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Search results for: antibody

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#38499458   2024/03/17 To Up

COVID-19 vaccination in cancer patients: Immune responses one year after the third dose.

Cancer patients (CPs), being immunosuppressed due to the treatment received or to the disease itself, are more susceptible to infections and their potential complications, showing therefore an increased risk of developing severe COVID-19 compared to the general population. We evaluated the immune responses to anti-SARS-CoV-2 vaccination in patients with solid tumors one year after the administration of the third dose and the effect of cancer treatment on vaccine immunogenicity was assessed. Healthy donors (HDs) were enrolled. Binding and neutralizing antibody (Ab) titers were evaluated using chemiluminescence immunoassay (CLIA) and Plaque Reduction Neutralization Test (PRNT) respectively. T-cell response was analyzed using multiparametric flow cytometry. CPs who were administered three vaccine doses showed lower Ab titers than CPs with four doses and HDs. Overall, a lower cell-mediated response was found in CPs, with a predominance of monofunctional T-cells producing TNFα. Lower Ab titers and a weaker T-cell response were observed in CPs without prior SARS-CoV-2 infection when compared to those with a previous infection. While no differences in the humoral response were found comparing immunotherapy and non-immunotherapy patients, a stronger T-cell response in CPs treated with immunotherapy was observed. Our results emphasize the need of booster doses in cancer patients to achieve a level of protection similar to that observed in healthy donors and underlines the importance of considering the treatment received to reach a proper immune response.
Roberta Campagna, Federica Dominelli, Maria Antonella Zingaropoli, Fabio Ciurluini, Giorgia Grilli, Alessandra Amoroso, Angelo De Domenico, Donatella Amatore, Maria Stella Lia, Enrico Cortesi, Vincenzo Picone, Claudio Maria Mastroianni, Maria Rosa Ciardi, Riccardo De Santis, Florigio Lista, Guido Antonelli, Ombretta Turriziani

2571 related Products with: COVID-19 vaccination in cancer patients: Immune responses one year after the third dose.



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#38499233   2024/03/16 To Up

Epitope mapping of SARS-CoV-2 RBDs by hydroxyl radical protein footprinting reveals the importance of including negative antibody controls.

Understanding protein-protein interactions is crucial for drug design and investigating biological processes. Various techniques, such as CryoEM, X-ray spectroscopy, linear epitope mapping, and mass spectrometry-based methods, can be employed to map binding regions on proteins. Commonly used mass spectrometry-based techniques are cross-linking and hydrogen‑deuterium exchange (HDX). Another approach, hydroxyl radical protein footprinting (HRPF), identifies binding residues on proteins but faces challenges due to high initial costs and complex setups. This study introduces a generally applicable method using Fenton chemistry for epitope mapping in a standard mass spectrometry laboratory. It emphasizes the importance of controls, particularly the inclusion of a negative antibody control, not widely utilized in HRPF epitope mapping. Quantification by TMT labelling is introduced to reduce false positives, enabling direct comparison between sample conditions and biological triplicates. Additionally, six technical replicates were incorporated to enhance the depth of analysis. Observations on the receptor-binding domain (RBD) of SARS-CoV-2 Spike Protein, Alpha and Delta variants, revealed both binding and opening regions. Significantly changed peptides upon mixing with a negative control antibody suggested structural alterations or nonspecific binding induced by the antibody alone. Integration of negative control antibody experiments and high overlap between biological triplicates led to the exclusion of 40% of significantly changed regions. The final identified binding region correlated with existing literature on neutralizing antibodies against RBD. The presented method offers a straightforward implementation for HRPF analysis in a generic mass spectrometry-based laboratory. Enhanced data reliability was achieved through increased technical and biological replicates alongside negative antibody controls.
Daniel Nyberg Larsen, Jakub Zbigniew Kaczmarek, Yaseelan Palarasah, Jonas Heilskov Graversen, Peter Højrup

2035 related Products with: Epitope mapping of SARS-CoV-2 RBDs by hydroxyl radical protein footprinting reveals the importance of including negative antibody controls.

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#38499217   2024/03/16 To Up

Construction and analysis of the immune effect of two different vaccine types based on Vibrio harveyi VgrG.

Vibrio harveyi poses a significant threat to fish and invertebrates in mariculture, resulting in substantial financial repercussions for the aquaculture sector. Valine-glycine repeat protein G (VgrG) is essential for the type VI secretion system's (T6SS) assembly and secretion. VgrG from V. harveyi QT520 was cloned and analyzed in this study. The localization of VgrG was determined by Western blot, which revealed that it was located in the cytoplasm, secreted extracellularly, and attached to the membrane. The effectiveness of two vaccinations against V. harveyi infection-a subunit vaccine (rVgrG) and a DNA vaccine (pCNVgrG) prepared with VgrG was evaluated. The findings indicated that both vaccines provided a degree of protection against V. harveyi challenge. At 4 weeks post-vaccination (p.v.), the rVgrG and pCNVgrG exhibited relative percent survival rates (RPS) of 71.43% and 76.19%, respectively. At 8 weeks p.v., the RPS for rVgrG and pCNVgrG were 68.21% and 72.71%, respectively. While both rVgrG and pCNVgrG elicited serum antibody production, the subunit vaccinated fish demonstrated significantly higher levels of serum anti-VgrG specific antibodies than the DNA vaccine group. The result of qRT-PCR demonstrated that the expression of major histocompatibility complex (MHC) class Iα, tumor necrosis factor-alpha (TNF-α), interferon γ (IFNγ), and cluster of differentiation 4 (CD4) were up-regulated by both rVgrG and pCNVgrG. Fish vaccinated with rVgrG and pCNVgrG exhibited increased activity of acid phosphatase, alkaline phosphatase, superoxide dismutase, and lysozyme. These findings suggest that VgrG from V. harveyi holds potential for application in vaccination.
Xiangyu Du, Minjie Kang, Chunhuan Yang, Xinping Yao, Lvliang Zheng, Ying Wu, Panpan Zhang, Han Zhang, Yongcan Zhou, Yun Sun

2583 related Products with: Construction and analysis of the immune effect of two different vaccine types based on Vibrio harveyi VgrG.

5 G100ug100ug LyophilizedOne 96-Well Microplate Ki1 module 15 ml 1 module500 MG0.2 mg2000 IU1 module

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#38499168   2024/03/16 To Up

Formation and clinical effects of anti-drug antibodies against biologics in psoriasis treatment: An analysis of current evidence.

Formation of anti-drug antibodies (ADAs) against biologics is an important cause of psoriasis treatment failure.
Xiaoying Sun, Ziyang Cui, Qingyun Wang, Liu Liu, Xiaojie Ding, Jiao Wang, Xiaoce Cai, Bin Li, Xin Li

2940 related Products with: Formation and clinical effects of anti-drug antibodies against biologics in psoriasis treatment: An analysis of current evidence.

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#38499123   2024/03/16 To Up

Rapid and sensitive detection of SARS-CoV-2 IgM through luciferase luminescence on an automatic platform.

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Yibing Zhang, Yun Zhang, Wenhao Zhou, Ping He, Xueni Sun, Junhua Li, Hongping Wei, Junping Yu

1861 related Products with: Rapid and sensitive detection of SARS-CoV-2 IgM through luciferase luminescence on an automatic platform.

200ul10 mg200ul200ug200ug100ul200ul25 mg100 ul25ml 200ul100ug Lyophilized

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#38498976   2024/03/18 To Up

Autologous HSCT with novel agent-based induction and consolidation followed by lenalidomide maintenance for untreated multiple myeloma.

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Yasuo Mori, Jun Takizawa, Yuna Katsuoka, Naoki Takezako, Koji Nagafuji, Hiroshi Handa, Junya Kuroda, Kazutaka Sunami, Tomohiko Kamimura, Ryosuke Ogawa, Yoshikane Kikushige, Mine Harada, Koichi Akashi, Toshihiro Miyamoto,

1490 related Products with: Autologous HSCT with novel agent-based induction and consolidation followed by lenalidomide maintenance for untreated multiple myeloma.

1000 tests100ug

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#38498694   2024/03/18 To Up

AQP4-DARPin1: A Chimeric Antigen Based on Scaffold Protein DARPin for Efficient Detection of AQP4-IgG in NMOSD.

AQP4-IgG is an autoantibody associated with neuromyelitis optica spectroscopic disorder (NMOSD), a central nervous system inflammatory disease that requires early diagnosis and treatment. We designed two fusion proteins, AQP4-DARPin1 and AQP4-DARPin2, comprising the complete antigenic epitopes of aquaporin-4 (AQP4) and the constant region of the scaffold protein DARPin. These fusion proteins were expressed and purified from and coated on microplates to develop an efficient method for detecting AQP4-IgG. Molecular dynamics simulation revealed that the fusion of AQP4 extracellular epitopes with DARPin did not alter the main structure of DARPin. The purified AQP4-DARPins bound recombinant antibody rAb-53 (AQP4-IgG) with affinities of 135 and 285 nM, respectively. Enzyme-linked immunosorbent assay (ELISA) and immunoprecipitation demonstrated that AQP4-DARPin1 specifically recognized AQP4-IgG in the NMOSD patient serum. AQP4-DARPin1 as a coated antigen showed higher ELISA signal and end point dilution ratio than full-length AQP4. Our AQP4-DARPin1-coated AQP4-IgG ELISA had 100% specificity and 90% sensitivity. These results indicate that AQP4-DARPin1, compared to existing detection strategies that use full-length or extracellular loop peptides of AQP4, provides a new and more effective approach to the ELISA detection of NMOSD.
Xiaofei Wang, Shubei Ma, Ying Bai, Xinyang Wu, Fangling Ji, Lingyun Jia

1831 related Products with: AQP4-DARPin1: A Chimeric Antigen Based on Scaffold Protein DARPin for Efficient Detection of AQP4-IgG in NMOSD.

50ul (1mg/ml)0.1ml (1mg/ml)0.1ml0.1ml50ul0.1ml0.1ml0.1ml (1mg/ml)0.1ml (1mg/ml)1mg0.1ml1 mg

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#38498555   2024/03/18 To Up

Sero-prevalence and risk factors associated with occurrence of anti-Brucella antibodies among slaughterhouse workers in Uganda.

Brucellosis is a febrile zoonosis occurring among high-risk groups such as livestock keepers and abattoir workers and is a public health priority in Uganda. The technical complexities of bacteriological and molecular methods make serological approaches the cornerstone of diagnosis of human brucellosis in resource limited settings. Therefore, proper application and interpretation of serological tests is central to achieve a correct diagnosis.
James Katamba Bugeza, Kristina Roesel, Denis Rwabiita Mugizi, Lordrick Alinaitwe, Velma Kivali, Clovice Kankya, Ignacio Moriyon, Elizabeth Anne Jessie Cook

1412 related Products with: Sero-prevalence and risk factors associated with occurrence of anti-Brucella antibodies among slaughterhouse workers in Uganda.

100 μg100 μg1 mg100 μg100 μg100 μg0.1 mg100 μg100 μg100 μg100 μg100 μg

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#38498504   2024/03/18 To Up

Glycoprofiling of proteins as prostate cancer biomarkers: A multinational population study.

The glycoprofiling of two proteins, the free form of the prostate-specific antigen (fPSA) and zinc-α-2-glycoprotein (ZA2G), was assessed to determine their suitability as prostate cancer (PCa) biomarkers. The glycoprofiling of proteins was performed by analysing changes in the glycan composition on fPSA and ZA2G using lectins (proteins that recognise glycans, i.e. complex carbohydrates). The specific glycoprofiling of the proteins was performed using magnetic beads (MBs) modified with horseradish peroxidase (HRP) and antibodies that selectively enriched fPSA or ZA2G from human serum samples. Subsequently, the antibody-captured glycoproteins were incubated on lectin-coated ELISA plates. In addition, a novel glycoprotein standard (GPS) was used to normalise the assay. The glycoprofiling of fPSA and ZA2G was performed in human serum samples obtained from men undergoing a prostate biopsy after an elevated serum PSA, and prostate cancer patients with or without prior therapy. The results are presented in the form of an ROC (Receiver Operating Curve). A DCA (Decision Curve Analysis) to evaluate the clinical performance and net benefit of fPSA glycan-based biomarkers was also performed. While the glycoprofiling of ZA2G showed little promise as a potential PCa biomarker, the glycoprofiling of fPSA would appear to have significant clinical potential. Hence, the GIA (Glycobiopsy ImmunoAssay) test integrates the glycoprofiling of fPSA (i.e. two glycan forms of fPSA). The GIA test could be used for early diagnoses of PCa (AUC = 0.83; n = 559 samples) with a potential for use in therapy-monitoring (AUC = 0.90; n = 176 samples). Moreover, the analysis of a subset of serum samples (n = 215) revealed that the GIA test (AUC = 0.81) outperformed the PHI (Prostate Health Index) test (AUC = 0.69) in discriminating between men with prostate cancer and those with benign serum PSA elevation.
Andrea Pinkeova, Adela Tomikova, Aniko Bertokova, Eva Fabinyova, Radka Bartova, Eduard Jane, Stefania Hroncekova, Karl-Dietrich Sievert, Roman Sokol, Michal Jirasko, Radek Kucera, Iris E Eder, Wolfgang Horninger, Helmut Klocker, Petra Ďubjaková, Juraj Fillo, Tomas Bertok, Jan Tkac

1953 related Products with: Glycoprofiling of proteins as prostate cancer biomarkers: A multinational population study.



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#38498344   2024/03/18 To Up

Surface chemical modification of poly(dimethylsiloxane) for stabilizing antibody immobilization and T cell cultures.

Advances in cell immunotherapy underscore the need for effective methods to produce large populations of effector T cells, driving growing interest in T-cell bioprocessing and immunoengineering. Research suggests that T cells demonstrate enhanced expansion and differentiation on soft matrices in contrast to rigid ones. Nevertheless, the influence of antibody conjugation chemistry on these processes remains largely unexplored. In this study, we examined the effect of antibody conjugation chemistry on T cell activation, expansion and differentiation using a soft and biocompatible polydimethylsiloxane (PDMS) platform. We rigorously evaluated three distinct immobilization methods, beginning with the use of amino-silane (PDMS-NH-Ab), followed by glutaraldehyde (PDMS-CHO-Ab) or succinic acid anhydride (PDMS-COOH-Ab) activation, in addition to the conventional physical adsorption (PDMS-Ab). By employing both stable amide bonds and reducible Schiff bases, antibody conjugation significantly enhanced antibody loading and density compared to physical adsorption. Furthermore, we discovered that the PDMS-COOH-Ab surface significantly promoted IL-2 secretion, CD69 expression, and T cell expansion compared to the other groups. Moreover, we observed that both PDMS-COOH-Ab and PDMS-NH-Ab surfaces exhibited a tendency to induce the differentiation of naïve CD4 T cells into Th1 cells, whereas the PDMS-Ab surface elicited a Th2-biased immunological response. These findings highlight the importance of antibody conjugation chemistry in the design and development of T cell culture biomaterials. They also indicate that PDMS holds promise as a material for constructing culture platforms to modulate T cell activation, proliferation, and differentiation.
Qiongjiao Zeng, Bowen Xu, Cheng Qian, Nan Li, Zhenhong Guo, Shuqing Wu

1281 related Products with: Surface chemical modification of poly(dimethylsiloxane) for stabilizing antibody immobilization and T cell cultures.

1 ml1000 tests100μg 100ul25 µg100 ul25 µg0.1 ml100 TESTS0.25 mg1,000 tests

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