An object of the present invention is to provide a novel plant growth inhibiting agent and a plant growth inhibiting method using the same. The plant growth inhibiting agent of the present invention comprises, as an active ingredient, a compound represented by the following formula (I′) and/or a salt thereof. In the formula (I′), R.sup.1a represents a substituted or unsubstituted C.sub.1 to C.sub.20 alkyl group, a substituted or unsubstituted C.sub.6 to C.sub.14 aryl group, a substituted or unsubstituted C.sub.3 to C.sub.13 heteroaryl group, or the like; R.sup.2 represents a substituted or unsubstituted C.sub.1 to C.sub.20 alkylene group, a substituted or unsubstituted C.sub.6 to C.sub.14 arylene group, or the like; R.sup.3a represents OH, a substituted or unsubstituted C.sub.1 to C.sub.6 alkoxy group, or the like; X represents an oxygen atom; Y represents a substituent; q represents any integer of 0 to 3; n represents 0 or 1; and m represents 0 or 1.

##STR00001##

The present invention provides among other things a composition of a polymeric reagent and an antioxidant, such as butylated hydroxyl toluene.

The present invention provides among other things a composition of a polymeric reagent and an antioxidant, such as butylated hydroxyl toluene.

In various embodiments methods are provided for identifying and/or quantifying one or more antigens of interest (biomarkers) on the surface of cell- or tissue-specific exosomes. In an illustrative embodiments the methods comprise: i) incubating a population of exosomes with one or more tissue-specific antibodies that bind an antigen specific to a tissue or cell type of interest that produces exosomes, where the tissue specific antibodies are attached to acceptor bead or magnetic beads so the antibodies bind exosomes displaying the antigen; ii) obtaining a purified population of exosomes bound by the tissue specific antibodies with and/or without photocleavable linker based technology; iii) incubating a test subset of the isolated tissue-specific exosomes with acceptor beads attached to test antibodies that bind an antigen of interest thereby binding exosomes that display the antigen of interest and a control subset with negative control acceptor beads; v) incubating the test subset of isolated exosomes and the control subset of exosomes with a donor-bearing antibody that binds an exosome specific antigen; and vi) detecting a signal produced upon illumination of the control subset and/or the test; and vii) detecting the antigen(s) of interest.

In various embodiments methods are provided for identifying and/or quantifying one or more antigens of interest (biomarkers) on the surface of cell- or tissue-specific exosomes. In an illustrative embodiments the methods comprise: i) incubating a population of exosomes with one or more tissue-specific antibodies that bind an antigen specific to a tissue or cell type of interest that produces exosomes, where the tissue specific antibodies are attached to acceptor bead or magnetic beads so the antibodies bind exosomes displaying the antigen; ii) obtaining a purified population of exosomes bound by the tissue specific antibodies with and/or without photocleavable linker based technology; iii) incubating a test subset of the isolated tissue-specific exosomes with acceptor beads attached to test antibodies that bind an antigen of interest thereby binding exosomes that display the antigen of interest and a control subset with negative control acceptor beads; v) incubating the test subset of isolated exosomes and the control subset of exosomes with a donor-bearing antibody that binds an exosome specific antigen; and vi) detecting a signal produced upon illumination of the control subset and/or the test; and vii) detecting the antigen(s) of interest.

Fluorescence quenching nitrodiarylethene analogs are useful in oligonucleotide conjugates and probes. These analogs, whose absorption spectra are substantially blue-shifted relatively to emission spectra of common fluorophores (such as fluorescein), do not need to rely on spectral overlap of quencher absorbance and fluorophore's emission for their quenching abilities. The oligonucleotide-quencher conjugates may be used in detection methods for nucleic acid targets.

Fluorescence quenching nitrodiarylethene analogs are useful in oligonucleotide conjugates and probes. These analogs, whose absorption spectra are substantially blue-shifted relatively to emission spectra of common fluorophores (such as fluorescein), do not need to rely on spectral overlap of quencher absorbance and fluorophore's emission for their quenching abilities. The oligonucleotide-quencher conjugates may be used in detection methods for nucleic acid targets.

Lactamium based ionic liquids are described. They comprise at least one of: the reaction product of a lactam compound having a formula (IV) ##STR00001## wherein n is 1, 2 or 4 to 8, and a Brøsted acid HX; or a Brøsted acid HX, where X is a halide, and a metal halide; where the reaction product is p-toluenesulfonate, halide, or the halometallate; or the reaction product of a lactam compound having a formula (V) ##STR00002## wherein the ring has at least C—C one double bond, and n is 1 to 8, and a Brøsted acid HX; or a Brøsted acid HX, where X is a halide, and a metal halide; or the reaction product of a lactam compound having a formula (VI) ##STR00003## wherein n is 1 to 8, m is 1 to 8, and the rings can be saturated or unsaturated; and a Brøsted acid HX; or a Brøsted acid HX, where X is a halide, and a metal halide.

This disclosure relates to trans-cyclooctene compounds and methods of using the same in bioorthogonal labeling experiments.

A method for producing a purified peptide from a supported crude peptide having a support and a first peptide chain bonded to the support at the C-terminus. The method includes: introducing a linker and a hydrophilic unit to an amino group of the first peptide chain of the supported crude peptide; cleaving a bond between the first peptide chain and the support before or after at least one of the linker and the hydrophilic unit is introduced to the amino group of the first peptide chain such that a support-free hydrophilized peptide is obtained; treating the support-free hydrophilized peptide by liquid chromatography; and cleaving a bond between the linker and the first peptide chain in the support-free hydrophilized peptide by chemical treatment after the liquid chromatography treatment such that a peptide including the first peptide chain is obtained.