A5008900440- Monoclonal and Polyclonal Antibodies Research
- Glycosylation and Glycoproteins Research
- Multiple Myeloma Research and Treatments
- Neuropeptides and Animal Physiology
- Protein purification and stability
- Receptor Mechanisms and Signaling
- Neuroscience and Neuropharmacology Research
- CAR-T cell therapy research
- Nanofabrication and Lithography Techniques
- HER2/EGFR in Cancer Research
- Adenosine and Purinergic Signaling
- Immune Cell Function and Interaction
- Transgenic Plants and Applications
- Nicotinic Acetylcholine Receptors Study
- Advanced ceramic materials synthesis
- Asthma and respiratory diseases
- Advanced Biosensing Techniques and Applications
- Galectins and Cancer Biology
- Pharmacological Effects of Natural Compounds
- Toxin Mechanisms and Immunotoxins
- T-cell and B-cell Immunology
- Peptidase Inhibition and Analysis
- Dermatology and Skin Diseases
- Silicon and Solar Cell Technologies
- Chemokine receptors and signaling
Glenmark Pharmaceuticals (Switzerland)
2011-2024
Ichnos Sciences (United States)
2023
Biognosys (Switzerland)
2022
International Museum of Horology
2018
University of Edinburgh
2000-2004
Abstract Antibody engineering can tailor the design and activities of therapeutic antibodies for better efficiency or other advantageous clinical properties. Here we report development ISB 1442, a fully human bispecific antibody designed to re-establish synthetic immunity in CD38+ hematological malignancies. 1442 consists two anti-CD38 arms targeting distinct epitopes that preferentially drive binding tumor cells enable avidity-induced blocking proximal CD47 receptors on same cell while...
ISB 1442 is a bispecific biparatopic antibody in clinical development to treat hematological malignancies. It consists of two adjacent anti-CD38 arms targeting non-overlapping epitopes that preferentially drive binding tumor cells and low-affinity anti-CD47 arm enable avidity-induced blocking proximal CD47 receptors. We previously reported the pharmacology 1442, designed reestablish synthetic immunity CD38+ Here, we describe discovery, optimization characterization antigen fragment (Fab)...
Bispecific antibodies (bsAbs) are of significant importance to the development novel antibody-based therapies, and heavy chain (Hc) heterodimers represent a major class bispecific drug candidates. Current technologies for generation Hc suboptimal often suffer from contamination by homodimers posing purification challenges. Here, we introduce new technology based on biomimicry wherein protein-protein interfaces two different immunoglobulin (Ig) constant domain pairs exchanged in part or fully...
The γ-aminobutyric acid type B (GABA<sub>B</sub>) receptor is a heterodimeric G-protein-coupled receptor. In humans, three splice variants of the GABA<sub>B</sub> 1 (R1) subunit differ in having one, both, or neither two putative complement control protein (CCP) modules at extracellular N terminus, prior to GABA-binding domain. <i>in vivo</i> function these predicted remains be discovered, but likely association with matrix proteins intriguing. portion R1a variant encompassing both its CCP...
Background The binding of two biological targets with a single IgGbased molecule is thought to be beneficial for clinical efficacy. However the technological challenges development bispecific platform are numerous. While correct pairing heterologous heavy and light chains (Hc Lc) can achieved by engineering native IgG scaffolds, crucial properties such as thermostability, effector function low immunogenicity should maintained [1]. has expressed at industrially relevant levels minimum...
We previously reported efficient heavy-chain assembly of heterodimeric bispecific antibodies by exchanging the interdomain protein interface human IgG1 CH3 dimer with constant α and β domains T-cell receptor, a technology known as engagement based on receptor (BEAT). Efficient heterodimerization in mammalian cell transient transfections was observed, but levels were influenced nature binding arms, particularly Fab-scFv-Fc format. In this study, we report single amino acid change that...
8044 Background: ISB 1342 is a bispecific antibody heterodimer based on the Ichnos proprietary Bispecific Engagement by Antibodies T cell receptor (BEAT) platform. first-in-class CD38 engager under investigation in subjects with relapsed multiple myeloma refractory to proteasome inhibitors (PIs), immunomodulators (IMiDs) and daratumumab (study 1342-101). Methods: was engineered single chain variable fragment (scFv) arm that specifically recognizes cluster of differentiation (CD)3-epsilon...
Heavy chain (Hc) heterodimers represent a majority of bispecific antibodies (bsAbs) under clinical development. Although recent technologies achieve high levels Hc heterodimerization (HD), traces homodimer contaminants are often present, and as consequence robust purification techniques for generating highly pure in single step needed. Here, we describe two different methods that exploit differences Protein A (PA) or G (PG) avidity between homo- heterodimers. Differential elution species was...
Abstract GBR 401 is a humanized monoclonal antibody directed against domain 2 of human B-lymphocyte antigen CD19 and displays number mechanisms which can specifically target kill B cells. Glenmark developing this product as B-cell depleting agent for cell malignancies. the archetypal marker used in diagnosis lymphomas/ leukemias by identification abnormal numbers and/or populations. Expression found majority lineage malignancies including, but not limited to non-Hodgkin's lymphoma, chronic...
ABSTRACT Over the past two decades, monoclonal antibodies have emerged as a versatile class of therapeutics with unique properties. More than 30 therapeutic are now approved in United States and European Union, numerous candidates filling preclinical clinical pipeline every major pharmaceutical companies biotechnology firms. Monoclonal advantage over traditional medicines that they able to specifically bind desired targets little no associated toxicity. In recent years, for oncology...