8 results about "SAA protein" patented technology

This invention belongs to the field of biodetection technology, specifically relating to a monoclonal antibody combination capable of simultaneously recognizing equine and feline serum amyloid A (SAA) and its application. The monoclonal antibody combination comprises 6E10 and 5A6. The CDR sequences of the heavy and light chain variable regions of 6E10 are shown in SEQ ID NO. 1-6, and the CDR sequences of the heavy and light chain variable regions of 5A6 are shown in SEQ ID NO. 7-12. This antibody combination can highly specifically recognize and bind to recombinant equine and feline SAA proteins, achieving multiple uses with a single antibody and reducing raw material development and production costs. The colloidal gold test strip constructed based on this combination exhibits high specificity, high sensitivity, and a wide detection range, with no cross-reactivity. It is easy to operate and requires no complex instruments, providing a stable and reliable biorecognition tool for assessing and monitoring inflammation-related physiological states in animals.

The invention relates to a characteristic peptide fragment group for SAA protein valuing and application of the characteristic peptide fragment group. The characteristic peptide fragment group comprises a sequence 1, a sequence 1 of an I site connected isotope, a sequence 2 and a sequence 2 of an F site connected isotope, the amino acid sequence of the sequence 1 comprises a sequence as shown in SEQ ID NO.1, and the amino acid sequence of the sequence 2 comprises a sequence as shown in SEQ ID NO.2. According to the method, the isotope labeled characteristic peptide fragment is introduced as an internal standard, so that the loss in the sample treatment process and the signal fluctuation in the mass spectrometric detection process are effectively corrected, and the influence of a matrix effect on a quantitative result is overcome, so that the quantitative accuracy of the SAA protein is remarkably improved.

The present application relates to a kind of novel protein and its application specially combined with small molecule HBC620 and induced its fluorescence enhancement.The amino acid sequence of the protein is as shown in SEQ ID NO:1.The protein obtained in the present application can effectively reduce the non-specific binding with other structure similar small molecules due to the directional design of binding pocket around HBC620, thereby reducing the background fluorescence interference, improving detection accuracy and system stability.

The present disclosure is based on the surprising and unexpected discovery that a ligand molecule with certain characteristics is able to bind to two protein molecules simultaneously and recruit them to form a transient or stable protein-protein interaction complex. The protein-protein interaction and other cross-domain interactions gained in this process contribute additional stabilization energy to the complex beyond the combination of the binary binding energies, and therefore, largely increase the binding potency of the ligand. Accordingly, the present disclosure provides a Protein-Protein Interaction Inducing Technology (PPIIT), which includes a method to design and identify the tripartite or bifunctional compounds and use such compounds to induce protein-protein interactions in various contexts. The present disclosure also provides a composition for the purpose of inducing protein-protein interactions.

Provided are a method for dissolving a poorly water-soluble protein, and a molded article produced using a protein solution obtained thereby. The present invention is a method for dissolving a poorly water-soluble protein, the method comprising a step for mixing a hydroxyl group-containing polymer, a poorly water-soluble protein, and an ionic liquid. In addition, the present invention makes it possible to produce a molded article using the poorly water-soluble protein solution obtained by the method.

This invention discloses a recombinant serum amyloid A (r) protein from the Pacific oyster. Cg SAA), preparation method and application, r Cg The SAA amino acid sequence is shown in SEQ ID NO. 1; the preparation method is to use primers P1 and P2 to... Cg The SAA coding region fragment was amplified by PCR, and the DNA sequences of primers P1 and P2 are shown in SEQ ID NO. 2 and SEQ ID NO. 3, respectively. The PCR amplification product was then mixed with the pET-30a vector via... Bam HI and Xhol After digestion with enzyme I, ligation was performed using T4 ligase, followed by transformation to construct recombinants; the recombinants were then transformed into *E. coli*. Transetta In the (DE3) expression strain, the expression strain was then cultured and IPTG was added to induce expression, followed by purification and refolding to obtain r. Cg SAA protein. The prepared r Cg SAA inhibits the growth of Vibrio splenti and Vibrio anguillarum under non-acidic conditions, and can also kill Vibrio splenti. It can be used to prepare drugs against Vibrio splenti and Vibrio anguillarum, and can be applied directly, effectively and safely to aquaculture.

The application provides a SAA recombinant protein and a preparation method and application thereof, and the preparation method comprises the following steps: S10, constructing a recombinant plasmid: a gene sequence of an amino acid sequence shown in SEQ ID NO: 1 or a nucleotide sequence corresponding to an amino acid sequence shown in SEQ ID NO: 2 is inserted into a pET-28a(+) plasmid which is double-digested by NdeI and XhoI after being double-digested by NdeI and XhoI, so that a recombinant plasmid is obtained; S20, transforming and culturing the recombinant plasmid; S30, protein expression and purification. The application solves the technical problem that the stability of the currently recombinantly expressed SAA protein in vitro is poor, and achieves the technical effect of improving the stability of the SAA recombinant protein in vitro.

The invention relates to a serum amyloid A (SAA) protein mutant and a preparation method thereof. Specifically, the serum amyloid A protein mutant contains core amino acids selected from the following groups: (a) the first amino acid is A or G; (b) the fifth amino acid is A or G; and / or (c) the 8th amino acid is A; wherein the amino acid position number is based on the sequence represented by any one of SEQ ID NO: 1 and SEQ ID NO: 69 to SEQ ID NO: 73. According to the method, the yield of SAA protein is increased, the problem of endotoxin is avoided, and the difference of folding modes or immunogenicity when other systems are used for expressing protein is avoided.