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1                                              Fab 5F10 fixes the B domain rigidly to the surface of th
2                                              Fab fragment of TRC105, a mAb that specifically binds to
3                                              Fab fragments of PG102, while retaining CD40 binding, di
4                                              Fab-7 boundary activity is known to depend on factors th
5                  Recombinant antibody HT2-10 Fab recognizing both HT-2 and T-2 toxins was developed f
6 MET crystal structure shows that the 107_A07 Fab comes into close proximity with the HGF/SF-binding S
7            The structure shows that ZIKV-117 Fabs cross-link the monomers within the surface E glycop
8 ted more from PEGylation than the anti-IL-13 Fab' did.
9 dence time of the anti-IL-17A and anti-IL-13 Fab' fragments in the lungs but PEGylation was able to p
10 f delivery of the anti-IL-17A and anti-IL-13 Fab' fragments within the lungs had a major impact on th
11 s residence time as well and the anti-IL-17A Fab' benefited more from PEGylation than the anti-IL-13
12 fect on the residence time of an anti-IL-17A Fab' fragment in the lungs of mice.
13    Finally, using I(125)-labeled anti-IL-17A Fab', we showed that the protein fragment hardly penetra
14  we determined the crystal structure of 2424 Fab in complex with a JRFL V3 peptide and showed that th
15       The antigenic regions targeted by 24E9 Fab were identified by hydrogen/deuterium exchange mass
16 esolution structure of the DBLbeta3_D4::24E9 Fab complex derived from small-angle x-ray scattering.
17 n X-ray crystal structure of an FcRn-DX-2507 Fab complex, revealing a nearly complete overlap of the
18                      However, monovalent 2D6 Fab fragments also inhibited V. cholerae motility, demon
19 led similar binding modes for MW1 and 3B5H10 Fab-huntingtin exon 1 complexes.
20 , we determined the crystal structure of 5G6 Fab fragment in complex with its epitope peptide KL10 (G
21        The similar binding properties of 5G6 Fab fragment to GPIbalpha on human platelets as those to
22                                      The 5G6 Fab-KL10 peptide complex structure confirmed the direct
23 inding to BMS-986010 (which contains the 7B7 Fab, where Fab is fragment antigen-binding region of an
24 al structure of the complex between C5 and a Fab fragment with the same sequence as eculizumab at a r
25 ostatin, proteins, and antibodies, such as a Fab arm of the antibody Herceptin and a designed antibod
26  E proteins within each spike are bound by a Fab molecule at domain III.
27                          Here, we describe a Fab identified from a minimalist synthetic library durin
28 ave solved the 4 A resolution structure of a Fab molecule bound to a picornavirus capsid.
29 cosahedral 3-fold axes prevents binding of a Fab to the third domain III of each E protein spike.
30 rowth factor) and two monovalent proteins (a Fab fragment and the transcription factor TBP) with low
31 EGF/angiopoietin 2 antibody with dual action Fab (DAF) as a potential therapeutic for neovascular age
32 Zr- and (124)I-labeled versions of alphaHER2 Fab-PAS200 allowed PET tumor imaging with high contrast.
33 nospecificity are compared among three GL-AM Fab pairs.
34 nd the antigen binding fragments F(ab')2 and Fab) targeting epidermal growth factor receptor were lab
35 d domain interactions for IgG antibodies and Fab fragments in the structural database.
36 o immobilize whole anti-PTHrP antibodies and Fab' fragments to surfaces as biorecognition elements.
37 ation fork with streptavidin (dsDNA end) and Fab (5' ssDNA) we located the positions of these labels
38 t bound to the CD4 peptide mimetic M48U1 and Fab of anti-cluster A antibody N60-i3 revealed no pertur
39 ighly dependent on local tumor perfusion and Fab permeation in the SUDHL-4 and Granta-519 tumors.
40               Atomic structures of virus and Fab were fitted into the corresponding cryo-EM densities
41                                     Antibody Fab fragments have been exploited with significant succe
42 holo-PDE6 in complex with the ROS-1 antibody Fab fragment was determined by cryo-electron microscopy.
43 ptamine 2B (5-HT2B) receptor and an antibody Fab fragment bound to the extracellular side of the rece
44 interested in the codon usage of an antibody Fab fragment gene exhibiting extreme toxicity in the E.
45  CyRPA alone and in complex with an antibody Fab fragment.
46 e heavy chain and light chain of an antibody Fab.
47 as to use (64)Cu-labeled anti-CD105 antibody Fab fragment for noninvasive assessment of angiogenesis
48  are functionalized with anti MC-LR antibody Fab' fragments for the selective capture of MC-LR from a
49 e-specific labeling of Env-specific antibody Fab with a fluorophore at high efficiency, and 3) optica
50 G2 and the crystal structure of the antibody Fab fragment, which was solved at 2.4 A resolution.
51 f two Fab' fragments, one from 1F5 antibody (Fab'1F5), the other from Rituximab (Fab'RTX).
52  and as complexes with fragment of antibody (Fab) from the neutralizing antibody H16.V5.
53 to a stabilized dimer of different antitumor Fabs.
54 nning antibody 8ANC195, that can be added as Fabs to a soluble native-like Env trimer to stabilize it
55 xtent of the antibody fragment (64)Cu-DOTA-B-Fab binding specificity.
56                                (64)Cu-DOTA-B-Fab is a stable and effective immuno-PET tracer for CA6
57          The antibody fragment (64)Cu-DOTA-B-Fab was more than 95% stable after 24 hours in human ser
58 cking experiments with an excess of either B-Fab or huDS6 were used to determine the extent of the an
59 pe controls with antilysozyme and anti-DM4 B-Fabs and blocking experiments with an excess of either B
60 x, incorporation of a miniPEG spacer between Fab' and MORF1 and between polymer backbone and pendant
61             This was accomplished by binding Fab fragments of the neutralizing antibody DV2-E104 to t
62 s (scFv), antibody fragment-antigen binding (Fab') units, and aptamers.
63 f the PG9_N100(F)Y fragment antigen binding (Fab) confirmed that the mutated residue retains the para
64 n complex with fragments of antigen binding (Fabs) from two human monoclonal antibodies, IgG-94 and I
65 iple epitopes for fragments antigen-binding (Fabs) of both antibodies, demonstrating that 3B5H10 does
66 n issue in the development of the biosensor, Fab' fragments should be chosen as they are relatively c
67 it/human monoclonal antibody fragments (both Fab and scFv) against rHBeAg.
68 ls by antibodies traditionally requires both Fab and Fc domains of IgG.
69                                        Bound Fab' fragments display higher surface densities, yieldin
70 d domain and is partly occluded by the bound Fab in the crystal structure.
71 functioning of the Bithorax complex boundary Fab-7, interacts specifically with a special class of CE
72 e binding could specifically be inhibited by Fab anti-C1q and C1q-derived peptides.
73 rived autoantibodies against complement C1q (Fab anti-C1q) and von Willebrand factor (VWF) led us to
74                             These so-called "Fab glycans" are primarily highly processed complex-type
75                           The altered-capsid-Fab complex map showed that binding of the Fab induced s
76 onucleotide (MORF1) attached to an anti-CD20 Fab' fragment (Fab'-MORF1); (2) multiple copies of compl
77 Fab site-specifically conjugated to anti-CD3 Fab using the genetically encoded noncanonical amino aci
78 in variable fragment (ScFv) into an anti-CD3 Fab.
79  crystal structure of NA in complex with CD6 Fab reveals a unique epitope, where the heavy-chain comp
80               The crystal structure of ch8H9 Fab fragment was solved to 2.5-A resolution and used as
81 ically significant difference when comparing Fab'1F5-MORF1 with Fab'RTX-MORF1.
82                                 In contrast, Fab fragments of antibody 5F10 bind the tip of the E2 B
83 any platforms for creating bsAbs, controlled Fab-arm exchange (cFAE) has proven useful based on minim
84  distinct bispecific molecules by controlled Fab-arm exchange (DuoBody technology).
85  whole panel of bsAbs produced by controlled Fab-arm exchange.
86             We recently described controlled Fab-arm exchange (cFAE) as an easy-to-use method for the
87                          By using controlled Fab-arm exchange, a set of BsAbs targeting EGFR and c-ME
88      Crystal structures of the corresponding Fab fragments were determined in complex with hypusine-
89 ar measurements in the presence of anti-CS20 Fab fragments did not show any effect, indicating that b
90 light-sheet fluorescence microscopy with Cy5-Fab-PAS200 confirmed better tracer extravasation in the
91 of the complex between an omalizumab-derived Fab and IgE-Fc, with one Fab bound to each C3 domain.
92 tope-labeled, protease-cleaved, mAb domains (Fab and Fc) has been demonstrated from both E. coli and
93                                 (177)Lu-DOTA-Fab-PEG24-EGF bound specifically to HER2 and EGFR on tum
94                                 (177)Lu-DOTA-Fab-PEG24-EGF inhibited tumor growth more effectively th
95 t TrR1 tumors were treated with (177)Lu-DOTA-Fab-PEG24-EGF or (111)In-DTPA-Fab-PEG24-EGF at the NOAEL
96  was measured after exposure to (177)Lu-DOTA-Fab-PEG24-EGF or (111)In-DTPA-Fab-PEG24-EGF or to monosp
97 tumors were growth-inhibited by (177)Lu-DOTA-Fab-PEG24-EGF or (111)In-DTPA-Fab-PEG24-EGF.
98  The maximum injected amount of (177)Lu-DOTA-Fab-PEG24-EGF that caused no observable adverse effects
99                  The binding of (177)Lu-DOTA-Fab-PEG24-EGF to tumor cells (MDA-MB-231, SK-OV-3, MDA-M
100                   The NOAEL for (177)Lu-DOTA-Fab-PEG24-EGF was 11.1 MBq (10 mug).
101             The tumor uptake of (177)Lu-DOTA-Fab-PEG24-EGF was 2-fold greater than (177)Lu-DOTA-trast
102                                 (177)Lu-DOTA-Fab-PEG24-EGF was more cytotoxic than (111)In-DTPA-Fab-P
103 ormal tissue biodistribution of (177)Lu-DOTA-Fab-PEG24-EGF was studied at 48 h after injection in ath
104 h (177)Lu-DOTA-Fab-PEG24-EGF or (111)In-DTPA-Fab-PEG24-EGF at the NOAEL, or with unlabeled immunoconj
105 or growth more effectively than (111)In-DTPA-Fab-PEG24-EGF because of a 9.3-fold-higher radiation-abs
106 o (177)Lu-DOTA-Fab-PEG24-EGF or (111)In-DTPA-Fab-PEG24-EGF or to monospecific (177)Lu- or (111)In-lab
107 y (177)Lu-DOTA-Fab-PEG24-EGF or (111)In-DTPA-Fab-PEG24-EGF.
108 G24-EGF was more cytotoxic than (111)In-DTPA-Fab-PEG24-EGF.
109 bodies requires the engineering of effective Fab libraries guided by the knowledge of the principles
110     We show in a crystal structure that ESK1 Fab binds to RMF/HLA-A*02:01 in a mode different from th
111  function appropriately when substituted for Fab-7: it blocks crosstalk but does not support bypass.
112 uences that are necessary and sufficient for Fab-7 boundary function in the BX-C.
113                        An antibody fragment (Fab) of MAb E was found to neutralize the virus at low m
114 te residing in the antigen-binding fragment (Fab or Fv) is an autonomous and complete unit for antige
115 SOSIP.664 with the antigen-binding fragment (Fab) of PGT145, a broadly neutralizing quaternary-struct
116 e influence of the antigen-binding fragment (Fab) on FcRn interactions has been reported, the underly
117 gth antibody or an antigen-binding fragment (Fab).
118 RF1) attached to an anti-CD20 Fab' fragment (Fab'-MORF1); (2) multiple copies of complementary oligon
119 dopt a methodology using antibody fragments (Fab) conjugated to gold nanoparticles (immunogold) to ma
120 odified alphaCD20 antigen-binding fragments (Fab), prepared by PASylation with a 200-residue polypept
121 ombinant antibody antigen-binding fragments (Fab), that is specific for HT-2 toxin and has a positive
122 matted as soluble antigen-binding fragments (Fab), these clones expressed well, were predominantly mo
123    Crystal structures of antibody fragments (Fabs) 311 and 317 with an (NPNA)3 peptide illustrate the
124 ed a series of synthetic antibody fragments (Fabs) against different conformations of betaarrs from p
125 ody derivatives, such as antibody fragments (Fabs) and single-chain variable fragments (scFvs), are n
126 re we describe synthetic antibody fragments (Fabs) as structural and biochemical probes to investigat
127 play library to engineer antibody fragments (Fabs) that can modulate the activity of the enzyme isoci
128 bes have been largely thought to result from Fab-antigen interactions, recent studies suggest that re
129                    With respect to function, Fab glycosylation can significantly affect stability, ha
130                               Thus, the gHgL/Fab structures delineate a site of herpesvirus vulnerabi
131 icient patients and reduced by the anti-GPVI Fab 9O12.
132 by comparing images with and without anti-HA Fab bound.
133                                     However, Fab-mediated effector functions contributed to the in vi
134 ependent antibodies in chimeric rabbit/human Fab format and validated it by next-generation sequencin
135                    The toxic synthetic human Fab gene contained domains optimized by the "one amino a
136                     We synthesized the human Fab antibody library (over 1.25 x 10(9) individual varia
137 ral potential applications for the humanized Fab/scFv.
138               (89)ZrDf-Fab-PAS200 and (124)I-Fab-PAS200 showed specific tumor uptake of 11 and 2.3 pe
139 d when the CD20-specific radiotracers (125)I-Fab-ABD and (125)I-Fab-PAS200 were applied (respective p
140 cific radiotracers (125)I-Fab-ABD and (125)I-Fab-PAS200 were applied (respective percentages injected
141  monovalent hapten and recombinant SPE-7 IgE Fab inhibit its cytokinergic activity as measured by mas
142                            Consequently, IgG Fab glycosylation appears to be an important, yet poorly
143 given to show the versatility of immobilized Fab' fragments in different applications and future dire
144  binds to several BX-C boundaries, including Fab-7 and Mcp To study Pita functions, we have used a bo
145 s and antibody-derived constructs (including Fab, Fc-fusions and bispecifics) in mammalian cells.
146  engineered hinge domain of IgG3 to increase Fab domain flexibility necessary for hetero-bivalent bin
147 ion considerably reduced toxicity, increased Fab expression from negligible levels to 10 mg/l, and re
148 e demonstrate that the antibody NT4X and its Fab fragment reacting with both the free N-terminus of A
149 ould inhibit the binding of both 2A5 and its Fab to Plg and its enhanced activation.
150 he capsid allowed us to determine the 50-kDa Fab structure by cryo-EM.
151   In the case of the AD-2S1 peptide, the KE5 Fab fragment complex identified nine germline-encoded co
152           A partially humanized chimeric LO1-Fab-Cys localized similarly to the parent antibody in mu
153 ation was found to be associated with its M1 Fab that activates the alternative pathway in an Fc-inde
154 IT consisting of a humanized anti-mesothelin Fab fused to domain III of Pseudomonas exotoxin A, in wh
155             We prepared the antibody mimetic Fab-PEG-Fab (FpFinfliximab) for direct intravitreal inje
156                                    Moreover, Fab glycans are associated with the anti-inflammatory ac
157 plexes display a compact rsCSP with multiple Fabs bound, with the rsCSP-Fab311 complex forming a high
158 ographic and competition binding analyses of Fab fragments and scFvs defined three spatially distinct
159                       Structural analyses of Fab fragments of mAbs 023.102 and pn132p2C05 in complex
160                 Crystallographic analysis of Fab alone or in complex with H5 or H7 HA proteins reveal
161                               In the case of Fab-7, we used a novel sensitized background to show tha
162 faces and hydrogen bonds of all complexes of Fab-protein or Fab-peptide was performed.
163 ron microscopy reveals marked flexibility of Fab arms of 7S and 5.7S IgY.
164 tremendous progress in the immobilization of Fab' fragments onto gold, Si-based, polysaccharide-based
165                         Specific patterns of Fab glycosylation are concurrent with physiological and
166 nd 3D electron microscopy reconstructions of Fab-trimer complexes revealed a horizontal binding angle
167   This review will show the current scope of Fab' immobilization techniques available and illustrate
168                             The structure of Fab m336 in complex with the MERS-CoV receptor-binding d
169                        Crystal structures of Fab-AbetapE3 complexes revealed two distinct binding mod
170 sal strategy to enhance the success rates of Fabs as structure determination chaperones.
171                        Studies of omalizumab Fab binding in solution demonstrate the allosteric basis
172 port the crystal structure of the omalizumab-Fab in complex with an IgE-Fc fragment.
173  an unusually extensive aromatic cage in one Fab and the histone N terminus to a pocket in the other,
174  omalizumab-derived Fab and IgE-Fc, with one Fab bound to each C3 domain.
175 e antibodies/ethanolamine) and one optimized Fab' fragment-based surface (TUBTS/Fab' fragments) were
176                 They are made up of an Fv or Fab that targets an antigen on a cancer cell fused to a
177 atic, exposure of V. cholerae to 2D6 IgA (or Fab fragments) resulted in a 5-fold increase in surface-
178 e generated that consist of anti-Her2 IgG or Fab site-specifically conjugated to anti-CD3 Fab using t
179 e was directly blocked by either PA50 mAb or Fab and suggested that receptor blockade is the mechanis
180 gen bonds of all complexes of Fab-protein or Fab-peptide was performed.
181 less to folded state stability than in other Fab domains.
182              A crystal structure of two PA50 Fabs bound to a segment of the TcdA CROPs helped define
183 riginal scFab format and 3-fold above parent Fab levels.
184         Here, we combined different anti-PEG Fab expressing 293T cells as capture cells (293T/3.3, 29
185     We prepared the antibody mimetic Fab-PEG-Fab (FpFinfliximab) for direct intravitreal injection to
186              FR104 is a monovalent pegylated Fab' Ab, antagonist of CD28, under development for treat
187 olved in the prolonged presence of PEGylated Fab' in the airway lumen might include binding to the mu
188 ssment of FR104 (n=5), a selective pegylated Fab' antibody fragment antagonist of CD28 that does not
189 mpared to the ligand-free trimer, the PGT145 Fab-BG505 SOSIP.664 complex displayed increased melting
190 result of the binding of multiple polyclonal Fabs to the C region of primary IgH.
191                              The most potent Fab fragment (2A4(GTP)) showed over 100-fold GTP-specifi
192  was validated using previously recalcitrant Fab-antigen complexes where introduction of an engineere
193                                  Recombinant Fab fragments recognizing different conformations of thi
194 ent on the heavy chain (HC) variable region (Fab) and the other present on the conserved HC constant
195        Inhibition of BAX by a representative Fab, 3G11, prevented mitochondrial translocation of BAX
196 ntibody (Fab'1F5), the other from Rituximab (Fab'RTX).
197 lly, we engineer mouse hybridomas to secrete Fab' fragments instead of the whole Ig.
198                                  We selected Fab fragments using the phage display technology.
199 fied by PG9, bind asymmetrically as a single Fab to the apex of the symmetric Env trimer using a prot
200                                          Six Fab fragments were found against 2'/3'-GTP-biotin and 8-
201 hes that consist of a tumor antigen-specific Fab molecule engrafted with a peptide neo-epitope, which
202         We show that a conformation-specific Fab can reactivate an IDH1 mutant associated with brain
203        In this study, the first GTP-specific Fab fragment and its application are described.
204  conformation-, epitope- and domain-specific Fabs, we feel that the CBP tag embodies all the attribut
205                                Specifically, Fab 3A2 bound to MMP-14 in the vicinity of the active po
206 y engineering strategy to generate synthetic Fab variants that significantly reduces elbow flexibilit
207                                The synthetic Fabs reported here reveal, as probes, novel mechanistic
208                              These synthetic Fabs bind with high affinity to BAX and inhibit its acti
209 The near-atomic structure also revealed that Fab binding had caused capsid destabilization in regions
210 the cryo-electron density maps, we show that Fab fragments of antibody 8B10 extend radially from the
211                    Prior studies showed that Fabs from these MAbs bind a soluble EBOV GP ectodomain a
212                                          The Fab (BRG) binds with 20nM dissociation constant to a sin
213                                          The Fab bound and ordered the apical loops of HPV16.
214                                          The Fab conformations in both structures were suitably posit
215                                          The Fab fragments stabilized the position of the B domain re
216                                          The Fab has a 20 pM affinity for ticagrelor, which is 100 ti
217                                          The Fab induced conformational changes in regions of the vir
218                                          The Fab traps the RNA in a hairpin conformation that contain
219 ing an oriented immobilization approach, the Fab' fragments are covalently attached to gold surface t
220 resolution of 2.5 A of a complex between the Fab fragments of E1 and HM14c10 and provide the first de
221 resolution of 2.5 A of a complex between the Fab fragments of E1 and HM14c10 provides the first detai
222 ll molecules is demonstrated, as binding the Fab to the capsid allowed us to determine the 50-kDa Fab
223 n of individual glycan species from both the Fab and Fc N-Linked glycosylation sites is consistent wi
224 ure of the nAChR alpha1 subunit bound by the Fab fragment of mAb35, a reference monoclonal antibody t
225  s(-1) over preformed fibrin-rich clots, the Fab 9O12 decreased the recruitment of platelets by up to
226 rategy by substituting modified DNAs for the Fab-7 boundary, which is located between the iab-6 and i
227                                 However, the Fab' fragment-based biosensor displayed better regenerab
228 dy with single residue pair mutations in the Fab region to promote efficient and stable cognate light
229 ific ADCs with linker-drug conjugated in the Fab region.
230 rugs are site-specifically conjugated in the Fab region.
231 mplex), to recognize a CCAATAAG motif in the Fab-7 insulator.
232        Here, we present the structure of the Fab fragment of such an antibody.
233 cket formed between VH and VL domains of the Fab fragments.
234                              For some of the Fab gene variants, we also observed striking differences
235           We redesigned five segments of the Fab gene with a "codon harmonization" method described b
236 " by E1 by increasing its recognition of the Fab HM14c10 light chain CDRs.IMPORTANCE A chimeric yello
237  and determined the crystal structure of the Fab in complex with its target, which identifies the bin
238 d-Fab complex map showed that binding of the Fab induced significant conformational changes that were
239 urine IgE, we reveal that interaction of the Fab region of 'free' SPE-7 IgE with the Fab of Fcepsilon
240 onal antibodies to be the CDR H3 loop of the Fab region, and show that they all have nano to micromol
241 ution, which allowed de novo building of the Fab structure.
242                            The nature of the Fab' fragment had an influence on its residence time as
243 t increase in thermodynamic stability of the Fab, a feature predicted by the computational model.
244 ink the constant and variable domains of the Fab, can introduce disorder and thus diminish their effe
245                               Overlay of the Fab-MET crystal structure with the InternalinB-MET cryst
246                               Several of the Fab/scFv, expressed in Escherichia coli, had unprecedent
247 alactose-alpha-1,3-galactose, located on the Fab region of cetuximab, was identified as the target re
248 Fc) constructed by using CocH to replace the Fab region of human IgG1.
249                       We identified that the Fab-binding site on BAX involves residues of helices alp
250                     We hypothesized that the Fab-bound complex would stabilize BG505 SOSIP.664 in its
251  coupling of antigen specificity through the Fab domain to signal transduction via Fc-Fc receptor int
252 ity capture of human IgGs via binding to the Fab region, followed by on-bead IdeS digestion to remove
253 l means of antigen recognition, in which the Fab fragment of an antibody acts as an adaptor, linking
254                                    While the Fab domains mediate highly specific antigenic recognitio
255 /2013, French Polynesia) in complex with the Fab fragment of a highly therapeutic and neutralizing hu
256 ies of the GI.1 P domain in complex with the Fab fragment of a human IgA monoclonal antibody (IgA 5I2
257 al structures of Der p 1 in complex with the Fab fragments of mAbs 5H8 or 10B9.
258  the Fab region of 'free' SPE-7 IgE with the Fab of FcepsilonRI-bound SPE-7 IgE is the basis of its c
259                             KD values of the Fabs were in subnanomolar to low nanomolar (nM) ranges a
260 Yersinia pestis were characterised for their Fab affinity against the purified protein and their Fc a
261 lographically determined structures of these Fab fragments into the cryo-electron density maps, we sh
262 form sampling techniques, we show that these Fab and Fc fingerprint spectra can be rapidly acquired i
263  models suggest two mechanisms for how these Fabs may prevent the conversion of PrP(C) into PrP(Sc).
264                             Several of these Fabs allosterically and selectively modulated the intera
265                  Interestingly, one of these Fabs selectively disrupted betaarr-clathrin interaction,
266 nces between rHBeAg and HBeAg, we used these Fabs in microscale immunoaffinity chromatography to puri
267                                         This Fab also reduced platelet adhesion to fibrin at low (300
268  been shown to be antigenic when attached to Fab oligosaccharides of monoclonal antibodies (mAbs) , w
269 e late boundary complex (LBC), that binds to Fab-7 sequences that have insulator functions in late em
270 across a series of antibody fragments (VL to Fab), and subsequently, the DCM was combined with molecu
271  we determined the structure of tralokinumab Fab in complex with human IL-13 to 2 A resolution.
272 2-fold greater than (177)Lu-DOTA-trastuzumab Fab or (177)Lu-DOTA-EGF.
273 fic (177)Lu- and (111)In-labeled trastuzumab Fab or EGF killed tumor cells that predominantly express
274 ific (177)Lu- or (111)In-labeled trastuzumab Fab or EGF.
275  and EGFR on BC cells by linking trastuzumab Fab fragments through a polyethylene glycol (PEG24) spac
276                                  NOTA-TRC105-Fab exhibited high purity and specifically bound to CD10
277                 Uptake of (64)Cu-NOTA-TRC105-Fab increased from a control level of 3.4 +/- 0.1 to 9.5
278                           (64)Cu-NOTA-TRC105-Fab PET may potentially be used for future diagnosis and
279 nt weekly PET scans using (64)Cu-NOTA-TRC105-Fab.
280 optimized Fab' fragment-based surface (TUBTS/Fab' fragments) were tested as biosensors.
281  as well as their complexes with each of two Fab fragments (HuM-P and HuM-R1), which recognize N- and
282 one and pendant MORF2, and comparison of two Fab' fragments, one from 1F5 antibody (Fab'1F5), the oth
283 recognition by the new bNAb BG1 in which two Fabs bind asymmetrically per Env trimer using a compact
284 structures of the complexes of IL-6 with two Fabs derived from conventional camelid antibodies that a
285 l properties, such as the ability to undergo Fab-arm exchange and limit immune complex formation.
286                                      We used Fab/scFv in the context of an enzyme-linked immunosorben
287 ), followed by dual enzymatic labeling using Fab fragments of anti-Dig and anti-FITC conjugated to pe
288  effects of these changes on cell viability, Fab yield and display on filamentous phage using differe
289                                    In vitro, Fab- and Fc-mediated effector functions, such as inhibit
290 whereas the IgG4 isotype can undergo in vivo Fab arm exchange leading to bispecific antibody and off-
291 ZM197M SOSIP.664 trimer complexed with VRC01 Fab against the CD4 binding site at subnanometer resolut
292 MS-986010 (which contains the 7B7 Fab, where Fab is fragment antigen-binding region of an antibody),
293 ermined the structure of CPV in complex with Fab E to 4.1 A resolution, which allowed de novo buildin
294  structures of the allergens in complex with Fab fragments of three murine mAbs that interfere with I
295       However, treatment of Y7A KI mice with Fab' fragments of the function-blocking anti-CLEC-2 anti
296 difference when comparing Fab'1F5-MORF1 with Fab'RTX-MORF1.
297 ortened CSP (rsCSP) construct saturated with Fabs.
298 asymmetric Protein A binding, and the scFv x Fab format.
299                                       ZKA190 Fab binds all 180 E protein copies, altering the virus q
300                                     (89)ZrDf-Fab-PAS200 and (124)I-Fab-PAS200 showed specific tumor u

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