This application relates to methods of quantifying AKT1 and AKT2 and determining AKT1 and AKT2 phosphorylation status. The disclosed methods allow for selection of cancer therapy.

Provided is a linker element and a method of using the linker element to construct a sequencing library, wherein the linker element consists of a linker A and a linker B, the linker A is obtained through the complementary pairing of a long nucleic acid strand and a short nucleic acid strand, the 5′ end of the long strand has a phosphoric acid modification, and the 3′ end of the short strand has an enclosed modification, with enzyme sites in the short strand; and the linker B is a nucleic acid single strand, and the 3′ end thereof can be in a complementary pairing with the 5′ end of the long strand of the linker A. Using the linker element of the present invention for constructing a sequencing library ensures the linking directionality of the linkers while solving the problems of fragment interlinking, linker self-linking and low linking efficiency, and reducing the purification reaction between steps, shortening the linking time and reducing costs.

A method evaluates a quality of a dephosphorylation reagent, the method including the steps of: providing a dephosphorylation reagent containing an alkaline phosphatase and a peptide fragment derived from the alkaline phosphatase; and evaluating the dephosphorylation reagent as having a high quality if a content ratio of the peptide fragment to the alkaline phosphatase is a predetermined reference value or less.

There is provided a protein stabilizer containing a compound represented by Formula (1) as an active ingredient. The protein stabilizer is capable of stabilizing a protein in a solution state for a long period of time without affecting an assay system, the protein being not limited to enzymes, labeling substances such as fluorescent substances and chemiluminescent substances, and assay target substances. There is also provided a protein stabilization method containing making the protein coexist with the compound represented by Formula (1) in a water-containing solution.

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In Formula (1), X is a hydrogen atom or a methyl group, and n is an integer of 3 to 17.

A bone delivery conjugate having a structure selected from the group consisting of: A) X-D.sub.n-Y-protein-Z; and B) Z-protein-Y-D.sub.n-X, wherein X is absent or is an amino acid sequence of at least one amino acid; Y is absent or is an amino acid sequence of at least one amino acid; Z is absent or is an amino acid sequence of at least one amino acid; and D.sub.n is a poly aspartate wherein n=10 to 16. Compositions comprising same and methods of use thereof.

Related to is the field of nucleic acid testing, and in particular, a test kit or a method for testing a target nucleic acid in a sample. The test kit comprises therein a hybridization solution, which contains therein a non-ionic surfactant, a cationic polymer, and a buffer solution having a pH value in the range from 6.5 to 8.5. The test kit can further comprise therein a Tris-HCl color developing solution having a pH value in the range from 9.0 to 10.0 and containing a C.sub.8-C.sub.18 alkylglucoside. Testing target nucleic acid in a sample using the test kit has the advantages of short time consumption, easy operation, high throughput, and low costs.

The invention concerns the use of bacterial ghosts as carrier and targeting vehicles for active substances.

This invention relates generally to a therapeutic use of alkaline phosphatase to modulate gastrointestinal tract flora levels in subject.

A composition contains an alkaline phosphatase and first to sixth peptide fragments, wherein content ratios of the first to sixth peptide fragments to the alkaline phosphatase satisfy formulas (1) to (6), respectively: (X.sub.1/Y)×100≤0.6000 (1); (X.sub.2/Y)×100≤0.1800 (2); (X.sub.3/Y)×100≤0.2000 (3); (X.sub.4/Y)×100≤0.8000 (4); (X.sub.5/Y)×100≤1.6000 (5); and (X.sub.6/Y)×100≤0.3500 (6), wherein X.sub.1 to X.sub.6 represent peak area values of the first to sixth peptide fragments calculated by an automatic integration method from an extracted ion chromatogram obtained by an LC-MS/MS analysis of the composition, respectively, and Y represents a peak area value of the alkaline phosphatase calculated by an automatic integration method from a chromatogram obtained by an LC-UV analysis of the composition.

A chimeric signal peptide for protein expression includes an N-region, a hydrophobic region, and a C-region, wherein the N-region and the C-region are from a same signal peptide of a first protein and the hydrophobic region is from a signal peptide of a second protein, wherein the first protein is different from the second protein. The first and second protein are independently selected from the group consisting of BM40, IL2, HA, Insulin, CD33, IFNA2, IgGK leader, AZU, and SEAP.