Markus Seeger

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Markus Seeger

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Redcar, UK, July 8, Absolute Antibody Ltd. Under the partnership, the original nanobodies and newly engineered formats are now available to the global research community for use as serological controls and in COVID therapeutic development.

The synthetic nanobodies possess particular promise for the development of inhalable drugs, which could offer a convenient treatment option for the COVID pandemic.

Nanobodies are small antibody fragments that can reach previously inaccessible parts of the body due to their compact size. Within a two-week timeframe, the lab had identified more than 60 unique anti-RBD sybodies from combinatorial display libraries.

Moreover, two of the sybodies can simultaneously bind the RBD, which could enable the construction of a polyvalent antiviral drug.

Absolute Antibody recombinantly produces the SARS-CoV-2 synthetic nanobodies for ensured batch-to-batch reproducibility, high purity and low endotoxin levels.

In addition, Absolute Antibody has used antibody engineering to fuse the nanobodies to Fc domains in different species, isotypes and subtypes.

These recombinant engineered antibodies extend the applications of the sybodies by varying effector function and permitting increased half-life in in vivo studies.

Researchers are exploring their potential as inhalable COVID drugs, which would be easier to administer and reach patient's lungs faster than other treatment formulations.

Within a two-week timeframe, the lab had identified more than 60 unique anti-RBD sybodies from combinatorial display libraries.

Moreover, two of the sybodies can simultaneously bind the RBD, which could enable the construction of a polyvalent antiviral drug.

The SARS-CoV-2 sybodies are therefore valuable tools for coronavirus research, diagnostics and therapeutic development, and the panel is now available to researchers worldwide via Absolute Antibody's online catalog.

Absolute Antibody recombinantly produces the SARS-CoV-2 synthetic nanobodies for ensured batch-to-batch reproducibility, high purity and low endotoxin levels.

In addition, Absolute Antibody has used antibody engineering to fuse the nanobodies to Fc domains in different species, isotypes and subtypes.

These recombinant engineered antibodies extend the applications of the sybodies by varying effector function and permitting increased half-life in in vivo studies.

In addition to the new synthetic antibodies, Absolute Antibody offers a variety of other engineered reagents for coronavirus research, including SARS-CoV-2 spike glycoprotein and nucleoprotein antibodies, ACE2 Fc fusion proteins, and anti-human immunoglobulin antibodies for use in diagnostic tests.

Absolute Antibody is also supporting coronavirus research by providing antibody engineering and manufacturing services, such as the production of gram quantities of human antibodies sequenced from recovering COVID patients.

For more information, and a full list of available synthetic nanobodies and engineered antibodies, please visit our website here. About Absolute Antibody, Ltd.

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Under the partnership, the original nanobodies and newly engineered formats are now available to the global research community for use as serological controls and in COVID therapeutic development.

The synthetic nanobodies possess particular promise for the development of inhalable drugs, which could offer a convenient treatment option for the COVID pandemic.

Nanobodies are small antibody fragments that can reach previously inaccessible parts of the body due to their compact size.

Within a two-week timeframe, the lab had identified more than 60 unique anti-RBD sybodies from combinatorial display libraries. Moreover, two of the sybodies can simultaneously bind the RBD, which could enable the construction of a polyvalent antiviral drug.

Absolute Antibody recombinantly produces the SARS-CoV-2 synthetic nanobodies for ensured batch-to-batch reproducibility, high purity and low endotoxin levels.

In addition, Absolute Antibody has used antibody engineering to fuse the nanobodies to Fc domains in different species, isotypes and subtypes.

These recombinant engineered antibodies extend the applications of the sybodies by varying effector function and permitting increased half-life in in vivo studies.

In addition to the new synthetic antibodies, Absolute Antibody offers a variety of other engineered reagents for coronavirus research, including SARS-CoV-2 spike glycoprotein and nucleoprotein antibodies, ACE2 Fc fusion proteins, and anti-human immunoglobulin antibodies for use in diagnostic tests.

Absolute Antibody is also supporting coronavirus research by providing antibody engineering and manufacturing services, such as the production of gram quantities of human antibodies sequenced from recovering COVID patients.

Kinases can access multiple well defined structural states and we are studying how small molecule inhibitors interact with these structures.

The aim for this NIH funded project is to understand the conformational exchange between kinase conformations as well as to understand the inhibitory mechanism of kinase inhibitors.

For this we are using X-ray crystallography, nuclear magnetic resonance spectroscopy NMR , protein engineering and other biophysical methods in collaboration with computational biologists.

The ubiquitin system relies on a highly modular system of enzymes to ligate ubiquitin onto substrate proteins which in many cases leads to the degradation of the substrate protein via the proteasome.

The potential of the ubiquitin system as a therapeutic target is illustrated by the success of the proteasome inhibitor bortezomib in the treatment of multiple myeloma.

We are interested in applying concepts from the field of protein kinase research to the study of ubiquitin conjugating enzymes E2 and ubiquitin ligases E3 with the aim of enabling specific therapeutics.

Our current aim is to study the change in substrate spectra of ubiquitin ligases upon aging in yeast cells. This is work is generously supported by the Ellison Medical Foundation.

Markus Seeliger developed an interest in protein engineering and biophysical chemistry during his diploma research at the Center for Protein Engineering with Alan Fersht and Laura Itzhaki.

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