Bayer Aktiengesellschaft

Basf Agricultural Solutions Seed US LLC

Icon Genetics Gmbh

Bayer Pharma Aktiengesellschaft

Ernst Weber

Nikolaus Pawlowski

Jan Tebbe

Fabien Poree

Bernd Laber

Michael Strerath

Gudrun Lange

Manuel Dubald

Marc Linka

Wayne Coco

Dorian Schönfeld

Nina Wobst

Katharina Filarsky

Christina Thies

Sandra Geske

Philipp Ellinger

Heike Balven-Ross

Beatrix Stelte-Ludwig

Ingo Flamme

Sylvestre Marillonnet

Simone Greven

Christoph Mahlert

Uwe Gritzan

Stefan Werner

Sandra Berndt

Christian Votsmeier

Mark Trautwein

Carola Engler

Karoline Dröbner

Andreas Wilmen

Winfried Wunderlich

Antje Schmidt

Kenneth Young

Yalda Sedaghat

Fionnuala Mary Mcaleese Eser

Patrick Jones

Frank Wunder

Hans-Georg Lerchen

Stefan Heitmeier

Anne-Sophie Rebstock

Yolanda Cancho Grande

Tobias Marquardt

Sven Wittrock

Lisa Dietz

Thomas Mondritzki

Damian Brockschnieder

Stephan Märsch

Romy Kandzia

Frank Thieme

Hannah Jörißen

Stefanie Hammer

Julian Marius Glück

Oliver Von Ahsen

Sabine Hoff

Matyas Gorjanacz

Ilka Mathar

Helge Roider

Wiebke Maria Nadler

Su-Yi Tseng

Lucas Hudson Hofmeister

Joerg Meding

Pedro Paz

Phaik Lyn Oh

Florian Sohler

Anke Mayer-bartschmid

Stuart Walsh

Marcel Geertz

Claudia Noack

Julian Marius Glueck

Hannah Jörissen

Christoph Thiel

Ramona Grutzner

Cindy Schulenburg

Julia Glunz

Melanie Fischer

Jenny Fitting

Christian Bertling

Pascale Buchmann

Ramona Gruetzner

The present disclosure relates to an isolated antibody or antigen-binding fragment thereof that binds to human Semaphorin 3A (Sema3A). An antibody conjugate and a pharmaceutical composition each comprising the isolated antibody or antigen-binding fragment thereof that binds to human Sema3A are also provided.

Anti-semaphorin 3A antibodies

The present invention relates to an antibody or a fragment thereof comprising at least one heterologous amino acid sequence incorporated within at least one CDR region of said antibody or fragment thereof, wherein said at least one heterologous amino acid sequence comprises an N-terminal linker sequence (Nils), an Atrial Natriuretic Peptide (ANP) and a C-terminal linker sequence (Ctls). Optionally, at least a portion of said at least one CDR region is replaced by said at least one heterologous amino acid sequence incorporated therein. The present invention further relates to such antibody or fragment thereof for use in a method for treatment, a composition comprising such antibody or fragment thereof, a nucleic acid or a mixture of nucleic acids encoding such antibody or fragment thereof, a host cell comprising such nucleic acid or such mixture of nucleic acids and to a process for producing such antibody or fragment thereof.

Atrial natriuretic peptide engrafted antibodies

The present invention relates to an isolated antibody or antigen-binding fragment thereof that binds to human A2AP. The isolated antibody or antigen-binding fragment according to the present invention i) cross-reacts with rabbit and/or cynomolgus A2AP, ii) does not inhibit human plasmin activity, and iii) increases plasmin mediated clot lysis in the presence of A2AP.

Anti-A2AP antibodies and uses thereof

The present disclosure relates to an isolated antibody or antigen-binding fragment thereof that binds to human Sema3A. The isolated antibody or antigen-binding fragment according to the present disclosure i) binds to human Sema3A of the sequence of SEQ ID NO: 600 with a dissociation constant (KD)≤50 nM, ≤20 nM, ≤10 nM, ≤1 nM, or ≤0.1 nM; ii) cross-reacts with mouse, cynomolgus, rat, pig and/or dog Sema3A, particularly wherein said isolated antibody or antigen-binding fragment thereof binds to mouse, cynomolgus, rat, pig and/or dog Sema3A with a dissociation constant (KD)≤50 nM, ≤20 nM, ≤10 nM, ≤1 nM, or ≤0.1 nM; iii) binds to human Sema3A of the sequence of SEQ ID NO: 600 with a binding activity as measured by surface plasmon resonance (SPR) of ≥60%, ≥70%, ≥80%, or ≥90%; iv) inhibits the activity of human Sema3A of the sequence of SEQ ID NO: 600 in an in vitro mesangial cell migration assay with an EC50 of ≤10 nM, ≤5 nM, ≤2.5 nM, or ≤1 nM; v) inhibits the activity of human Sema3A of the sequence of SEQ ID NO: 600 in an in vitro growth cone collapse assay with an EC50 of ≤50 nM, ≤25 nM, ≤10 nM, or ≤5 nM; vi) inhibits the activity of human Sema3A of the sequence of SEQ ID NO: 600 in an in vitro HUVEC repulsion assay with an EC50 of ≤1 nM, or ≤0.3 nM, ≤0.1 nM, ≤0.07 nM, ≤0.06 nM and/or vii) exhibits an increased potency against cellular Sema3A, of the sequence of SEQ ID NO: 600, induced HUVEC repulsion.

Anti-sema3a antibodies and uses thereof

The present invention relates to tools and methods for the generation of antibodies which specifically bind chemokine receptors, such as CC or CXC chemokine receptors. Provided are isolated sulfated polypeptides and conjugates thereof, which can be used for example as antigens or for off target panning to facilitate the generation of anti-human, anti-, and/or anti-mouse chemokine receptor antibodies, e.g. for the generation of antibodies with fully human CDRs and/or other favorable properties for therapeutic use. The present invention furthermore relates to antibodies and conjugates thereof which can be obtained by applying the aforementioned tools and methods. Provided are antibodies specifically binding to human,and/or murine CCR8 with favorable properties for therapeutic use, such as cross-reactive antibodies, fully human antibodies, low internalizing (including non-internalizing) antibodies, and antibodies efficiently inducing ADCC and/or ADCP in Treg cells.

Methods of treatment using CCR8 antibodies

System for producing a nucleic acid construct of interest, said system comprising:

System and method of modular cloning

In the present invention, HPPD polypeptides and plants containing them showing a full tolerance against one or more HPPD inhibitor herbicides belonging to various chemical classes are described. A set of mutant HPPD polypeptides have been designed which have either no or only a significantly reduced affinity to HPPD inhibitor herbicides and, at the same time, the rate of dissociation of the HPPD inhibitors of the mutant HPPD polypeptide is increased to such an extent that the HPPD inhibitors no longer act as slow-binding or slow, tight-binding inhibitors but, instead of this, have become fully reversible inhibitors. In particular, isolated polynucleotides encoding mutant HPPD polypeptides conferring tolerance to HPPD inhibitor herbicides belonging to various chemical classes are provided. Additionally, amino acid sequences corresponding to the polynucleotides are encompassed.

HPPD variants and methods of use

Bispecific antibodies binding ALK-1 and BMPR-2 The present invention relates to bispecific antibodies binding human ALK-1 and human BMPR-2. Also provided are BsABs which are agonists of ALK-1/BMPR-2 signaling, and BsABs which do not trigger osteogenic signaling. Furthermore, the invention relates to pharmaceutical uses of the BsABs, in particular for the treatment of pulmonary hypertension. Also provided are methods to screen for BsABs for use in the therapy, e.g. of pulmonary hypertension.

Bispecific antibodies binding ALK-1 and BMPR-2

The present application relates to novel binder drug conjugates (ADCs), to active metabolites of these ADCs, to processes for preparing these ADCs, to the use of these ADCs for the treatment and/or prophylaxis of diseases and to the use of these ADCs for preparing medicaments for treatment and/or prophylaxis of diseases, in particular hyperproliferative and/or angiogenic disorders such as, for example, cancer diseases. Such treatments can be effected as monotherapy or else in combination with other medicaments or further therapeutic measures.

Antibody drug conjugates of kinesin spindel protein (KSP) inhibitors with antiB7H3-antibodies

A process of inserting a nucleic acid sequence of interest into an acceptor nucleic acid is provided. The process comprises amplifying by PCR a DNA comprising in the following order a sequence segment U, a nucleic acid sequence segment of known nucleotide sequence K2, and a nucleic acid sequence segment of known sequence K3. The process further comprises treating the linear double-stranded DNA molecules from the PCR amplification with an exonuclease to obtain a single-stranded overhang at the first end of the DNA and a single-stranded overhang comprising nucleic acid segments K2 and K3 at the second end of the DNA. The process additionally comprises annealing the product of the exonuclease treatment to a linearized double-stranded acceptor nucleic acid which has been designed to complement the single-stranded overhangs of the product of the exonuclease treatment.

Process of clean cloning

Growing community of inventors

Langenfeld, Germany

Ernst Weber