To develop robust mAb biologics, it is vital to fully characterize the protein, including its primary sequence, mutations, and important post-translational modifications
To develop robust mAb biologics, it is vital to fully characterize the protein, including its primary sequence, mutations, and important post-translational modifications
To develop robust mAb biologics, it is vital to fully characterize the protein, including its primary sequence, mutations, and important post-translational modifications
To develop robust mAb biologics, it is vital to fully characterize the protein, including its primary sequence, mutations, and important post-translational modifications
To develop robust mAb biologics, it is vital to fully characterize the protein, including its primary sequence, mutations, and important post-translational modifications
To develop robust mAb biologics, it is vital to fully characterize the protein, including its primary sequence, mutations, and important post-translational modifications
To develop robust mAb biologics, it is vital to fully characterize the protein, including its primary sequence, mutations, and important post-translational modifications
Authors: Teresa Nunez, Amber Couzens, Jin Duan, Chelsea Reitzel, Rosalin Dubois, Lin Wu, Qixin Liu, Thierry Le Bihan, Marko Jović, Dominic Narang, Bin Ma Published: Nov 13, 2023 Abstract In this study, the challenge of accessing functional antibodies from the circulating antibody repertoire was addressed using Rapid Novor's antibody [...]
Our client is a biotechnology company developing therapeutics that target cancer-specific carbohydrate antigens on the surface of tumour cells.
Our client is a biotechnology company developing therapeutics that target cancer-specific carbohydrate antigens on the surface of tumour cells.
To develop robust mAb biologics, it is vital to fully characterize the protein, including its primary sequence, mutations, and important post-translational modifications
With 22 functional T cell receptor (TCR)Vβ subunit families making up the normal T cell repertoire, signals from these cell surface receptors often determine the fate of normal cells. However, mutations in TCR signaling proteins are frequently associated with peripheral T cell lymphomas (TCLs), including adult T cell leukemia/lymphoma (ATL), which indicates a driving role for TCRs in TCL oncogenesis. As TCL and ATL are clonal in nature, tumour cells typically express a single TCRVβ subunit with no bias in the usage of TCRVβ subunit families. Consequently, targeting the specific TCRVβ subunit presents a promising therapeutic approach that is highly selective and tumour-specific.
De novo protein sequencing can support the development of antibody-based reagents, including Dbs and other antibody fragments. Working with the exact amino acid sequence of the mAb can help facilitate the in silico design and conjugation design processes, ensuring accuracy in the final engineered format.
By conducting an in-depth analysis of non-antigen immunized sheep Ig repertoires via NGS, this data provides further insight into the adaptive immunity of sheep and lays a foundation for future work on immunogenetics and ovine antibody drug development.
Antibodies with established, specific targets can be sequenced and utilized to engineer the hinge region and antigen-binding domains with antibody fragments and derivatives. With the sequence information in hand, further steps to optimizing a viable therapeutic approach can be more accessible.
To date, near-complete cryo-electron microscopy (cryo-EM) density maps of pTSC were obtained by either employing chemical cross-linking or graphene oxide-coated grids during sample preparation; however, this may not reflect the true native state of pTSC.
De novo protein sequencing provided the research team with insurance by securing the complete amino acid sequence of a therapeutic mAb candidate for ADAD. This mass spectrometry-based protein sequencing technique can be used to obtain the sequence information of any antibody or protein for biomarker discovery, characterization, and validation. Access to this structural information only broadens our understanding of disease pathogenesis and fosters the development of innovative therapeutic or preventative treatments.
αβTCR-engineered T cells have been applied in clinical trials, specifically directed against cancer/testis antigens. Though the clinical outcomes are promising, only a small proportion of patients benefit from these novel treatments. Lower response rates are partially attributed to a heterogeneous mixture of non-engineered and poorly engineered T cells that remain in the administered therapeutic product. For successful translation of these novel treatments into the clinic, engineering efforts should be reinforced with effective methods for engineered T cell purification and engineered T cell elimination post infusion into patients.
Hendra virus (HeV) and Nipah virus (NiV) are types of Henipaviruses (HNVs) that originated in bats and can infect the human respiratory system with detrimental consequences. As enveloped, single-stranded RNA viruses, HeV and NiV use attachment (G) and fusion (F) glycoproteins on the envelope membrane to enter host cells. So far, there are no approved therapeutics or vaccines to combat the viruses in humans.
Monoclonal antibodies are essential reagents and research tools. They are commonly generated and produced in hybridoma cells and are expected to be highly consistent. However, the instability and fragility of hybridoma cells can cause unwanted mutations, additional chains, and permanent loss of important antibodies. On the other hand, the lack of standardization validation for commercial antibodies often keeps researchers in the dark leading to the reproducibility crisis.
The ongoing pandemic has reinforced the need for in vitro diagnostics to globally surveille emerging pathogens and provide better medical care. In particular, immunoassays are favoured due to their affordability, ease, and speed. Nevertheless, the combination of rapidly evolving pathogens, and more complex diseases resulting from increasing life expectancy worldwide require more sensitive and specific immunoassays in the nick of time. To increase sensitivity, immunoassay development can benefit from exploiting industry-leading technologies such as de novo protein sequencing.
Circulating in blood is a multitude of biologically important antibodies. These pools of polyclonal antibodies (pAb) are invaluable sources for drug discovery against various diseases, and for the development of robust immunoreagents for diagnostics, and research.
To develop robust mAb biologics, it is vital to fully characterize the protein, including its primary sequence, mutations, and important post-translational modifications
In this study, we conducted a large-scale statistical analysis of protein sequencing data from samples digested with multiple proteases to understand the impact of using different combinations of proteases to improve the depth of sequence coverage in the application of de novo protein sequencing.
Monoclonal antibodies (mAbs) are widely used in research, diagnosis, and pharmaceutical purposes. Lately, the relatively lower quality of research-purpose mAbs is a point of concern within the research community.
The DNA sequences of antibodies are highly diverse due to the V-(D)-J recombination and hypersomatic mutations. As such, relying on homology-based searches to sequence novel antibodies can introduce bias to sequences obtained from proteomics approaches.