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Fab fragment glycosylated IgG may play a central role in placental immune evasion.

How does the placenta protect the fetus from immune rejection by the mother?

1736 related Products with: Fab fragment glycosylated IgG may play a central role in placental immune evasion.

Anti beta3 AR Human, Poly Anti VGLUT 1 Rat, polyclo Anti Rat VGLUT 2, Rabbit Rabbit Anti-intestinal FA Rabbit Anti-intestinal FA Rabbit Anti-intestinal FA Rabbit Anti-intestinal FA Rabbit Anti-intestinal FA Rabbit Anti-intestinal FA Interleukin-34 IL34 (N-t Interleukin-34 IL34 anti anti HSV (II) gB IgG1 (mo

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Conversion of TBAb response to TSAb response by anti-human IgG antibody.

Previously, we reported the conversion phenomenon (CP) of thyroid blocking antibody (TBAb) to thyroid stimulating antibody (TSAb) by induced cAMP production during incubation of TBAb-bound porcine thyroid cells (PTC) with rabbit anti-IgG Ab. In the present experiment we examined the CP by TBAb-positive sera with high TSH binding inhibitor immunoglobulin (TBII) activity in primary hypothyroidism. Two patients with extremely high TBII patients; patient No.1 (35 yo male) with TSH 26.5μU/ml, TSAb negative, TBII 4,600 U/L, TBAb100% and patient No.2 (40 yo female) with TSH 4.5μU/ml, TSAb negative, TBII 1,620 U/L, TBAb 99.8% were examined. Cyclic AMP production was examined by 2nd incubation (3h) of anti-IgG Ab with TBAb-bound PTC that was made by 1st incubation (0.5h) of TBAbpositive serum and PTC. When sera (0.001-0.05 ml) of patient No.1 and No.2 were tested, cAMP production showed 980- 3,700% and 570-3,000% in a dose-dependent manner, respectively. Cyclic AMP production was also observed by anti- IgG fragments Ab [(Fab')2, Fab and light chain]. Cyclic AMP production by anti-F(ab')2 was higher than anti-Fab Ab, and cAMP by anti-κ Ab was significantly higher (>3 fold) than anti-λ Ab. Cyclic AMP production by TBAb-positive sera with high TBII activity (35-270 U/L) showed a correlation with serum TBII activity (R=0.76). The fact that all high TBAb-positive sera show the CP of TBAb to TSAb suggests that TSAb activity may be present in TBAb molecule and TBAb may be the precursor of TSAb.

1862 related Products with: Conversion of TBAb response to TSAb response by anti-human IgG antibody.

Anti beta3 AR Human, Poly anti CD54 IgG2b k monoclo anti CD66e IgG1 monoclona Mouse anti Human IgA anti Mouse anti Human IgE anti Mouse anti Human IgE anti Mouse anti Human IgE anti Mouse anti Human IgE anti Mouse anti Human IgG anti Mouse anti Human IgG anti Mouse anti Human IgG anti Mouse anti Human IgM anti

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Characterization of murine anti-human Fab antibodies for use in an immunoassay for generic quantification of human Fab fragments in non-human serum samples including cynomolgus monkey samples.

Generic immunoassay formats in animal serum have been described for pharmacokinetic (PK) analysis of human full-length antibodies, but not of human antigen binding fragment (Fab) proteins. Here we characterize two murine monoclonal antibodies (mAb) raised against human immunoglobulin G (IgG) which bind to unique epitopes in the Fab region of human IgG. mAb M-1.7.10 is directed against the constant domain of the kappa light chain and mAb M-1.19.31 binds to the constant domain 1 (CH1) of the heavy chain. Surface plasmon resonance analysis showed that mAb M-1.7.10 does not cross-react with sera from mouse, rat, rabbit, dog, marmoset, rhesus macaque, baboon and cynomolgus monkey, but binds to human and chimpanzee serum (dissociation constant K(D) of 6.8 × 10(-12) and 3.1 × 10(-11)M, respectively). mAb M-1.19.31 shows a higher K(D) for human and chimpanzee IgG (2.0 × 10(-9)M and 5.8 × 10(-10)M, respectively), but also does not bind to serum of the other species. Therefore, mAb M-1.7.10 was used as capture and mAb M-1.19.31 as detection reagent in a generic enzyme linked immunosorbent assay (ELISA) to quantify the human anti-IGF-1R Fab in mouse serum. The generic human Fab assay showed a limit of detection of 31.5 ng/mL anti-IGF-1R Fab. Intra- and inter-assay precision was less than 12% and the accuracy range for all controls was within ±20% of the target concentration. The generic human Fab ELISA was applied to determine serum levels of human anti-IGF-1R Fab after intravenous (iv) administration of 10mg/kg to mice. The resulting concentration-time profile was nearly identical to that obtained by analysis with a validated specific ELISA for anti-IGF-1R Fab. The mean relative concentration of anti-IGF-1R Fab analyzed by the generic assay was 82-118% of that of the specific assay. This equivalence was confirmed in a cynomolgus monkey study with the full length human mAb anti-TROP-2 IgG. Both specific ELISAs used mAb M-1.7.10 as detection reagent and their targets for capturing. In conclusion, the two murine anti-human Fabs are versatile tools as capture and detection reagents for human antibodies in generic and specific PK ELISA formats for animal studies. Their use in specific ELISAs as detection reagents allows the usage of Fc-fusion proteins as capture reagents.

1275 related Products with: Characterization of murine anti-human Fab antibodies for use in an immunoassay for generic quantification of human Fab fragments in non-human serum samples including cynomolgus monkey samples.

Rabbit Anti-intestinal FA Goat Anti-Human Synaptota Goat Anti-Human STK39 SPA Goat Anti-Human SPHK1, (i Goat Anti-Human SODD, (in Goat Anti-Human SIGLEC8, Goat Anti-Human SH2D4A, ( Goat Anti-Human SEPT7, (i Goat Anti-Human SEPT6, (i Goat Anti-Human S100A9, ( Goat Anti-Human RABIF, (i Goat Anti-Human PXR NR1I2

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Generic anti-drug antibody assay with drug tolerance in serum samples from mice exposed to human antibodies.

Knowledge of the anti-drug antibody (ADA) status is necessary in early research studies. Because specific assay materials are sparse and time is pressing, a generic assay format with drug tolerance for detection of ADAs in serum samples from mice exposed to immunoglobulin G (IgG) or antigen-binding fragments (Fabs) is highly desirable. This article describes a generic immune complex assay in the sandwich enzyme-linked immunosorbent assay (ELISA) format based on (i) transformation of free ADAs to immune complexes by preincubation with excess drug, (ii) the use of a murine anti-human Fab constant domain Fab as capture reagent, (iii) detection of the immune complexes by a peroxidase-labeled rabbit anti-murine Fc antibody, and (iv) ADA-positive control conjugates consisting of human Fab and murine IgG. Results of the experiments suggest that the generic immune complex assay for mouse serum samples was at least equivalent to specific ADA immune assays and even superior regarding drug tolerance. The generic immune complex assay confers versatility as it detects ADAs in complex with full-length IgG as well as with Fabs independent of the target specificity in mouse serum samples. These features help to save the sparse amounts of specific antibodies available in early research and development and speed up drug candidate selection.

2732 related Products with: Generic anti-drug antibody assay with drug tolerance in serum samples from mice exposed to human antibodies.

Goat Anti-Human TOM1L1 SR Rabbit Anti-Human Toll In Anti C Reactive Protein A Anti AGO2 Human, Monoclon Anti AGO2 Human, Monoclon Anti AGO2 Human, Monoclon Anti AGO2 Human, Monoclon Anti Human AGO3, Monoclon Human Serum Albumin antib Human Serum Albumin antib Mouse anti Human IgA anti Mouse anti Human IgE anti

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Immunological similarity of thyroid stimulating antibody (TSAb) and thyroid blocking antibody (TBAb) with animal IgG.

Previously we reported neutralization and partial purification of TSAb and TBAb activity using heterophilic antibody (Ab) to animal IgG from Graves' disease. Thus, we examined immunological similarity of TSAb and TBAb with animal IgG using experimentally generated anti-animal IgG [dog (d), bovine (b), porcine (p) and rabbit (rb)] Abs. TBII activity of TSAb- and TBAb-positive serum was neutralized by these anti-animal IgG Abs. Applied TSAb- or TBAb-IgG protein (purified by Protein A) on these anti-animal IgG Abs-bound column was found mainly in the unbound fraction (UF) (>65%) and partially in the bound fraction(BF) (<35%). The TBII and TSAb activity of TSAb-IgG in the BF showed significantly higher than the UF. Thus, the ratio of TBII activity (U/L)/mg protein in the BF/UF was high. TBII activity of TBAb-IgG was similarly purified by this column. We examined immunological characteristics of TSAb-and TBAb-Fab or F(ab')₂ using rabbit anti-bF(ab')₂ Ab. TBII and TSAb activity of TSAb-Fab or- F(ab')₂ and TBII activity of TBAb-Fab or -F(ab')₂ were neutralized by anti-bF(ab')₂ Ab. Partial purification of TSAb- or TBAb-Fab and -F(ab')₂ by anti-bF(ab')₂ Ab-bound column was also possible. Immunological similarity of TSAb- and TBAb-IgG with animal IgG such as d, b, p, rb by anti-animal IgG Ab, and TSAb- or TBAb-Fab and -F(ab')₂ with bFab by anti-bF(ab')₂ Ab were demonstrated. These fact suggest that both Fab and Fc portion of TSAb- and TBAb-IgG molecule have immunological similarity with animal IgG.

2442 related Products with: Immunological similarity of thyroid stimulating antibody (TSAb) and thyroid blocking antibody (TBAb) with animal IgG.

B-Phycoerythrin antibody 2-Amino Benzimidazole Su 2-Amino Benzimidazole Su Interleukin-34 IL34 (N-t Interleukin-34 IL34 anti 2,3 dinor 6 keto Prostag Blocking Buffer Antibody Measles Virus Nucleoprote HIV1 tat antibody, Monocl Adenovirus antibody, Mono Adenovirus antibody, Mono Human IgG antibody, Monoc

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Measurement of serum levels of natalizumab, an immunoglobulin G4 therapeutic monoclonal antibody.

Human immunoglobulin G4 (IgG4) is a poor trigger of effector functions and, therefore, is the preferred subclass for therapeutic monoclonal antibodies that merely aim to block their in vivo targets. An example is natalizumab, a recombinant IgG4 antibody directed against α4-integrin and used for treatment of multiple sclerosis. Efficient treatment requires that the pharmacokinetics of therapeutic monoclonal antibodies can be accurately monitored. For natalizumab, this requires special precautions due to recently reported structural peculiarities of human IgG4. Here we describe the development of an assay to determine serum levels of natalizumab. Compared with other IgG subclasses, human IgG4 possesses unique structural properties that influence its interactions in both in vivo and in vitro settings. Thus, IgG4 undergoes Fab arm exchange in vivo, resulting in effectively monovalent antibodies. Furthermore, IgG4 is able to bind to other human and nonhuman IgG via Fc interactions. We demonstrate how these features can interfere with measurement of specific IgG4 and describe how we addressed these issues, resulting in an assay that is not sensitive to Fab arm exchange by natalizumab or to IgG4 Fc interactions.

2207 related Products with: Measurement of serum levels of natalizumab, an immunoglobulin G4 therapeutic monoclonal antibody.

Human Serum Albumin antib Human Serum Albumin antib FDA Standard Frozen Tissu FDA Standard Frozen Tissu Monoclonal Anti-Bovine Se Anti C Reactive Protein A MOUSE ANTI BOVINE ROTAVIR Anti AGO2 Human, Monoclon Anti AGO2 Human, Monoclon Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon Anti AGO2 Mouse, Monoclon

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Development of a novel homogenous electrochemiluminescence assay for quantitation of ranibizumab in human serum.

A solution-phase electrochemiluminescence assay (ECLA) was developed to quantify ranibizumab in serum from patients treated with this biotherapeutic for neovascular age-related macular degeneration. Ranibizumab, a recombinant humanized Fab ("fragment, antigen binding"), binds with high affinity and specificity to vascular endothelial growth factor A (VEGF-A), inhibiting its activity. Fab molecules contain the amino acid sequence that binds antigen and are composed of one constant and one variable domain from each heavy and light chain of the antibody. High assay sensitivity was required to enable pharmacokinetic (PK) evaluation of ranibizumab-dosed patients in clinical trials. Our assay's lower limit of quantitation is 300 pg/mL ranibizumab in neat serum, achieving a 67-fold improvement in sensitivity relative to a conventional ELISA-based PK method. In this assay, ruthenium-labeled affinity-purified rabbit anti-ranibizumab antibodies and biotinylated rhVEGF are added to serum samples. During overnight incubation, these two labeled molecules bind to ranibizumab, and the resulting immune complex is then captured by streptavidin-coated paramagnetic beads and analyzed for electrochemiluminescence. The ranibizumab PK ECLA has a reporting range of 300-24,000 pg/mL, based on accuracy and precision parameters. It showed high precision for both intra- and inter-assay analyses. Recovery of ranibizumab from 10 individual donors averaged between 100% and 119% of nominal concentration. There was no cross-reactivity observed in the assay to other recombinant humanized antibodies (whole molecules or monoclonal antibody fragments) or human IgG. To our knowledge, this report represents the first description of development and validation of an ECLA-based PK assay for a recombinant humanized Fab therapeutic agent.

1252 related Products with: Development of a novel homogenous electrochemiluminescence assay for quantitation of ranibizumab in human serum.

Human interleukin 2(IL-2) Mouse Anti-Insulin-Like G Anti AGO2 Human, Monoclon Anti AGO2 Human, Monoclon Bone Morphogenetic Protei Growth Differentiation Fa DNA (cytosine 5) methyltr Human Serum Albumin antib Human Serum Albumin antib Human Macrophage Inflamma Human Macrophage Inflamma Human Interleukin-32 alph

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Binding of thymoglobulin to natural killer cells leads to cell activation and interferon-gamma production.

Thymoglobulin is an antithymocyte globulin preparation used in hematopoietic stem cell transplantation (HSCT) to prevent rejection and graft-versus-host disease. Because natural killer (NK)-cell alloreactivity improves HSCT outcome, but only in patients receiving thymoglobulin, we investigated the in vitro effects of thymoglobulin on purified NK cells. Thymoglobulin binding to NK cells and NK-cell activation were assessed by flow cytometry. NK surface targets for thymoglobulin were determined by competition inhibition assays using monoclonal antibodies. Chromium 51 (Cr) release assay, Annexin V combined with 7-amino-actinomycin D staining, and carboxyfluorescein diacetate succinimidyl ester staining were used to study cytotoxic activity, apoptosis/cell death, and NK-cell proliferation, respectively. Interferon (IFN)-gamma production was determined by ELISA. Thymoglobulin, thymoglobulin derived-F(ab')2 fragments as well as rabbit IgG bound NK cells, and competed strongly with anti-CD16. Thymoglobulin enhanced the expression of activation (CD69 and NKG2D) and degranulation (CD107a) markers on NK cells. It competed with CD18 binding and decreased NK activity, but not interleukin-15-induced killer activity. Effects on apoptosis/cell death and proliferation were minimal. F(ab')2 fragments and rabbit IgG strongly induced IFN-gamma production by NK cells. Thymoglobulin binds to NK cells by CD16 by its variable and constant regions. The decrease in NK-cell cytotoxic activity is restored by interleukin-15, and contrasts sharply with the induction of activation, degranulation, and IFN-gamma production. These data support the hypothesis that thymoglobulin treatment is required to observe the improvement in HSCT outcome by NK-cell alloreactivity.

2346 related Products with: Binding of thymoglobulin to natural killer cells leads to cell activation and interferon-gamma production.

Human Tonsil Microvascula AccuzolTM Total RNA Extra Mouse Anti-Human CD94 (Na Recombinant Human Interfe Cell Meter™ Fluorimetri Cell Meter™ Fluorimetri Nycodenz, non ionic, non Dog Receptor-binding canc Mouse Anti-Mouse NC1.1 (N Mouse Anti-Mouse NC1.1 (N Mouse Anti-Mouse Natural Fluorescein 5 thiosemicar

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Antibody elicited against the gp41 N-heptad repeat (NHR) coiled-coil can neutralize HIV-1 with modest potency but non-neutralizing antibodies also bind to NHR mimetics.

Following CD4 receptor binding to the HIV-1 envelope spike (Env), the conserved N-heptad repeat (NHR) region of gp41 forms a coiled-coil that is a precursor to the fusion reaction. Although it has been a target of drug and vaccine design, there are few monoclonal antibody (mAb) tools with which to probe the antigenicity and immunogenicity specifically of the NHR coiled-coil. Here, we have rescued HIV-1-neutralizing anti-NHR mAbs from immune phage display libraries that were prepared (i) from b9 rabbits immunized with a previously described mimetic of the NHR coiled-coil, N35(CCG)-N13, and (ii) from an HIV-1 infected individual. We describe a rabbit single-chain Fv fragment (scFv), 8K8, and a human Fab, DN9, which specifically recognize NHR coiled-coils that are unoccupied by peptide corresponding to the C-heptad repeat or CHR region of gp41 (e.g. C34). The epitopes of 8K8 and DN9 were found to partially overlap with that of a previously described anti-NHR mAb, IgG D5; however, 8K8 and DN9 were much more specific than D5 for unoccupied NHR trimers. The mAbs, including a whole IgG 8K8 molecule, neutralized primary HIV-1 of clades B and C in a pseudotyped virus assay with comparable, albeit relatively modest potency. Finally, a human Fab T3 and a rabbit serum (both non-neutralizing) were able to block binding of D5 and 8K8 to a gp41 NHR mimetic, respectively, but not the neutralizing activity of these mAbs. We conclude from these results that NHR coiled-coil analogs of HIV-1 gp41 elicit many Abs during natural infection and through immunization, but that due to limited accessibility to the corresponding region on fusogenic gp41 few can neutralize. Caution is therefore required in targeting the NHR for vaccine design. Nevertheless, the mAb panel may be useful as tools for elucidating access restrictions to the NHR of gp41 and in designing potential improvements to mimetics of receptor-activated Env.

2556 related Products with: Antibody elicited against the gp41 N-heptad repeat (NHR) coiled-coil can neutralize HIV-1 with modest potency but non-neutralizing antibodies also bind to NHR mimetics.

HIV1 gp41 antibody, Monoc Shiga Toxin 1 antibody, M Shiga Toxin 2 antibody, M Candida albicans antibody Cholera toxin antibody, M Diphtheria toxin antibody Diphtheria toxin antibody HIV1 gp41 antibody, Monoc Rabbit Anti-HIV-1 gp41 An Rabbit Anti-HIV-1 gp41 An Mouse Anti-HIV-1 gp41 Ant Coiled coil domain contai

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Autoimmune autonomic ganglionopathy: IgG effects on ganglionic acetylcholine receptor current.

Autoimmune autonomic ganglionopathy (AAG) is an acquired immune-mediated form of diffuse autonomic failure. Many patients have serum antibodies that bind to the ganglionic acetylcholine receptors (AChRs) that mediate fast synaptic transmission in autonomic ganglia. Previous clinical studies and observations in animal models suggest that AAG is an antibody-mediated neurologic disorder.

1415 related Products with: Autoimmune autonomic ganglionopathy: IgG effects on ganglionic acetylcholine receptor current.

EIA for Quantitative Dete EIA for Quantitative Dete Rabbit Anti-Leptin recept Rabbit Anti-Leptin recept Rabbit Anti-Leptin recept Rabbit Anti-Leptin recept Rabbit Anti-Leptin recept Rabbit Anti-Leptin recept Rabbit Anti-Nociceptin re Rabbit Anti-Nociceptin re Rabbit Anti-Nociceptin re Rabbit Anti-Nociceptin re

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