200results about "Polypeptide with Strep-tag" patented technology

The present invention provides compositions including peptide display scaffolds that present at least one candidate peptide and at least one detectable moiety in at least one of the N-terminal and C-terminal candidate peptide presenting domains that when expressed in a cell are accessible at a surface of the cell outermembrane. In addition, the present invention also provides kits and methods for screening a library of cells presenting the candidate peptides in peptide display scaffolds to identify a ligand for an enzyme.

The invention discloses a recombinant humanized III type collagen alpha 1 chain and an application thereof. The nucleotide sequence for coding the recombinant humanized III type collagen alpha 1 chainis shown as SEQID NO: 1. The recombinant humanized III type collagen alpha 1 chain sequentially comprises an amino-terminal affinity purification label, a humanized III type collagen mature peptide chain and a carboxy-terminal affinity purification label from an amino terminal. According to the recombinant humanized III type collagen alpha 1 chain disclosed by the embodiment of the invention, a specificity affinity purification label is designed at two ends of the humanized III type collagen mature peptide chain, so that purification of overall-length protein is facilitated, and the recombinant humanized III type collagen alpha 1 chain can also be used for identification of collagen. According to the recombinant humanized III type collagen alpha 1 chain disclosed by the embodiment of theinvention, the III type collagen mature peptide chain is adopted, the propeptide at two ends is removed, and the expression number of the gene without propeptide is far higher than those of the gene containing the propeptide.

The invention relates to mutant forms of the outer membrane-located lipoprotein CsgG, in particular, modifications at one or more of positions Tyr51; Asn55; and Phe56. The invention also relates to analyte detection and characterisation using said mutant CsgG.

The invention provides compositions and methods of identifying, modifying and producing modified target molecules, including therapeutic molecules by modification with non-natural amino acids. Certain aspects of the invention include methods of adding a chemical moiety to a target molecule, and the compositions resulting therefrom. Certain aspects of the invention also relate to kits for identifying, modifying and producing modified target molecules described herein.

The present invention provides compositions including peptide display scaffolds that present at least one candidate peptide and at least one detectable moiety in at least one of the N-terminal and C-terminal candidate peptide presenting domains that when expressed in a cell are accessible at a surface of the cell outermembrane. In addition, the present invention also provides kits and methods for screening a library of cells presenting the candidate peptides in peptide display scaffolds to identify a ligand for an enzyme.

The present invention relates to methods for treating cancers and metastatic diseases by modulating latexin expression and / or latexin activity.

Provided is a method of producing a template DNA used for protein synthesis comprising a step of amplifying a linear double-stranded DNA by polymerase chain reaction (PCR), by using a reaction solution comprising a first double-stranded DNA fragment comprising a sequence coding for a protein or a portion thereof, a second double-stranded DNA fragment comprising a sequence overlapping with the 5′ terminal region of the first DNA fragment, a third double-stranded DNA fragment comprising a sequence overlapping with the 3′ terminal region of the first DNA fragment, a sense primer which anneals with the 5′ terminal region of the second DNA fragment, and an anti-sense primer which anneals with the 3′ terminal region of the third DNA fragment, wherein the second DNA fragment comprises a regulatory sequence for transcription and translation of a gene, and the concentrations of the second DNA fragment and the third DNA fragment in the reaction solution each range from 5 to 2,500 pmol / L. The use of this method enables efficient production of a template DNA for expression and purification of a protein.