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#33451977   2021/01/15 To Up

Phase 1 Study of the CD47 Blocker TTI-621 in Patients with Relapsed or Refractory Hematologic Malignancies.

TTI-621 (SIRPα-IgG1 Fc) is a novel checkpoint inhibitor that activates antitumor activity by blocking the CD47 "don't eat me" signal. This first-in-human phase 1 study (NCT02663518) evaluated the safety and activity of TTI-621 in relapsed/refractory (R/R) hematologic malignancies.
Stephen M Ansell, Michael Maris, Alexander M Lesokhin, Robert Chen, Ian W Flinn, Ahmed Sawas, Mark D Minden, Diego Villa, Mary-Elizabeth M Percival, Anjali S Advani, James M Foran, Steven Horwitz, Matthew Mei, Jasmine Zain, Kerry J Savage, Christiane Querfeld, Oleg E Akilov, Lisa D Johnson, Tina Catalano, Penka S Petrova, Robert A Uger, Eric L Sievers, Anca Milea, Kathleen Roberge, Yaping Shou, Owen A O'Connor

2825 related Products with: Phase 1 Study of the CD47 Blocker TTI-621 in Patients with Relapsed or Refractory Hematologic Malignancies.

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#33451741   2020/11/23 To Up

Decreased Immunoglobulin G Core Fucosylation, A Player in Antibody-dependent Cell-mediated Cytotoxicity, is Associated with Autoimmune Thyroid Diseases.

Autoimmune thyroid diseases (AITD) are the most common group of autoimmune diseases, associated with lymphocyte infiltration and the production of thyroid autoantibodies, like thyroid peroxidase antibodies (TPOAb), in the thyroid gland. Immunoglobulins and cell-surface receptors are glycoproteins with distinctive glycosylation patterns that play a structural role in maintaining and modulating their functions. We investigated associations of total circulating IgG and peripheral blood mononuclear cells glycosylation with AITD and the influence of genetic background in a case-control study with several independent cohorts and over 3,000 individuals in total. The study revealed an inverse association of IgG core fucosylation with TPOAb and AITD, as well as decreased peripheral blood mononuclear cells antennary α1,2 fucosylation in AITD, but no shared genetic variance between AITD and glycosylation. These data suggest that the decreased level of IgG core fucosylation is a risk factor for AITD that promotes antibody-dependent cell-mediated cytotoxicity previously associated with TPOAb levels.
Tiphaine C Martin, Mirna Šimurina, Marta Ząbczyńska, Marina Martinic Kavur, Magdalena Rydlewska, Marija Pezer, Kamila Kozłowska, Andrea Burri, Marija Vilaj, Renata Turek-Jabrocka, Milena Krnjajić-Tadijanović, Małgorzata Trofimiuk-Müldner, Ivo Ugrina, Anna Lityńska, Alicja Hubalewska-Dydejczyk, Irena Trbojevic-Akmacic, Ee Mun Lim, John P Walsh, Ewa Pocheć, Tim D Spector, Scott G Wilson, Gordan Lauc

2871 related Products with: Decreased Immunoglobulin G Core Fucosylation, A Player in Antibody-dependent Cell-mediated Cytotoxicity, is Associated with Autoimmune Thyroid Diseases.

100ug Lyophilized100ug Lyophilized100ug Lyophilized50 ul100ug Lyophilized

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#33451393   2020/12/02 To Up

Site-specific N-glycan Analysis of Antibody-binding Fc γ Receptors from Primary Human Monocytes.

FcγRIIIa (CD16a) and FcγRIIa (CD32a) on monocytes are essential for proper effector functions including antibody dependent cellular cytotoxicity (ADCC) and phagocytosis (ADCP). Indeed, therapeutic monoclonal antibodies (mAbs) that bind FcγRs with greater affinity exhibit greater efficacy. Furthermore, post-translational modification impacts antibody binding affinity, most notably the composition of the asparagine(N)-linked glycan at N162 of CD16a. CD16a is widely recognized as the key receptor for the monocyte response, however the post-translational modifications of CD16a from endogenous monocytes are not described. Here we isolated monocytes from individual donors and characterized the composition of CD16a and CD32a N-glycans from all modified sites. The composition of CD16a N-glycans varied by glycosylation site and donor. CD16a displayed primarily complex-type biantennary N-glycans at N162, however some individuals expressed CD16a V158 with ∼20% hybrid and oligomannose types which increased affinity for IgG1 Fc according to surface plasmon resonance binding analyses. The CD16a N45-glycans contain markedly less processing than other sites with >75% hybrid and oligomannose forms. N38 and N74 of CD16a both contain highly processed complex-type N-glycans with N-acetyllactosamine repeats and complex-type biantennary N-glycans dominate at N169. The composition of CD16a N-glycans isolated from monocytes included a higher proportion of oligomannose-type N-glycans at N45 and less sialylation plus greater branch fucosylation than we observed in a recent analysis of NK cell CD16a. The additional analysis of CD32a from monocytes revealed different features than observed for CD16a including the presence of a predominantly biantennary complex-type N-glycans with two sialic acids at both sites (N64 and N145).
Jacob T Roberts, Kashyap R Patel, Adam W Barb

2299 related Products with: Site-specific N-glycan Analysis of Antibody-binding Fc γ Receptors from Primary Human Monocytes.

100ul4 Membranes/Box 100ul 100ul4 Arrays/Slide1 kit4 Membranes/Box4 Membranes/Box 100ul100 μg4 Membranes/Box4 Membranes/Box

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#33451345   2021/01/15 To Up

A phase Ib/II study of xentuzumab, an IGF-neutralising antibody, combined with exemestane and everolimus in hormone receptor-positive, HER2-negative locally advanced/metastatic breast cancer.

Xentuzumab-a humanised IgG1 monoclonal antibody-binds IGF-1 and IGF-2, inhibiting their growth-promoting signalling and suppressing AKT activation by everolimus. This phase Ib/II exploratory trial evaluated xentuzumab plus everolimus and exemestane in hormone receptor-positive, locally advanced and/or metastatic breast cancer (LA/MBC).
Peter Schmid, Marie-Paule Sablin, Jonas Bergh, Seock-Ah Im, Yen-Shen Lu, Noelia Martínez, Patrick Neven, Keun Seok Lee, Serafín Morales, J Alejandro Pérez-Fidalgo, Douglas Adamson, Anthony Gonçalves, Aleix Prat, Guy Jerusalem, Laura Schlieker, Rosa-Maria Espadero, Thomas Bogenrieder, Dennis Chin-Lun Huang, John Crown, Javier Cortés

1837 related Products with: A phase Ib/II study of xentuzumab, an IGF-neutralising antibody, combined with exemestane and everolimus in hormone receptor-positive, HER2-negative locally advanced/metastatic breast cancer.

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#33447556   // To Up

Proteomics-based analysis indicating α-enolase as a potential biomarker in primary Sjögren's syndrome.

Primary Sjögren's syndrome (pSS) is a chronic autoimmune disease. Its etiology is not well understood. Salivary glands are the main target organ in pSS, investigating the changes of salivary protein in pSS patients may not only be a valuable way of identifying new biomarkers/antigens for pSS, but also of revealing the pathogenesis underlying this autoimmune disease. In the present study, we aimed to investigate new biomarkers and explore their potential role in pSS.
Pan Wei, Yixiao Xing, Boya Li, Feng Chen, Hong Hua

1715 related Products with: Proteomics-based analysis indicating α-enolase as a potential biomarker in primary Sjögren's syndrome.

96 samples100 plates100 assays100 assays100 assays100 assays100ug10 plates100 assays48 samples

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#33446980   // To Up

Neutrophil CD64 a Diagnostic and Prognostic Marker of Sepsis in Adult Critically Ill Patients: A Brief Review.

Sepsis is a life-threatening organ dysfunction with increased incidence of morbidity and mortality. Early diagnosis and prompt therapeutic intervention is the cornerstone of sepsis care. Biomarkers play an important role in sepsis having both diagnostic and prognostic implications. Neutrophil CD64 (nCD64) is a useful candidate biomarker for sepsis. Neutrophil CD64 also known as Fc receptor 1 (FcR1), is a high-affinity receptor present on neutrophils for Fc part of immunoglobulin-G (IgG) heavy chain. Its expression gets strongly upregulated in response to proinflammatory cytokines of infection within 4-6 hours. Neutrophil CD64 integrates function involving both innate and adaptive immune responses. The aim of this review is to present literature about nCD64 as a diagnostic and prognostic marker in patients with sepsis/septic shock.
Rupali Patnaik, Afzal Azim, Vikas Agarwal

1268 related Products with: Neutrophil CD64 a Diagnostic and Prognostic Marker of Sepsis in Adult Critically Ill Patients: A Brief Review.

18 kgs100 assays

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#33446839   2021/01/14 To Up

Generation and functional characterization of a single-chain variable fragment (scFv) of the anti-FGF2 3F12E7 monoclonal antibody.

Single-chain variable fragments (scFvs) are small-sized artificial constructs composed of the immunoglobulin heavy and light chain variable regions connected by a peptide linker. We have previously described an anti-fibroblast growth factor 2 (FGF2) immunoglobulin G (IgG) monoclonal antibody (mAb), named 3F12E7, with notable antitumor potential revealed by preclinical assays. FGF2 is a known angiogenesis-associated molecule implicated in tumor progression. In this report, we describe a recombinant scFv format for the 3F12E7 mAb. The results demonstrate that the generated 3F12E7 scFv, although prone to aggregation, comprises an active anti-FGF2 product that contains monomers and small oligomers. Functionally, the 3F12E7 scFv preparations specifically recognize FGF2 and inhibit tumor growth similar to the corresponding full-length IgG counterpart in an experimental model. In silico molecular analysis provided insights into the aggregation propensity and the antigen-recognition by scFv units. Antigen-binding determinants were predicted outside the most aggregation-prone hotspots. Overall, our experimental and prediction dataset describes an scFv scaffold for the 3F12E7 mAb and also provides insights to further engineer non-aggregated anti-FGF2 scFv-based tools for therapeutic and research purposes.
Rodrigo Barbosa de Aguiar, Tábata de Almeida da Silva, Bruno Andrade Costa, Marcelo Ferreira Marcondes Machado, Renata Yoshiko Yamada, Camila Braggion, Kátia Regina Perez, Marcelo Alves Silva Mori, Vitor Oliveira, Jane Zveiter de Moraes

2351 related Products with: Generation and functional characterization of a single-chain variable fragment (scFv) of the anti-FGF2 3F12E7 monoclonal antibody.

100ul100ug100 ug100ul100ul100 ul100ug100ul100ug25 µg100ul100 ul

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