Methods for diagnosing or monitoring a condition, disorder or disease associated with circadian, diurnal or other temporal rhythms by detecting circa-miRNAs and circa-microbiomes associated with said condition, disorder or disease. Methods for correcting or normalizing sequence data to correct for diurnal or circadian fluctuations in quantities of circa-miRNAs and/or circa-microbiomes by adjusting or normalizing values based on the time of day when a saliva sample containing these RNAs was collected.

A method of quantitatively determining the concentration of at least one analyte in a sample by: (i) adding a portion of the sample to a first analyte assay formulation and to an analyte assay reference formulation to generate a first analyte sample and analyte reference sample and determining the concentration of the at least one analyte in the sample; and/or (ii) adding a portion of the sample to a second analyte assay formulation and determining the concentration of the at least one analyte in the sample, as well as formulations, kits of parts, systems and computer implemented methods associated with the method.

The disclosure relates to a multi-epitope fusion protein as well as to its use as calibrator and/or control in an in vitro diagnostics immunoassay for detecting HCV core antigen. The multi-epitope fusion protein has two to six different non-overlapping linear peptides present in the amino acid sequence of hepatitis C virus (HCV) core protein, wherein each of the peptides is separated from the other peptides by a spacer consisting of a non-HCV amino acid sequence and having a chaperone amino acid sequence. No further HCV specific amino acid sequences are present in the polypeptide. A further aspect relates to a reagent kit for detecting HCV core antigen containing said multi-epitope fusion protein as calibrator or control or both.

The current disclosure provides for specific peptides, and derived ionization characteristics of the peptides, from the tumor necrosis factor receptor superfamily member 8 protein (CD30) that are particularly advantageous for quantifying the CD30 protein directly in biological samples that have been fixed in formalin by the method of Selected Reaction Monitoring (SRM) mass spectrometry, or what can also be termed as Multiple Reaction Monitoring (MRM) mass spectrometry. Such biological samples are chemically preserved and fixed wherein the biological sample is selected from tissues and cells treated with formaldehyde containing agents/fixatives including formalin-fixed tissue/cells, formalin-fixed/paraffin embedded (FFPE) tissue/cells, FFPE tissue blocks and cells from those blocks, and tissue culture cells that have been formalin fixed and or paraffin embedded. A protein sample is prepared from the biological sample using the Liquid Tissue reagents and protocol and the CD30 protein is quantitated in the Liquid Tissue sample by the method of SRM/MRM mass spectrometry by quantitating in the protein sample at least one or more of the peptides described. These peptides can be quantitated if they reside in a modified or an unmodified form. An example of a modified form of a CD30 peptide is phosphorylation of a tyrosine, threonine, serine, and/or other amino acid residues within the peptide sequence.

A method of quantitatively determining the concentration of at least one analyte in a sample by: (i) adding a portion of the sample to a first analyte assay formulation and to an analyte assay reference formulation to generate a first analyte sample and analyte reference sample and determining the concentration of the at least one analyte in the sample and/or (ii) adding a portion of the sample to a second analyte assay formulation and determining the concentration of the at least one analyte in the sample, as well as formulations, kits of parts, systems and computer implemented methods associated with the method.

The present invention relates to a method for the absolute quantification of naturally processed HLA-restricted cancer peptides, i.e. the determination of the copy number of peptide(s) as presented per cell. The present invention can not only be used for the development of antibody therapies or peptide vaccines, but is also highly valuable for a molecularly defined immuno-monitoring, and useful in the processes of identifying of new peptide antigens for immunotherapeutic strategies, such as respective vaccines, antibody-based therapies or adoptive T-cell transfer approaches in cancer, infectious and/or autoimmune diseases.

A method and device are provided for measuring a level of a clinically relevant analyte (such as glucose) in a fluid (such as blood). The device includes a flow path for conducting said fluid through the device; a detection chamber arranged on said flow path; and detector means arranged to detect analyte levels in the fluid in said chamber, wherein: said detection chamber contains a predetermined amount of an analyte such that that analyte mixes with fluid in the detection chamber to form, at the detector means, a calibration sample of the fluid at a time after the arrival of the fluid in said detection chamber, and said detector means is arranged to detect a first analyte level of an unadulterated sample of the fluid at a first time which is before the formation of said calibration sample and to detect a second analyte level of said calibration sample at a second time which is after the formation of said calibration sample.

The present invention provides an antibody which comprises a variable heavy (VH) chain comprising CDR1, CDR2 and CDR3, and/or a variable light (VL) chain comprising CDR1, CDR2 and CDR3, wherein the CDRs have the same amino acid sequence as those from a complete antibody isolated from a synovial tissue sample of rheumatoid arthritis patients, as listed in Tables 1 and 2 or Tables 1 A and 2 A.

The invention relates to a sealed bag containing a reference fluid for the calibration or quality control of a sensor element for measuring body fluid parameters, the bag comprising peripheral walls of a first layered material. The bag further comprises an access port formed by an opening in the first layered material, wherein the opening is sealed by a cover of a second layered material, wherein the second layered material is more resistant to oxidation by the reference fluid than the first layered material.

The present invention relates to a method for the absolute quantification of naturally processed HLA-restricted cancer peptides, i.e. the determination of the copy number of peptide(s) as presented per cell. The present invention can not only be used for the development of antibody therapies or peptide vaccines, but is also highly valuable for a molecularly defined immuno-monitoring, and useful in the processes of identifying of new peptide antigens for immunotherapeutic strategies, such as respective vaccines, antibody-based therapies or adoptive T-cell transfer approaches in cancer, infectious and/or autoimmune diseases.