An object of the present invention is to provide a standard substance for quantification of PSA having a specific sugar chain that can be used in a general purpose quantification, wherein the standard substance has less unbalanced sugar chain expression patterns, can be manufactured with high reproducibility, and enables the quantification of patient's sample comprising a high concentration of PSA, and preparation method therefor, standard solution for PSA quantification, and PSA quantification method. The standard substance comprises a compound having the structure of a PSA with a sugar chain represented by any of the following formulae A to D, and is isolated and purified from a natural product, chemically or enzymatically altered from a natural product, or the compound is artificially synthesized.

Provided herein are methods for inkjet printing objects, including objects which may be used as elements of microfluidic devices. The microfluidic devices incorporating the elements are also provided. Such microfluidic devices include those configured to quantify the expression and activity of exosomal matrix metalloprotease, MMP14. These microfluidic devices may be used in methods of monitoring breast cancer in patients having breast cancer.

Provided herein are methods for inkjet printing objects, including objects which may be used as elements of microfluidic devices. The microfluidic devices incorporating the elements are also provided. Such microfluidic devices include those configured to quantify the expression and activity of exosomal matrix metalloprotease, MMP14. These microfluidic devices may be used in methods of monitoring breast cancer in patients having breast cancer.

This invention reveals the potential applications of modified porcine plasma fibronectin that could be applied as a safe material for clinical wound healing and tissue repair. In order to seek safe sources of plasma fibronectin for practical consideration in wound dressing, this invention isolated and modified fibronectin from porcine plasma and demonstrated that modified porcine plasma fibronectin has similar ability as homo plasma fibronectin being as a suitable substrate for stimulation of cell adhesion and directed cell migration. The present invention also reveals a material and a pharmaceutical composition enhance wound healing.

This invention reveals the potential applications of modified porcine plasma fibronectin that could be applied as a safe material for clinical wound healing and tissue repair. In order to seek safe sources of plasma fibronectin for practical consideration in wound dressing, this invention isolated and modified fibronectin from porcine plasma and demonstrated that modified porcine plasma fibronectin has similar ability as homo plasma fibronectin being as a suitable substrate for stimulation of cell adhesion and directed cell migration. The present invention also reveals a material and a pharmaceutical composition enhance wound healing.

The present invention generally pertains to methods of quantitating therapeutic proteins co-administered to a subject using LC-MRM-MS. In particular, the present invention pertains to the use of dual enzymatic digestion to generate unique surrogate peptides allowing for the accurate quantitation of co-administered therapeutic proteins using LC-MRM-MS.

The present invention generally pertains to methods of quantitating therapeutic proteins co-administered to a subject using LC-MRM-MS. In particular, the present invention pertains to the use of dual enzymatic digestion to generate unique surrogate peptides allowing for the accurate quantitation of co-administered therapeutic proteins using LC-MRM-MS.

The present invention includes a method for analyzing reactions. The method includes the steps of providing a solution of at least one acceptor chemical and at least one donor chemical. The donor chemical is capable of donating a chemical moiety to the acceptor chemical. The solution further includes at least one controller chemical that affects the reaction between the donor chemical and the acceptor chemical. The solution is then incubated so that a portion of the acceptor chemical reacts with the donor chemical to form an acceptor product. Unreacted donor chemical is separated from the acceptor product. The acceptor product or the donor chemical is then measured using X-ray fluorescence. Another aspect of the present invention includes a method for analyzing protein function. The method includes the steps of providing a solution of at least one acceptor chemical and at least one donor chemical. The donor chemical is capable of donating a chemical moiety to the acceptor chemical. The donor chemical includes a functional group selected from ester, anhydride, imide, acyl halide, and amide. The solution is then incubated so that a portion of the acceptor chemical reacts with the donor chemical to form an acceptor product. Unreacted donor chemical is separated from the acceptor product. The acceptor product or the donor chemical is then measured using X-ray fluorescence. Yet another aspect of the present invention includes a method for analyzing protein function. The method includes the steps of providing a solution of at least one acceptor chemical and at least one donor chemical. The solution is then incubated so that a portion of the acceptor chemical reacts with the donor chemical to form an acceptor product. Unreacted donor chemical is separated from the acceptor product. The acceptor product or the donor chemical is then measured using X-ray fluorescence. An additional analytical method is also used to measure either the acceptor product or the donor chemical.

The present invention includes a method for analyzing reactions. The method includes the steps of providing a solution of at least one acceptor chemical and at least one donor chemical. The donor chemical is capable of donating a chemical moiety to the acceptor chemical. The solution further includes at least one controller chemical that affects the reaction between the donor chemical and the acceptor chemical. The solution is then incubated so that a portion of the acceptor chemical reacts with the donor chemical to form an acceptor product. Unreacted donor chemical is separated from the acceptor product. The acceptor product or the donor chemical is then measured using X-ray fluorescence. Another aspect of the present invention includes a method for analyzing protein function. The method includes the steps of providing a solution of at least one acceptor chemical and at least one donor chemical. The donor chemical is capable of donating a chemical moiety to the acceptor chemical. The donor chemical includes a functional group selected from ester, anhydride, imide, acyl halide, and amide. The solution is then incubated so that a portion of the acceptor chemical reacts with the donor chemical to form an acceptor product. Unreacted donor chemical is separated from the acceptor product. The acceptor product or the donor chemical is then measured using X-ray fluorescence. Yet another aspect of the present invention includes a method for analyzing protein function. The method includes the steps of providing a solution of at least one acceptor chemical and at least one donor chemical. The solution is then incubated so that a portion of the acceptor chemical reacts with the donor chemical to form an acceptor product. Unreacted donor chemical is separated from the acceptor product. The acceptor product or the donor chemical is then measured using X-ray fluorescence. An additional analytical method is also used to measure either the acceptor product or the donor chemical.

Provided herein are compounds useful for imaging granzyme B. An exemplary compound provided herein is useful as a radiotracer for position emission tomography (PET) and/or single photon emission tomography (SPECT) imaging. Methods of imaging granzyme B, combination therapies, and kits comprising the granzyme B imaging agents are also provided.