Disclosed are methods and apparatus for separation of biomolecules via two-dimensional gel electrophoresis, methods and apparatus for immunoblotting separated biomolecules, and methods for the use of biomolecules processed via the methods and apparatus of the present invention, including use in a clinical setting. The methods and apparatus for separation of biomolecules via two-dimensional gel comprises vertical agarose gel electrophoresis in the first dimension, and the electrophoresis of a novel non-denaturing 3-35% concave gradient polyacrylamide gel in the second dimension. This novel gel can be cast in a modified gel caster that can facilitate the pouring of multiple gels simultaneously. The methods and apparatus for immunoblotting are useful with any type of immunoblotting, including Western blot, Northern blot, and Southern blot analyzes. These methods and apparatus provide safe, efficient and cost-effective immunoblots, while facilitating the reduction of exposure to toxic or radioactive materials, as well as the disposal of those materials.

The present application provides novel compositions, methods, and assays for use in identification of appropriate diagnostic markers in blood. These compositions, methods, and assays are capable of distinguishing normal levels of detectable markers from changes in marker levels that are indicative of changes in health status.

The present invention provides biomarker-based methods for diagnosing stroke in a patient suspected of having suffered a stroke, and also for discriminating between ischemic stroke and transient ischemic attack. Substrates comprising probes for specific combinations of biomarkers useful in the methods of the invention are also described.

The present invention primarily relates to a method for analyzing the amount of immunoregulatory integrin binding factors and/or patient endogenous antibodies which are directed against such factors, the factors having the capacity to modulate the immune functions in a. subject suffering from cancer or inflammatory or autoimmune diseases, by utilizing binding reagents to determine these factors and/or the patient endogenous antibodies which are directed against such factors, whereby the prognosis and/or the therapeutic efficacy of any treatment of a subject suffering from cancer or inflammatory or autoimmune diseases can be determined and/or monitored. The invention further relates to the use of therapeutically active compounds for eliminating, inhibiting or enhancing such binding factors for the manufacture of pharmaceuticals to be used in the treatment of cancer, inflammatory conditions or autoimmune diseases.

The invention provides methods and compositions for the rapid and sensitive detection of post-translationally modified proteins, and particularly of those with posttranslational glycosylations. The methods can be used to detect O-GlcNAc posttranslational modifications on proteins on which such modifications were undetectable using other techniques. In one embodiment, the method exploits the ability of an enginered mutant of -1,4-galactosyltransferase to selectively transfer an unnatural ketone functionality onto O-GlcNAc glycosylated proteins. Once transferred, the ketone moiety serves as a versatile handle for the attachment of biotin, thereby enabling detection of the modified protein. The approach permits the rapid visualization of proteins that are at the limits of detection using traditional methods. Further, the preferred embodiments can be used for detection of certain disease states, such as cancer, Alzheimer's disease, neurodegeneration, cardiovascular disease, and diabetes.

The current invention pertains to stabilized peptoids or peptoid-peptide hybrids. The peptoids or peptoid-peptide hybrids are stabilized by side chain-side to side chain linkages and/or backbone cyclization. The current invention also provides a positional library scanning method for identification of peptoids or peptoid-peptide hybrids having a desired biological activity.

A microfluidic array supporting a lipid bilayer assembly on which membrane proteins can be assembled is described.

Methods, devices, and reagents are described for performing assays for hemoglobin Ale, glycated albumin, and other glycated proteins. The methods involve a ratio determination between glycated protein and non-gtycated protein. In some applications, the assay utilizes LOCI for signal generation. This invention is directed to assays and corresponding devices and reagents for detection of glycated protein, particularly including glycated hemoglobin. As is generally understood, such detection is useful in the management of blood glucose levels in diabetic patients and for monitoring the status of pre-diabetic individuals.

The present invention provides substance which can specifically interact with sugar chains. Further, the present invention provides a method for separating, concentrating, or purifying sugar chains or a sugar chain-containing substance in a sample, comprising the steps of: a) contacting a sugar chain-trapping carrier comprising a substance which can specifically interact with sugar chains with the sample in a fluid phase under conditions that the sugar chain-trapping carrier can react with the sugar chains or sugar chain-containing substance; b) isolating a composite of the sugar chain-trapping carrier and the sugar chains or sugar chain-containing substance from the fluid phase; and c) exposing the composite to the conditions that the interaction between the sugar chain-trapping carrier and the sugar chains or sugar chain-containing substance is at least partially eliminated.

The invention discloses a method for measurement of peptidic degradation products of a proteolytic cascade (for example, the renin-angiotensin system (RAS) and the bradykinin system) in biological samples, especially blood samples, wherein the sample is incubated until a steady state equilibrium is reached for at least one peptidic degradation product involved in said proteolytic cascade and wherein said at least one peptidic degradation product in steady state equilibrium of the proteolytic cascade is quantified in the sample.