Disclosed are P. gingivalis antibodies raised against a chimeric or fusion protein, wherein the chimeric or fusion protein comprises a first peptide joined directly or through a linker to a second peptide or polypeptide, wherein (A) the first peptide comprises a region of a P. gingivalis trypsin-like enzyme and (B) the second peptide or polypeptide comprises an adhesin domain of P. gingivalis.

The present invention relates to compositions, methods, uses and kits for treating cancer. The present invention relates to methods for minimising the progression of cancer in a subject, the method comprising administering to the subject therapeutically effective amounts of chymotrypsinogen and trypsinogen, thereby minimising the progression of cancer in the subject. In particular, the methods provide a means for treating cancer by reducing the number of cancer stem cells in the subject.

The present disclosure pertains to compositions comprising anti-VEGF proteins and methods for producing such compositions.

The present disclosure pertains to compositions comprising anti-VEGF proteins.

The present invention is directed to non-soy oilseed protein products, very low in, or free of, beany, green, vegetable or similar flavour notes and useful for the fortification of food and beverage products and prepared without the use of salt in the process. The non-soy oilseed protein products of the present invention are obtained by extracting non-soy oilseed protein source with water to form an aqueous non-soy oilseed protein solution, at least partially separating the aqueous non-soy oilseed protein solution from residual non-soy oilseed protein source, adjusting the pH of the aqueous non-soy oilseed protein solution to a pH between about 1.5 and a value about 1 pH unit lower than the typical pH of isoelectric precipitation to solubilize the bulk of the protein and form an acidified non-soy oilseed protein solution then separating the acidified non-soy oilseed protein solution from the acid insoluble solid material. The acidified non-soy oilseed protein solution may be dried following optional concentration and diafiltration to form a non-soy oilseed protein product, which may be an isolate. The acid insoluble solid material may be washed with acidified water and then dried to form another non-soy oilseed protein product. These products may be dried at the acidic pH at which they were prepared or may be adjusted in pH before drying.

Proteases are enzymes which hydrolyze protein enzymes, eliminating their activity. The present invention exploits the hydrolyzing activity of proteases including proteinase K, endoproteinase LysC and/or trypsin to control the activity of restriction enzymes and/or eliminate or reduce production of unwanted DNA or RNA fragments (known as star activity).

Provided is a gene for trypsin-like serine protease, a protein encoded thereby and use thereof. The nucleotide sequence of the gene for trypsin-like serine protease is set forth in SEQ ID No. 1, the amino acid sequence of the protein encoded by the gene for trypsin-like serine protease is set forth in SEQ ID No. 2. The protein encoded by the gene provided by the present disclosure is capable of inhibiting P. aeruginosa, A. hydrophila, V. parahaemolyticus and V. harveyi.

The present disclosure pertains to compositions comprising anti-VEGF proteins and methods for producing such compositions.

The invention relates to truncated growth factors and variants thereof. The invention also relates to methods of making and using the truncated growth factors. The invention further relates to compositions including a protease and a growth factor comprising a bone morphogenic protein (BMP) or a variant thereof. The invention also relates to methods of using the composition.

Methods and reagents to obtaining a sample enriched in peptides comprising the third complementarity-determining region of the heavy chain (CDRH3) of immunoglobulins, such as IgGs, are described. These methods are based on the use of targeted protease digestion of immunoglobulins and affinity purification of CDRH3 peptides using specific antibodies. Such methods and reagents are useful for analyzing the immunoglobulin repertoire.