A diagnostic and prognostic method and system for sequentially analyzing in a biological fluid or tissue extract the presence of an antigenic infectious agent, infectious organism or its toxic product; an antibody response to the antigenic infectious agent, infectious organism or its toxic product; one or more biomarkers formed during infection in response to a communicable disease; and one or more biomarkers to assess the severity of the disease and to monitor the effectiveness of drug therapy or vaccination.

A wash solution for removal of unbound proteins, unreacted antisera, and excess stain from an electrophoresis gel plate and a method of using the wash solution. The wash solution contains one or more of Hexamethylindanopyran, Tetramethyl acetyloctahydronaphthalenes, Hexyl cinnamal, Butylphenyl methylpropional, d-Limonene and Linalool. Alternatively, the wash solution react with lipids and fats in the unbound proteins and/or unreacted antisera, and/or causes pores in the gel to expand yielding a more efficient removal of unbound protein and unbound antisera, and/or contains protease enzymes that digest proteins and an amylase enzyme to hydrolyze starches and sugars.

A wash solution for removal of unbound proteins, unreacted antisera, and excess stain from an electrophoresis gel plate and a method of using the wash solution. The wash solution contains one or more of Hexamethylindanopyran, Tetramethyl acetyloctahydronaphthalenes, Hexyl cinnamal, Butylphenyl methylpropional, d-Limonene and Linalool. Alternatively, the wash solution react with lipids and fats in the unbound proteins and/or unreacted antisera, and/or causes pores in the gel to expand yielding a more efficient removal of unbound protein and unbound antisera, and/or contains protease enzymes that digest proteins and an amylase enzyme to hydrolyze starches and sugars.

A diagnostic and prognostic method and system for sequentially analyzing in a biological fluid or tissue extract the presence of an antigenic infectious agent, infectious organism or its toxic product; an antibody response to the antigenic infectious agent, infectious organism or its toxic product; one or more biomarkers formed during infection in response to a communicable disease; and one or more biomarkers to assess the severity of the disease and to monitor the effectiveness of drug therapy or vaccination.

A diagnostic and prognostic method and system for sequentially analyzing in a biological fluid or tissue extract the presence of an antigenic infectious agent, infectious organism or its toxic product; an antibody response to the antigenic infectious agent, infectious organism or its toxic product; one or more biomarkers formed during infection in response to a communicable disease; and one or more biomarkers to assess the severity of the disease and to monitor the effectiveness of drug therapy or vaccination.

Some embodiments of the systems and methods provided herein relate to an assay. Some such embodiments include multiplex affinity probes and an antigen probe. multiplex affinity probes and an antigen probe Some embodiments include contacting a biological sample with the probes, wherein target binding agents such as antibodies in the biological sample compete away the multiplex affinity probes from binding to the antigen probe. Some such embodiments include detecting a decrease in binding of the multiplex affinity probes to the antigen probe, thereby indicating the presence or an amount of the target binding agents in the biological sample.

Described are cell-based methods for detecting botulinum neurotoxin (BoNT) potency and/or activity in the absence of LD.sub.50 assays that rely upon large numbers of laboratory animals.

A method of capturing human immunoglobulin Fc domains in a biofluid sample is provided. The method includes providing an affinity capture device. The affinity capture device includes a surface having an aptamer that is at least 80% identical to SEQ ID NO 1 immobilized onto the surface of the affinity capture device. The biofluid sample is diluted with a binding buffer. The binding buffer includes (A) tris(hydroxymethyl)aminomethane (Tris), trimethylamine (TES), 2-ethanesulfonic acid (MES), or 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (HEPES); (B) a magnesium cation at a concentration between about 10 .Math.M to about 20 mM; and (C) a total monovalent cation concentration from 0 to no greater than 100 mM. The human immunoglobulin Fc domains in the biofluid sample are adsorbed to the aptamer with the binding buffer.

A method of capturing human immunoglobulin Fc domains in a biofluid sample is provided. The method includes providing an affinity capture device. The affinity capture device includes a surface having an aptamer that is at least 80% identical to SEQ ID NO 1 immobilized onto the surface of the affinity capture device. The biofluid sample is diluted with a binding buffer. The binding buffer includes (A) tris(hydroxymethyl)aminomethane (Tris), trimethylamine (TES), 2-ethanesulfonic acid (MES), or 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (HEPES); (B) a magnesium cation at a concentration between about 10 .Math.M to about 20 mM; and (C) a total monovalent cation concentration from 0 to no greater than 100 mM. The human immunoglobulin Fc domains in the biofluid sample are adsorbed to the aptamer with the binding buffer.

An immunofixation electrophoresis applicator system and method deposits antisera in spaced apart locations on a substrate where the antisera is deposited as an elongated bead in a first direction and retained against migration in a direction transverse to said first direction at least by surface tension.