PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 24647109-7 2014 Solubilized His-tagged scFv proteins were purified using Ni(2+)-Sepharose column chromatography in the presence of 3.5 M Gdn-HCl. Histidine 12-15 immunglobulin heavy chain variable region Homo sapiens 23-27 25613910-4 2015 A 6 x histidine tag was fused to the C-terminus of IC16-scFv allowing hybridization with a small organic beta-sheet binder via Ni-NTA complexation. Histidine 6-15 immunglobulin heavy chain variable region Homo sapiens 56-60 26693887-4 2016 The ScFv construct (Vkappa-Linker-VH) was expressed as a fusion protein with N-terminal His tag in Escherichia coli and purified using immobilized metal affinity chromatography (IMAC) without the addition of reducing agents. Histidine 88-91 immunglobulin heavy chain variable region Homo sapiens 4-8 26301925-3 2015 After sequence analysis, the scFv/1N8 gene was cloned into the prokaryotic expression vector PET32a with a His-tag. Histidine 107-110 immunglobulin heavy chain variable region Homo sapiens 29-33 26301925-5 2015 Moreover, the binding activity and specificity of the scFv were determined by indirect ELISA (His-tag) and competitive ELISA. Histidine 94-97 immunglobulin heavy chain variable region Homo sapiens 54-58 24884357-6 2015 The soluble scFv anti-p17 from crude HB2151 lysated was subsequently purified by immobilized metal ion affinity chromatography (IMAC) with His-tag. Histidine 139-142 immunglobulin heavy chain variable region Homo sapiens 12-16 16139234-6 2005 The increased coupling strength provided via the bivalent anchoring significantly reduced scFv displacement in complex solutions containing large amounts of histidine-containing proteins, verified via cholera toxin detection in serum. Histidine 157-166 immunglobulin heavy chain variable region Homo sapiens 90-94 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. Histidine 144-153 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. Histidine 16-19 immunglobulin heavy chain variable region Homo sapiens 93-97 22695166-5 2012 Indirect evidence for the noncovalent multimerization of scFv was the presence of a major peak of multimerized scFv without a His tag (due to differential cleavage) in the Q-TOF profile, unlike monomeric scFv, which copurified with normally His-tagged scFv and recognized the target antigen. Histidine 126-129 immunglobulin heavy chain variable region Homo sapiens 57-61 22695166-5 2012 Indirect evidence for the noncovalent multimerization of scFv was the presence of a major peak of multimerized scFv without a His tag (due to differential cleavage) in the Q-TOF profile, unlike monomeric scFv, which copurified with normally His-tagged scFv and recognized the target antigen. Histidine 241-244 immunglobulin heavy chain variable region Homo sapiens 57-61 22695166-5 2012 Indirect evidence for the noncovalent multimerization of scFv was the presence of a major peak of multimerized scFv without a His tag (due to differential cleavage) in the Q-TOF profile, unlike monomeric scFv, which copurified with normally His-tagged scFv and recognized the target antigen. Histidine 241-244 immunglobulin heavy chain variable region Homo sapiens 111-115 22695166-5 2012 Indirect evidence for the noncovalent multimerization of scFv was the presence of a major peak of multimerized scFv without a His tag (due to differential cleavage) in the Q-TOF profile, unlike monomeric scFv, which copurified with normally His-tagged scFv and recognized the target antigen. Histidine 241-244 immunglobulin heavy chain variable region Homo sapiens 111-115 22695166-5 2012 Indirect evidence for the noncovalent multimerization of scFv was the presence of a major peak of multimerized scFv without a His tag (due to differential cleavage) in the Q-TOF profile, unlike monomeric scFv, which copurified with normally His-tagged scFv and recognized the target antigen. Histidine 241-244 immunglobulin heavy chain variable region Homo sapiens 111-115 16255580-1 2005 A recombinant single-chain fragment variable (scFv) antibody (designated A10B) was engineered to contain two histidines within the linker peptide used to join the scFv heavy and light chains. Histidine 109-119 immunglobulin heavy chain variable region Homo sapiens 46-50 19285990-5 2009 Incorporation of a six-histidine (His(6)) peptide into the C-terminus of the 41s fiber protein resulted in markedly increased Ad5F41s6H infectivity in 293AR cells, which express a membrane-anchored scFv against the C-terminal oligohistidine tag, as compared to the Ad5F41s vector and the parental 293 cells. Histidine 23-32 immunglobulin heavy chain variable region Homo sapiens 198-202 19285990-5 2009 Incorporation of a six-histidine (His(6)) peptide into the C-terminus of the 41s fiber protein resulted in markedly increased Ad5F41s6H infectivity in 293AR cells, which express a membrane-anchored scFv against the C-terminal oligohistidine tag, as compared to the Ad5F41s vector and the parental 293 cells. Histidine 34-37 immunglobulin heavy chain variable region Homo sapiens 198-202 8621385-4 1996 Comparison of experimental results for scFv 9-40/212 with its mutant scFv 9-40/212Arg-34L indicated that the pH dependence of mAb 9-40 was due to the titration of His-34L in the active site. Histidine 163-166 immunglobulin heavy chain variable region Homo sapiens 39-43 11567181-2 2001 In this paper, we examine a novel one-step method for direct 99mTc labelling of a recombinant anti-CEA scFv fragment through a C-terminal peptide tag containing a six-histidine sequence. Histidine 167-176 immunglobulin heavy chain variable region Homo sapiens 103-107 16201198-8 2001 The 5 x his-tagged ScFv antibodies were purified on IDA-Ni2+ resin by immobilized metal chelate affinity chromatography (IMAC). Histidine 8-11 immunglobulin heavy chain variable region Homo sapiens 19-23 11099853-3 2000 For achieving efficient purification of scFvs by immobilized metal-ion affinity chromatography (IMAC), a His-tag was placed either at the C-terminal (scFv-His6) or N-terminal (His6-scFv) of the coding sequence. Histidine 105-108 immunglobulin heavy chain variable region Homo sapiens 40-44 11099853-3 2000 For achieving efficient purification of scFvs by immobilized metal-ion affinity chromatography (IMAC), a His-tag was placed either at the C-terminal (scFv-His6) or N-terminal (His6-scFv) of the coding sequence. Histidine 105-108 immunglobulin heavy chain variable region Homo sapiens 150-154 11099853-4 2000 Solid-phase radioimmunoassay for scFv-His6 showed only 20-25% binding whereas both His6-scFv and scFv (no His-tag) showed 60-65% binding. Histidine 38-41 immunglobulin heavy chain variable region Homo sapiens 33-37 11099853-7 2000 Comparative homology modeling for scFv and scFv-His6 showed that the C-terminal position of the His-tag partially covered the antigen-binding site of the protein. Histidine 48-51 immunglobulin heavy chain variable region Homo sapiens 43-47 11099853-8 2000 The study demonstrates that the C-terminal position of His-tag on the CC49 scFv adversely affects the binding properties of the construct. Histidine 55-58 immunglobulin heavy chain variable region Homo sapiens 75-79 10768836-3 2000 The scFv was fused to a human heavy chain IgG1 constant region (CH1-CH3) and contained an intact 6 His tag and enterokinase recognition site (RS10B5huFc). Histidine 99-102 immunglobulin heavy chain variable region Homo sapiens 4-8 10549857-2 1999 This single-chain Fv (scFv) with a histidine tag was expressed in Escherichia coli as an inclusion body. Histidine 35-44 immunglobulin heavy chain variable region Homo sapiens 22-26 10068041-4 1998 Inspection of the structure of the complex suggested that it might be possible to convert the scFv into a bond-specific protease by the introduction of three catalytic residues: a glutamate to increase the nucleophilicity of a nearby water molecule, a lysine to increase the polarizability of the carbonyl group and a histidine to provide a proton to convert the amine into a better leaving group. Histidine 318-327 immunglobulin heavy chain variable region Homo sapiens 94-98 8621385-4 1996 Comparison of experimental results for scFv 9-40/212 with its mutant scFv 9-40/212Arg-34L indicated that the pH dependence of mAb 9-40 was due to the titration of His-34L in the active site. Histidine 163-166 immunglobulin heavy chain variable region Homo sapiens 69-73