19 results about "Protein A" patented technology

The present application provides an isolated antigen-binding protein, comprising: a first antigen-binding domain and a second antigen-binding domain, wherein the first antigen-binding domain specifically binds to TNF-like protein A (TL1A), and the first antigen binding domain and the second antigen binding domain are different.

This invention generally relates to methods for enriching antibodies of interest. Specifically, this invention relates to enriching therapeutic antibodies from upstream cell culture processes using protein A chromatography in the form of a centrifugal column for product quality property profiling analysis.

The present disclosure relates to a method for improving the quality of glycosylated antibody drug conjugates (DAR distribution, stability, etc.) using activated carbon. Specifically, the present disclosure employs hydrophobic interaction chromatography (HIC) column, protein A chromatography, activated carbon stirring, and buffer exchange, alone or in series, to remove free glycosyltransferases. As a result, the purity of the glycosylated antibody drug conjugates is improved, and the degradation of the antibody drug conjugates is prevented. Ultimately, the drug substance (DS) of OBI-902 (anti-TROP2 antibody drug conjugate) and OBI-904 (anti-Nectin-4 antibody drug conjugate) is further determined.

This invention relates to a high-titer prealbumin antibody purification method and its application, belonging to the field of biotechnology. The method utilizes Protein A affinity chromatography to capture total IgG from antiserum, followed by purification using an affinity chromatography column prepared by targeted conjugation of a specific sequence peptide. The antibody purified by this method achieves a titer of 1:256,000 in ELISA detection, with a half-maximal effective concentration (EC50). 50 The antibody concentration was 3.2 ng / mL, exhibiting extremely high affinity and reactivity. When used in a double-antibody sandwich chemiluminescent immunoassay, it achieved a detection limit of 0.08 µg / mL, a wide dynamic range (0.08–400 µg / mL), and a titer retention rate as high as 88% after accelerated storage at 37°C for 14 days, demonstrating significantly better stability than antibodies prepared by traditional methods. This invention provides a highly active and stable core antibody raw material for the preparation of high-performance immunodiagnostic reagents.

The application discloses a B cell conservative epitope peptide on a porcine Lawsonia intracellularis (LI) self-transcription protein A (LatA) and application of the B cell conservative epitope peptide in LI specific antibody diagnosis. The B cell conservative epitope peptide of the application has a sequence of NGNGNPAN and is named as NN8. The B cell conservative epitope peptide can be expressed on the surface of an inert carrier S9H bacterium in a functional display mode. An NN8-antibody direct mediation agglutination test is established based on the surface display expression of the S9H bacterium, the LI antibody is specifically recognized by the NN8, and there is no cross reaction with serum antibodies of other porcine infectious diseases. Animal test results show that the method can detect specific serum antibodies 7 days after a weakly virulent strain infects and vaccinates Balb / c mice. The diagnosis method has strong specificity, good sensitivity, convenient operation, and the result is directly determined, and is expected to become a technical means for visual on-site precise and convenient diagnosis and vaccine evaluation of LI infection.

The present application relates to a method for preparing an antibody group and an antibody group prepared by the method, which can prepare a high-purity and high-quality desired antibody group by removing impurities without using an expensive protein A column, and in particular, can achieve process automation and greatly reduce production costs.

A CRISPR-Cas-Geminin system that maintains potent on-target editing activity but has reduced off-target editing activity relative to wild-type Cas, and methods of use.

A method for constructing a mouse model for rapid degradation of Myostatin (MSTN) protein is provided. The method includes: inserting sequentially a 5′ homologous arm, 3 X (Glu-Ala-Ala-Ala-Lys) (3xEAAAK), an FK506-binding protein (FKBP1A) gene synonymous mutation sequence, 3xEAAAK, a red fluorescent protein monomeric Cherry (mCherry) sequence and a 3′ homologous arm into a Donor vector backbone to obtain a Donor recombinant vector; designing a Guide Ribonucleic Acid (gRNA) based on a third exon of the Mstn gene; mixing the gRNA, CRISPR-associated protein 9 (Cas9) protein, and the Donor recombinant vector and co-injecting a mixture of the above into mouse fertilized eggs, culturing the fertilized eggs in vitro and transplanting to obtain the F0 generation mice; and hybridizing the F0 generation mice with wild-type mice, or further breeding hybridized offspring to obtain a knock-in mouse model.

This invention provides a sample pretreatment kit and its application for the simultaneous detection of Aβ40, Aβ42, and lencanezumab, belonging to the field of biodetection technology. The kit includes: mixed magnetic beads, internal standard solution, trypsin digestion solution, enzyme digestion enhancer, and ammonia; the mixed magnetic beads are composed of protein A magnetic beads and streptavidin magnetic beads; the internal standard solution is composed of… 15 N-labeled Aβ40, 15 This kit consists of N-labeled Aβ42 and lencanezumab internal standard peptides. The pretreatment kit eliminates the need for anti-IgG1 antibodies, requiring only Protein A for detection, thus shortening sample processing time, greatly simplifying the sample handling process, and increasing throughput. The kit can simultaneously detect Aβ40, Aβ42, and lencanezumab, providing more reliable data support for clinical diagnosis and treatment efficacy evaluation, and significantly promoting the development of companion detection technologies for Alzheimer's disease biomarkers and therapeutic drugs.

The present application belongs to the field of biotechnology and antibody engineering pharmacy, and particularly relates to a single-domain antibody and a preparation method thereof. The present application is based on the key amino acid sites involved in the combination with Protein A, and the amino acids at the key sites of other single-domain antibodies not combined with Protein A are mutated, so that the combination ability of the mutated single-domain antibody with Protein A is significantly improved, and the mutated single-domain antibody can be purified through Protein A filler, and meanwhile the characteristics of the single-domain antibody are not changed.

A nucleic acid construct comprising a first polynucleotide encoding MGAT1 gene or a homologous gene having at least 85% sequence identity thereof, a second polynucleotide encoding MGAT2 gene or a homologous gene having at least 85% sequence identity thereof, and a third polynucleotide encoding MAN2A2 gene or a homologous gene having at least 85% sequence identity thereof. A nucleic acid construct combination comprising a first, a second, and a third nucleic acid constructs, which comprise a first polynucleotide encoding MGAT1 gene or a homologous gene having at least 85% sequence identity thereof, a second polynucleotide encoding MGAT2 gene or a homologous gene having at least 85% sequence identity thereof, and a third polynucleotide encoding MAN2A2 gene or a homologous gene having at least 85% sequence identity thereof respectively. A method of regulating the high mannose glycoform content of a recombinant protein during a mammalian cell culture process is also provided, which comprises an expression of the recombinant protein and an overexpression of three proteins that are involved in an N-glycosylation pathway in a mammalian host cell. A highly effective method for reducing the high mannose glycoform content of recombinant proteins in CHO cells.

This invention discloses an antibody-BPA protein-nucleic acid tag complex, its preparation method, and its applications. This invention combines recombinant protein A-bpa-SNAP-tag with O... 6 The protein-nucleic acid complex is obtained by binding to an oligonucleotide modified with benzylguanine; the protein-nucleic acid complex is then conjugated with an antibody, followed by ultraviolet irradiation to obtain an antibody-BPA protein-nucleic acid tag complex. This invention utilizes the high affinity and specific binding of Protein A in BPA protein to the Fc fragment of immunoglobulin (IgG) to pre-construct the protein-nucleic acid complex; in use, simply mixing the target antibody with this complex achieves targeted, rapid, and universal labeling of the antibody with a nucleic acid tag.

The application discloses monoclonal antibodies of myxovirus resistance protein A and application thereof, and belongs to the technical field of biology. The application provides monoclonal antibodies MxA-1# and MxA-25# of myxovirus resistance protein A, the monoclonal antibody MxA-1# is produced by a hybridoma cell strain with a preservation number of CGMCC No.46772, the amino acid sequence of a light chain variable region is shown as SEQ ID NO.12, and the amino acid sequence of a heavy chain variable region is shown as SEQ ID NO.17; the monoclonal antibody MxA-25# is produced by a hybridoma cell strain with a preservation number of CGMCC No.46774, the amino acid sequence of a light chain variable region is shown as SEQ ID NO.22, and the amino acid sequence of a heavy chain variable region is shown as SEQ ID NO.26. Both the two antibodies have strong binding capacity with the MxA protein, and lay a foundation for preparing a myxovirus resistance protein A detection kit.

This invention provides a protein composition that can enhance the proliferative activity of lentivirus-infected cells and its application. The protein composition includes at least one of protein A, protein B, and protein C; the amino acid sequence of protein A is selected from one of SEQ ID NO: 1-6; the amino acid sequence of protein B is selected from one of SEQ ID NO: 7-11; and the amino acid sequence of protein C is selected from one of SEQ ID NO: 12-13. By synthesizing a nucleic acid molecule encoding the protein composition provided by this invention, integrating it into a recombinant vector, and transfecting cells using a lentivirus transfection system, the lentivirus-infected cells can express the above-mentioned protein composition, thereby enhancing the proliferative activity of lentivirus-infected cells, reducing the risk of mass cell death after lentivirus infection, and allowing lentivirus-infected cells to survive well after a period of culture, thus improving the infection efficiency of lentivirus on cells.

The present invention relates to methods for isolating a product and / or reducing impurities such as Host Cell Proteins (HCP), aggregates and residual Protein A (rPA) from a load fluid comprising a FC-containing proteins. 5

This invention relates to a humanized Helicobacter pylori cytotoxin-associated protein A monoclonal antibody and its application. The humanized Helicobacter pylori cytotoxin-associated protein A monoclonal antibody includes a heavy chain variable region and a light chain variable region. The nucleic acid sequence of the heavy chain variable region includes CDR1 shown in SEQ ID No. 1 or SEQ ID No. 2, CDR2 shown in SEQ ID No. 3 or SEQ ID No. 4, and CDR3 shown in SEQ ID No. 5 or SEQ ID No. 6. The nucleic acid sequence of the light chain variable region includes CDR1 shown in SEQ ID No. 7 or SEQ ID No. 8, CDR2 with the sequence LVS or KVS, and CDR3 shown in SEQ ID No. 9 or SEQ ID No. 10.

This invention discloses an immunochromatographic assay kit, preparation method, and application for the detection of apolipoprotein E4. The kit includes a test card and sample diluent. The test card comprises a test strip, which includes a PVC base, absorbent paper, a glass fiber pad, and a nitrocellulose membrane. The glass fiber pad is loaded with polystyrene latex microspheres for physical adsorption. The surface of the polystyrene latex microspheres is modified with sulfonyl or hydroxyl groups, and the zeta potential ranges from -15V to -20V. After the polystyrene latex microspheres are uniformly coated on a glass slide and dried, the contact angle between them and water droplets is greater than 90°. The nitrocellulose membrane is loaded with anti-APOE4 antibody, coating solution, and protein A. The sample diluent includes PBS, TWEEN-20, Tetronic 1307, and CHAPS. This invention eliminates the need for monoclonal antibody-labeled latex microspheres, reducing false positives and reagent batch-to-batch variation, and achieving higher sensitivity.

A method for producing a cyclic peptide, comprising: (i) providing a denatured cyanylated peptide of the formula H2N–(Ai)–(A1)n–(Ad)–(Ac)–(A2)m–COOH in solution, wherein Ai is a terminal amino acid bearing the terminal NH2 group; (A1)n is a peptide linkage containing n independently selected A1 amino acid residues connected to each other by amide bonds, wherein n is 1-28; Ac is a single cysteine with its thiol (SH) group derivatized as a thiocyanide (SCN) group; Ad is an amino acid directly attached to Ac; and (A2)m is a peptide linkage containing m independently selected A2 amino acid residues connected to each other by amide bonds, wherein m is at least 3; (ii) exposing the denatured cyanylated peptide produced in step (i) to a pH in a range of 8-10 to elicit an intramolecular cyanylation- aminolysis reaction between the terminal NH2 group and Ad to produce the cyclic peptide.