a cysteine within the scFv linker sequence (i.e., scFv-cys) for preparation of biosensor surfaces markedly increases the density of available antigen-binding sites, yielding a system that is highly selective, rapid, and capable of detecting low concentrations of antigens in complex samples. Cysteine 54-57 immunglobulin heavy chain variable region Homo sapiens 74-78 15656582-5 2005 To evaluate the general applicability of this unpaired cysteine for PEGylation of scFv-c, conjugation efficiency was determined for four different scFvs and several PEG molecules having thiol reactive groups. Cysteine 55-63 immunglobulin heavy chain variable region Homo sapiens 82-86