Disclosed are a conotoxin polypeptide -CPTx-bt103, a method for preparation thereof, and an application thereof. The conotoxin polypeptide of the present invention consists of 29 amino acids, has a molecular weight of 3141.43 daltons, and has the full sequence RTNCGETCLKDEQCVGACQICVPSQLKCL (SEQ ID NO. 1).

The present invention relates to artificially synthesized modified mono-methylated lysines and modified mono-methylated lysine derivatized polypeptides. The present invention also relates to production of a completely new antibody by using this modified mono-methylated lysine and modified mono-methylated lysine derivatized polypeptide as an antigen, this antibody can be used in recognizing and enriching the modified polypeptide after the lysine mono-methylated polypeptide being derivatized in vitro. By using this antibody, it is capable of detecting whether a mono-methylation modification is present in amino acids on the polypeptide sequence, the present invention also relates to a preparation method of said antibody. Moreover, the present invention also relates to a method for identifying and quantifying the lysine mono-methylated modified substrate in cell or tissue; more specifically, it belongs to identifying and quantifying the lysine mono-methylated modified substrate in cell or tissue by using proteomics approach of affinity enrichment for specific antibody and mass spectrometry.

The present disclosure describes analog conotoxin peptides of the -contoxin peptide RgIA. These analog conotoxin peptides block the 910 subtype of the nicotinic acetylcholine receptor (nAChR) and can be used for treating pain, inflammatory conditions, inflammation, and/or cancer.

Disclosed are a conotoxin polypeptide -CPTx-bt104, a method for preparation thereof, and an application thereof. The conotoxin polypeptide of the present invention consists of 11 amino acids, has a molecular weight of 1313.47 daltons, and has the full sequence SLCCPEDRWCC (SEQ. ID NO. 1).

The present invention relates to transgenic ornamental fish, as well as methods of making such fish by in vitro fertilization techniques. Also disclosed are methods of establishing a population of such transgenic fish and methods of providing them to the ornamental fish industry for the purpose of marketing.

The present invention relates to novel peptide antagonists that inhibit binding of acetylcholine to the active site of the muscle-type nicotinic acetylcholine receptor. The peptide antagonists of the invention are useful in cosmetic compositions that prevent or improve the appearance of skin wrinkles and related skin conditions. The invention further relates to cosmetic and pharmaceutical compositions comprising a peptide antagonist of the invention, and methods for their use.

Provided herein are methods for selecting a population of cells expressing a target polypeptide. In some aspects, the disclosure provides methods for sorting and selecting populations of transfected host cells based on their early expression of a selectable polypeptide. In certain embodiments, the sorting is performed using fluorescence-activated cell sorting or magnetic-activated cell sorting based on the selectable polypeptide. Such selection methods can be further utilized to generate clonal populations of producer cells, e.g. for large-scale manufacturing of a target polypeptide of interest.

Materials and methods for prevention of biofouling that incorporate the presence of a conotoxin peptide on a surface are described. The conotoxin peptide is either directly or indirectly adhered to the surface and interferes with the ability of biofouling organisms to settle on the surface.

The present invention relates to peptides of SEQ ID NO: 27 and peptidomimetics thereof and to their use as antimicrobial and anticancer agents. Said peptides being based on the heavy chain (HC) of a centrocin from the sea urchin Echinus esculentus.

Mussels strongly adhere to a variety of surfaces by secreting byssal threads that contain mussel foot proteins (Mfps). Recombinant production of Mfps presents an attractive route for preparing advanced adhesive materials. Using synthetic biology strategies, Mfp5 together with Mfp5 oligomers containing two or three consecutive, covalently-linked Mfp5 sequences (named Mfp5.sup.2 and Mfp5.sup.3) were synthesized. Positive correlations were found between Mfp5 molecular weight and underwater adhesive properties, including adhesion force, adhesion work, protein layer thickness, and recovery distance. Dopa-modified Mfp5.sup.3 displayed a high adhesion force (20136 nN m.sup.1) and a high adhesion work (6821 fJ m.sup.1) for 200 s cure times, higher than previously reported Mfp-mimetic adhesives. Results disclosed herein highlight the power of synthetic biology in producing biocompatible and highly adhesive Mfp-based materials.