INTENDED USE & DESCRIPTION
For use as quantitative controls for the determination of cytokine concentrations in biological fluids. Concentrations have been assigned using R&D Systems’ Quantikine® kits. Controls are prepared in a buffered protein solution with preservatives. They contain recombinant human cytokines at low, medium and high concentrations. Controls are supplied lyophilized.
STORAGE & STABILITY
Unreconstituted Controls should be stored at 2-8 °C and are stable for at least 6 months from date of receipt. Depending on the analyte of interest, reconstituted controls may be stable when stored at
REAGENT PREPARATION
Reconstitute each vial with the volume of deionized or distilled water indicated on the product datasheet.
PROCEDURE & EXPECTED VALUES
Controls should be assayed in the same manner as unknown specimens.
The acceptable ranges for the analytes in these controls are printed on the product datasheet. Due to possible variations in techniques and methodologies, it is recommended that each laboratory determine its own target range. Laboratories using other test systems should establish their own acceptable ranges as these assays may produce different values.
TECHNICAL HINTS & LIMITATIONS OF THE PROCEDURE
• The ranges were determined using R&D Systems’ Quantikine kits. If expected values are not obtained, verify that the lot numbers on the vials correspond with the lot numbers listed above and the correct volume of deionized or distilled water was used for reconstitution of the controls.
• The results obtained with these controls depend upon several factors associated with methods and instrumentation. Test systems other than those supplied by R&D Systems may result in values that differ from those printed on this product datasheet.
The matrix metalloproteinases (MMPs) consist of 24 known human zinc proteases with essential roles in breaking down components of the extracellular matrix (ECM). Additional MMP substrates include cytokines, chemokines, growth factors and binding proteins, cell/cell adhesion molecules, and other proteinases. With a few exceptions, MMPs share common structural motifs including a pro-peptide domain, a catalytic domain, a hinge region, and a hemopexin-like domain. Synthesized as pro-enzymes, most MMPs are secreted before conversion to their active form. MMP activities are modulated on several levels including transcription, pro-enzyme activation, or by their endogenous inhibitors, tissue inhibitors of metalloproteinases (TIMPs). A subset of MMPs are associated with membranes and designated as membrane-type metalloproteinases (MT-MMP).
