Patents
Literature
Patsnap Eureka AI that helps you search prior art, draft patents, and assess FTO risks, powered by patent and scientific literature data.

6 results about "Polyhistidine-tag" patented technology

A polyhistidine-tag is an amino acid motif in proteins that typically consists of at least six histidine (His) residues, often at the N- or C-terminus of the protein. It is also known as hexa histidine-tag, 6xHis-tag, His6 tag, by the US trademarked name HIS TAG (US Trademark serial number 74242707), and most commonly as His-Tag. The tag was invented by Roche, although the use of histidines and its vectors are distributed by Qiagen. Various purification kits for histidine-tagged proteins are available from Qiagen, Sigma, Thermo Scientific, GE Healthcare, Macherey-Nagel, Cube Biotech, Clontech, Bio-Rad, and others.

High-affinity monoclonal antibodies against His-tags attached to the C-terminus of membrane proteins

To provide a high-affinity monoclonal antibody for a His-tag added to the C terminus of membrane protein.SOLUTION: The present invention provides a monoclonal antibody for a histidine tag (His-tag) or an antigen-binding fragment thereof, wherein the monoclonal antibody recognizes, as an epitope, a His-tag added to the C terminus of a membrane protein.SELECTED DRAWING: None
Owner:CHIBA UNIV

His-tagged diversity nucleic acid aptamer and use thereof

PendingCN122104717APeptide preparation methodsBiological testingAptamerPolyhistidine-tag
The application discloses a histidine tag diversity nucleic acid aptamer and application thereof, and belongs to the technical field of biological processing. The nucleotide sequence of the histidine tag diversity nucleic acid aptamer is shown in SEQ ID NO. 3, or SEQ ID NO. 4, or SEQ ID NO. 5, or SEQ ID NO. 6. The application also discloses an application of the histidine tag diversity nucleic acid aptamer in preparation of a biosensor element for targeted recognition of a histidine tag-containing protein or polypeptide. The application also discloses an application of the histidine tag diversity nucleic acid aptamer in qualitative analysis, quantitative detection and separation and purification of the histidine tag-containing protein or polypeptide. The histidine tag diversity nucleic acid aptamer is obtained by taking HisA1-T63 aptamer as an initial chain, preliminarily improving the aptamer through sequence truncation, and repositioning a functional module to a loop region for diversity modification, thereby expanding the structural diversity of the histidine tag nucleic acid aptamer.
Owner:OCEAN UNIV OF CHINA

Metal ion-driven melittin nanoassemblies, methods of making and use thereof

PendingCN122127485ABiocideNanomedicineBiotechnologyXanthomonas campestris
This invention discloses a metal ion-driven meliosteum peptide nanoassembly, its preparation method, and its applications, relating to the field of agricultural biotechnology. The meliosteum peptide nanoassembly is formed by the self-assembly of a hexahistidine-tagged meliosteum peptide with divalent metal ions through coordination. The average particle size of the meliosteum peptide nanoassembly is 20 nm–30 nm. The meliosteum peptide nanoassembly obtained by this invention through the self-assembly of a hexahistidine-tagged meliosteum peptide with zinc ions exhibits excellent antibacterial, anti-biofilm activity, stability, and biocompatibility, and can be used to control plant bacterial diseases caused by Xanthomonas and other fungi.
Owner:GUIZHOU UNIV

A method for expressing BirA enzyme in prokaryotic escherichia coli and purifying the same

The application discloses a method for expressing BirA enzyme by using prokaryotic Escherichia coli and purifying the BirA enzyme, and relates to the technical fields of genetic engineering and protein engineering. A recombinant expression vector for expressing the BirA enzyme is a pET-28A-BirA plasmid which is constructed by inserting a BirA enzyme coding gene into a multiple cloning site of a pET-28A vector. An 8× histidine tag coding nucleotide sequence is fused to a C terminal of the BirA enzyme coding gene. The nucleotide sequence of the BirA enzyme coding gene is shown as SEQ ID NO:1. The prokaryotic expression system is simple in culture condition, short in cycle, and low in cost, and is suitable for large-scale preparation. The 8× histidine tag is introduced into the C terminal of the BirA enzyme gene, so that the expression product can be purified by one-step nickel column affinity chromatography, and the purification process is simple and high in efficiency.
Owner:CHONGQING MEDICAL UNIVERSITY

Polypeptides and compositions for oral administration and methods of use thereof

PCT designated stageWO2026112546A2Peptide/protein ingredientsAntipyreticOral medicationCaplacizumab
Disclosed herein are compositions and constructs related to a polypeptide, PT-X'n-PTA-Hm (1 ), or pharmaceutically acceptable salts thereof, wherein PT is a peptide transport or fragment thereof; X'n is linker comprising a triazole moiety, n = 0 or 1; PTA is a peptide therapeutic agent selected from the group consisting of a modified semaglutide, a modified tirzepatide, caplacizumab, ozoralizumab; and Hm is a histidine tag where m is 0 to 6; as well as uses thereof.
Owner:IMAGINE PHARMA LLC

Soluble recombinant human podoplanin receptor

PendingCN122295119ADiseaseThreonine
This article discloses a material composition and a method for using the composition to treat... For example Methods for treating cancer or inflammatory joint diseases. The composition is a soluble recombinant human flatfoot protein receptor (srhPDPN) comprising a first amino acid sequence at least 95% homologous to SEQ ID NO:1. The srhPDPN may comprise a tag peptide or polypeptide (such as a multihistidine tag) fused to the first amino acid sequence. The srhPDPN may comprise a signal peptide fused to the first amino acid sequence. The signal peptide may comprise an amino acid sequence at least 95% homologous to SEQ ID NO:2. Multiple threonine residues of the srhPDPN may be partially glycosylated with sialic acid, and in some embodiments, 17 threonine residues of the srhPDPN are partially glycosylated with sialic acid. Treatment may include allowing the composition to act as a decoy receptor or ligand trap to inhibit PDPN signaling.
Owner:SAINTERI CO LTD