Methods for analysis of a glucuronide ligand-drug conjugate are provided.

Methods for analysis of a glucuronide ligand-drug conjugate are provided.

Disclosed are pharmaceutical compositions containing saposin C and phosphatidylserine that are useful for treating various cancers.

Disclosed are pharmaceutical compositions containing saposin C and phosphatidylserine that are useful for treating various cancers.

This document relates to methods and materials for detecting premalignant and malignant neoplasms. For example, methods and materials for determining whether or not a stool sample from a mammal contains nucleic acid markers or polypeptide markers of a neoplasm are provided.

This document relates to methods and materials for detecting premalignant and malignant neoplasms. For example, methods and materials for determining whether or not a stool sample from a mammal contains nucleic acid markers or polypeptide markers of a neoplasm are provided.

Disclosed are pharmaceutical compositions containing saposin C and phosphatidylserine that are useful for treating various cancers. Also disclosed are methods for assaying potency of a test composition comprising saposin C and an anionic phospholipid.

Disclosed are pharmaceutical compositions containing saposin C and phosphatidylserine that are useful for treating various cancers. Also disclosed are methods for assaying potency of a test composition comprising saposin C and an anionic phospholipid.

Disclosed is a novel means for accurate qualitative and quantitative analyses for each N-glycosylation site. The method of analyzing N-linked sugar chain(s) of glycoprotein according to the present invention comprises: treating a part of a glycopeptide-containing sample to be analyzed with endo-β-N-acetylglucosaminidases to cleave off sugar chains while leaving one GlcNAc of the chitobiose core on the Asn at the N-glycosylation site; subjecting the obtained sugar chain-cleaved sample to preliminary liquid chromatography/mass spectrometry; predicting the retention time of the glycopeptide of interest and the mass-to-charge ratio (m/z) of the precursor ion in main analysis based on the results of the preliminary liquid chromatography/mass spectrometry; and carrying out the main analysis. By this method, the binding sites and structures of N-linked sugar chains in a glycoprotein can be analyzed. By using the sugar chain-cleaved sample as an internal standard in the main analysis, quantitative analysis of sugar chains at each glycosylation site also becomes possible.

A β-1,6-glucanase mutant which is a mutant of β-1,6-glucanase (EC 3.2.1.75), wherein a Glu residue located at a position corresponding to Glu (E)-321 in SEQ ID NO: 1 is substituted by an amino acid residue X or a Glu (E) residue located at a position corresponding to each of Glu (E)-225 and Glu (E)-321 in SEQ ID NO: 1 is substituted by an amino acid residue X, wherein the amino acid residue (X) is selected from the group consisting of Gln (Q), Gly (G), Ala (A), Leu (L), Tyr (Y), Met (M), Ser (S), Asn (N), and His (H); and a method for measuring β-1,6-glucan, including measuring β-1,6-glucan bonded to the mutant.