Abstract: Devices, methods, kits and means for easy, accurate, and fast estimation of soil microbial load, including fungal load, and fungal to bacterial ratio are described. The methods include extracting soil biomass into an extraction fluid to obtain a soil extract and detecting the fungal fraction, the bacterial fraction, and the fungal to bacterial ratio in the soil extract. The devices typically include microBIOMETER®, devices for particle size discrimination, and devices for absorbance and reflectance detection. The difference in microscopic sizes or spectroscopic absorbance of the fungal particles relative to those of the bacterial particles is used to compute the contribution of each type of particle to the biomass. In one example, the relative coverage of the microBIOMETER® device membrane by the fungal and/or bacterial particles can be measured by and then calculated using a cell phone camera and application.

Abstract: Devices, methods, kits and means for easy, accurate, and fast estimation of soil microbial load, including fungal load, and fungal to bacterial ratio are described. The methods include extracting soil biomass into an extraction fluid to obtain a soil extract and detecting the fungal fraction, the bacterial fraction, and the fungal to bacterial ratio in the soil extract. The devices typically include microBIOMETER®, devices for particle size discrimination, and devices for absorbance and reflectance detection. The difference in microscopic sizes or spectroscopic absorbance of the fungal particles relative to those of the bacterial particles is used to compute the contribution of each type of particle to the biomass. In one example, the relative coverage of the microBIOMETER® device membrane by the fungal and/or bacterial particles can be measured by and then calculated using a cell phone camera and application.

Abstract: Devices, methods, and kits for easy, accurate, and fast estimation of soil microbial load are provided. The devices include membranes that are rapidly wettable with aqueous fluids and retain soil microorganisms of up to 200 micrometers in size, without retaining soil pigments. The method requires reconstituting a soil sample in an extraction fluid so that the microorganisms in the soil sample are released from particles of the soil sample and into the extraction fluid. The method does not require a filtration step. The extraction fluid containing the microorganisms suspended therein is then pipetted onto the membrane device, or the membrane is dipped into the extraction fluid. The color appearing on the membrane is then compared to color intensity gray scale strips to determine the soil microbial load.

Abstract: Devices, methods, and kits for easy, accurate, and fast estimation of soil microbial load are provided. The devices include membranes that are rapidly wettable with aqueous fluids and retain soil microorganisms of up to 200 micrometers in size, without retaining soil pigments. The method requires reconstituting a soil sample in an extraction fluid so that the microorganisms in the soil sample are released from particles of the soil sample and into the extraction fluid. The method does not require a filtration step. The extraction fluid containing the microorganisms suspended therein is then pipetted onto the membrane device, or the membrane is dipped into the extraction fluid. The color appearing on the membrane is then compared to color intensity gray scale strips to determine the soil microbial load.

Abstract: Methods and compositions for the preparation of soil samples and the determination of the number of microbes within a soil sample are disclosed. The methods include measuring, solubilizing, bleaching and filtering soil samples and measuring the turbidity of the filtered solution. The turbidity of the sample can be determined by visual inspection of a Secchi disk viewed through the column liquid sample in a transparent tubular cylinder, or by using a cell phone camera and application. Devices and kits for the rapid, cost efficient determination of microbial numbers in the field setting are disclosed. The disclosed devices and methods can also be used for applications other than determination of microbial numbers.

Abstract: Methods and compositions for the preparation of soil samples and the determination of the number of microbes within a soil sample are disclosed. The methods include measuring, solubilizing, bleaching and filtering soil samples and measuring the turbidity of the filtered solution. The turbidity of the sample can be determined by visual inspection of a Secchi disk viewed through the column liquid sample in a transparent tubular cylinder, or by using a cell phone camera and application. Devices and kits for the rapid, cost efficient determination of microbial numbers in the field setting are disclosed. The disclosed devices and methods can also be used for applications other than determination of microbial numbers.

Abstract: The invention is directed to preferred repeat sequences of Neural Thread Protein (NTP), peptides, mimetics, antibodies, and nucleic acids of the preferred sequences, and diagnostic and therapeutic methods of using such preferred NTP sequences.

Abstract: A method of improving specific immune responses to small immunogens, haptens, has been developed by changing the linkage between the hapten and carrier being used for immunization. Antibodies to a glycated protein have been developed, utilizing an immunogen which is composed of a glycated peptide mimic of the glycated peptide sequence which is the target epitope, wherein the peptide mimic is constructed to conformationally mimic the conformation of the peptide in the native protein, the peptide mimic contains no charged groups or other immunodominant group, and the peptide mimic is connected to a spacer sequence equivalent to a peptide spacer of between one and thirty amino acids in length, which serves to position the peptide epitope in a conformation that approximates its conformation in the native protein. In a further embodiment the peptide mimic and spacer are linked to a carrier molecule.

Abstract: A method of improving specific immune response to small immunogens, haptens, has been developed by changing the linkage between the hapten and carrier being used for immunization. High affinity antibodies to cotinine have been produced using this method. Antibodies to a glycated protein have also been developed, utilizing an immunogen which is composed of a glycated peptide mimic of the glycated peptide sequence which is the target epitope, wherein the peptide mimic is constructed to conformationally mimic the conformation of the peptide in the native protein, the peptide mimic contains no charged groups or other immunodominant group, and is connected to a spacer sequence equivalent to a peptide spacer of between one and thirty amino acids in length, which serves to position the peptide epitope in a conformation that approximates its conformation in the native protein. In another embodiment, the peptide mimic and spacer are linked to a carrier molecule.

Abstract: The invention is directed to preferred repeat sequences of Neural Thread Protein (NTP), peptides, mimetics, antibodies, and nucleic acids of the preferred sequences, and diagnostic and therapeutic methods of using such preferred NTP sequences.

Abstract: A method of improving specific immune responses to small immunogens, haptens, has been developed by changing the linkage between the hapten and carrier being used for immunization. High affinity antibodies to the hapten cotinine have been produced using this method. Antibodies to a glycated protein have also been developed, utilizing an immunogen which is composed of a glycated peptide mimic of the glycated peptide sequence which is the target epitope, wherein the peptide mimic is constructed to conformationally mimic the conformation of the peptide in the native protein, the peptide mimic contains no charged groups or other immunodominant group, and the peptide mimic is connected to a spacer sequence equivalent to a peptide spacer of between one and thirty amino acids in length, which serves to position the peptide epitope in a conformation that approximates its conformation in the native protein. In a further embodiment the peptide mimic and spacer are linked to a carrier molecule.

Abstract: A method has been developed to detect the levels of apolipoproteins A-1 and B in saliva, which is correlated with the levels of HDL and LDL in serum, respectively. In unstimulated saliva, the ration of Apo A to Apo B is correlated with the ration of HDL to LDL in serum. Albumin can be used to normalize the sample for dilution. The high degree of correlation in combination with a simple, quick test that can be performed at the site of collection provides a cost effective, patient friendly means to monitor an individual's risk of heart disease. In the preferred embodiment, saliva production is stimulated by means such as breath mint or tart solution (such as lemon) and the effect of dilution controlled by reference to albumin.

Abstract: A method of improving specific immune responses to smal immunogens, haptens, has been developed by changing the linkage between the hapten and carrier being used for immunization. High affinity antibodies to the hapten cotinine have been produced using this method. Antibodies to a glycated protein have also been developed, utilizing an immunogen which is composed of a glycated peptide mimic of the glycated peptide sequence which is the target epitope, wherein the peptide mimic is constructed to conformationally mimic the conformation of the peptide in the native protein, the peptide mimic contains no charged groups or other immunodominant group, and the peptide mimic is connected to a spacer sequence equivalent to a peptide spacer of between one and thirty amino acids in length, which serves to position the peptide epitope in a conformation that approximates its conformation in the native protein. In a further embodiment the peptide mimic and spacer are linked to a carrier molecule.

Abstract: A method of improving specific immune responses to smal immunogens, haptens, has been developed by changing the linkage between the hapten and carrier being used for immunization. High affinity antibodies to the hapten cotinine have been produced using this method. Antibodies to a glycated protein have also been developed, utilizing an immunogen which is composed of a glycated peptide mimic of the glycated peptide sequence which is the target epitope, wherein the peptide mimic is constructed to conformationally mimic the conformation of the peptide in the native protein, the peptide mimic contains no charged groups or other immunodominant group, and the peptide mimic is connected to a spacer sequence equivalent to a peptide spacer of between one and thirty amino acids in length, which serves to position the peptide epitope in a conformation that approximates its conformation in the native protein. In a further embodiment the peptide mimic and spacer are linked to a carrier molecule.

Abstract: A method of improving specific immune responses to smal immunogens, haptens, has been developed by changing the linkage between the hapten and carrier being used for immunization. High affinity antibodies to the hapten cotinine have been produced using this method. Antibodies to a glycated protein have also been developed, utilizing an immunogen which is composed of a glycated peptide mimic of the glycated peptide sequence which is the target epitope, wherein the peptide mimic is constructed to conformationally mimic the conformation of the peptide in the native protein, the peptide mimic contains no charged groups or other immunodominant group, and the peptide mimic is connected to a spacer sequence equivalent to a peptide spacer of between one and thirty amino acids in length, which serves to position the peptide epitope in a conformation that approximates its conformation in the native protein. In a further embodiment the peptide mimic and spacer are linked to a carrier molecule.

Abstract: A method of improving specific immune responses to smal immunogens, haptens, has been developed by changing the linkage between the hapten and carrier being used for immunization. High affinity antibodies to the hapten cotinine have been produced using this method. Antibodies to a glycated protein have also been developed, utilizing an immunogen which is composed of a glycated peptide mimic of the glycated peptide sequence which is the target epitope, wherein the peptide mimic is constructed to conformationally mimic the conformation of the peptide in the native protein, the peptide mimic contains no charged groups or other immunodominant group, and the peptide mimic is connected to a spacer sequence equivalent to a peptide spacer of between one and thirty amino acids in length, which serves to position the peptide epitope in a conformation that approximates its conformation in the native protein. In a further embodiment the peptide mimic and spacer are linked to a carrier molecule.

Abstract: A method has been developed to detect the levels of apolipoproteins A-1 and B in saliva, which is correlated with the levels of HDL and LDL in serum, respectively. In unstimulated saliva, the ratio of Apo A to Apo B is correlated with the ratio of HDL to LDL in serum. Albumin can be used to normalize the sample for dilution. The high degree of correlation in combination with a simple, quick test that can be performed at the site of collection provides a cost effective, patient friendly means to monitor an individual's risk of heart disease. In the preferred embodiment, saliva production is stimulated by means such as breath mint or tart solution (such as lemon) and the effect of dilution controlled by reference to albumin. In the most preferred embodiment, the assay is an ELISA assay performed using the Serex laminated strip format as described in U.S. Pat. Nos. 5,710,009, 5,500,375, and 5,451,504. These strips are advantageous since they serve as the collection and assay device.

Abstract: A monoclonal antibody, Serex A93, recognizes peptide linked pyridinoline in Type I bone collagen fragments and can be used to quantitate bone resorption. The hybridoma producing this antibody has been deposited with the American Type Culture Collection, Rockville, Md., under accession number HB-12254. The epitope reactive with the antibody is stable to acid hydrolysis and therefore is not a linear peptide. The antibody recognizes pyridinoline in bound or conjugated form, but not in the free form found in urine. The antibody is useful in immunoassays for determining bone resorption, utilizing body fluids such as urine, saliva, blood, or sweat.

Abstract: A method of improving specific immune responses to small immunogens, haptens, has been developed by changing the linkage between the hapten and carrier being used for immunization. High affinity antibodies to the hapten cotinine have been produced using this method. Antibodies to a glycated protein have also been developed, utilizing an immunogen which is composed of a glycated peptide mimic of the glycated peptide sequence which is the target epitope, wherein the peptide mimic is constructed to conformationally mimic the conformation of the peptide in the native protein, the peptide mimic contains no charged groups or other immunodominant group, and the peptide mimic is connected to a spacer sequence equivalent to a peptide spacer of between one and thirty amino acids in length, which serves to position the peptide epitope in a conformation that approximates its conformation in the native protein. In a further embodiment the peptide mimic and spacer are linked to a carrier molecule.

Abstract: A method and device are provided for the semi-quantitative and quantitative determination of an analyte in a sample. A non-competitive trap which can bind unreacted labelled receptor to analyte but has virtually no binding capabilities to receptor in the presence of analyte is used. Labelled receptor:analyte complex is trapped in a second trap. The relative amounts of unbound receptor in the non-competitive trap versus the amount of receptor:analyte complex in the second trap is a measure of the amount of analyte in the sample.