Provided is a near-infrared-absorbing dye increasing a visible light transmittance and having a near-infrared blocking characteristic. The near-infrared-absorbing dye has an absorption characteristic measured by dissolving the dye in dichloromethane satisfying the following requirements. In an absorption spectrum at a wavelength of 400 to 800 nm, there is a maximum absorption wavelength .sub.max in a wavelength region of 670 nm or more. The following relational expression is established between a maximum absorption constant .sub.A with respect to light with a wavelength of 430 to 550 nm and a maximum absorption constant .sub.B with respect to light with a wavelength of 670 nm or more, where .sub.B/.sub.A65. In a spectral transmittance curve, an average transmittance of light with a wavelength of 430 to 460 nm is 94.0% or more when a transmittance at the maximum absorption wavelength .sub.max is set to 1%.

Provided is a near-infrared-absorbing dye increasing a visible light transmittance and having a near-infrared blocking characteristic. The near-infrared-absorbing dye has an absorption characteristic measured by dissolving the dye in dichloromethane satisfying the following requirements. In an absorption spectrum at a wavelength of 400 to 800 nm, there is a maximum absorption wavelength .sub.max in a wavelength region of 670 nm or more. The following relational expression is established between a maximum absorption constant .sub.A with respect to light with a wavelength of 430 to 550 nm and a maximum absorption constant .sub.B with respect to light with a wavelength of 670 nm or more, where .sub.B/.sub.A65. In a spectral transmittance curve, an average transmittance of light with a wavelength of 430 to 460 nm is 94.0% or more when a transmittance at the maximum absorption wavelength .sub.max is set to 1%.

According to the present teachings, compositions, kits, and methods for protein melt analysis are provided that utilizing one or more fluorophore dyes. In some embodiments, a method comprises preparing a sample by mixing at least one protein with two or more dyes, and applying a controlled heating, while recording the fluorescence emission of the sample. The methods can be used, for example, for screening conditions for optimized protein stability, screening for ligands that bind and enhance protein stability (e.g., protein-protein interactions), screening for mutations for enhanced stability, screening crystallization conditions for protein stability, screening storage conditions for protein stability, and screening conditions in which a protein will be used (e.g., production conditions, treatment conditions, etc.) for protein stability.

A stereo viewing device comprises a first lens comprising a first lens filter, and a second lens comprising a second lens filter. The first lens filter comprises a first set of light absorbing dyes that define a first set of rejection bands. The first set of light absorbing dyes comprises at least a first polymethine dye. The second lens filter comprises a second set of light absorbing dyes that define a second set of rejection bands different from the first set of rejection bands. The second set of light absorbing dyes comprises at least a second polymethine dye.

A stereo viewing device comprises a first lens comprising a first lens filter, and a second lens comprising a second lens filter. The first lens filter comprises a first set of light absorbing dyes that define a first set of rejection bands. The first set of light absorbing dyes comprises at least a first polymethine dye. The second lens filter comprises a second set of light absorbing dyes that define a second set of rejection bands different from the first set of rejection bands. The second set of light absorbing dyes comprises at least a second polymethine dye.

The composition includes two or more near infrared absorbing compounds having an absorption maximum in a wavelength range of 650 to 1000 nm and having a solubility of 0.1 mass % or lower in water at 23? C., in which the two or more near infrared absorbing compounds include a first near infrared absorbing compound having an absorption maximum in a wavelength range of 650 to 1000 nm, and a second near infrared absorbing compound having an absorption maximum in a wavelength range of 650 to 1000 nm which is shorter than the absorption maximum of the first near infrared absorbing compound, and a difference between the absorption maximum of the first near infrared absorbing compound and the absorption maximum of the second near infrared absorbing compound is 1 to 150 nm.

Provided are dyes and compositions which are useful in a number of applications, such as the detection and monitoring protein aggregation, kinetic studies of protein aggregation, neurofibrillary plaques analysis, evaluation of protein formulation stability, and analysis of molecular chaperone activity.

A method for forming a patterned cured film using a negative photosensitive composition. The composition includes a photopolymerizable compound and a photopolymerization initiator including an oxime ester compound of a specific structure having a 9,9-disubstituted fluorenyl group which is used for formation of a thick film resist pattern. The composition is mixed with an alkali-soluble resin which is a polymer of a monomer having an unsaturated double bond and includes a unit derived from a monomer having an aromatic group.

The present disclosure relates to a fluorogenic pH-sensitive dye including an aryl compound having a sulfonyl group (SO.sub.2); and an agarose compound covalently bonded to the sulfonyl group (SO.sub.2) of the aryl compound.

According to the present teachings, compositions, kits, and methods for protein melt analysis are provided that utilizing one or more fluorophore dyes. In some embodiments, a method comprises preparing a sample by mixing at least one protein with two or more dyes, and applying a controlled heating, while recording the fluorescence emission of the sample. The methods can be used, for example, for screening conditions for optimized protein stability, screening for ligands that bind and enhance protein stability (e.g., protein-protein interactions), screening for mutations for enhanced stability, screening crystallization conditions for protein stability, screening storage conditions for protein stability, and screening conditions in which a protein will be used (e.g., production conditions, treatment conditions, etc.) for protein stability.