MILLIPLEX^® Human MMP Panel

Luminex is a registered trademark of Luminex Corp

MILLIPLEX is a registered trademark of Merck KGaA, Darmstadt, Germany

xMAP is a registered trademark of Luminex Corp

MILLIPLEX^® Qualified assays undergo rigorous assay development, verification, and Quality Control testing to achieve optimal performance. Simultaneously analyze up to 3 analytes in human serum, plasma, urine, and cell culture supernatants.Analytes included: MMP-3, MMP-12, MMP-13Assay Characteristics: Refer to kit protocol for assay cross-reactivity, sensitivity, precision, and accuracy.

For research use only. Not for use in diagnostic procedures.Label License/Sticker for Assay Product:By opening the packaging containing this Assay Product (which contains fluorescently labeled microsphere beads authorized by Luminex Corporation) or using this Assay Product in any manner, you are consenting and agreeing to be bound by the End User Terms and Conditions and the End User License Agreement available at http://support.diasorin.com/end-user-terms-and-conditions/. If you do not agree to all of the terms and conditions, you must promptly return this Assay Product for a full refund prior to using it in any manner.

Targeted 3-Plex Design: Focused Luminex^® xMAP^® magnetic bead platform specifically quantitates MMP-3, MMP-12, and MMP-13 simultaneously, providing concentrated analysis of key tissue remodeling enzymes in a single well.Broad Sample Compatibility: Analytically verified across serum, plasma, urine, tissue/cell lysates, and culture supernatants with neat sample processing - no dilution required for most applications.Streamlined Workflow: Optimized 3-analyte configuration delivers fast, one-day results while maximizing sample conservation and minimizing hands-on time for research studies.Precision Research Focus: Concentrate on three critical MMPs involved in tissue degradation and remodeling processes, enabling targeted investigation of specific pathological pathways in inflammation research.Mechanistic Research Applications: Target MMPs specifically associated with collagen degradation (MMP-3, MMP-13) and elastin breakdown (MMP-12) to investigate tissue destruction mechanisms in arthritis, cardiovascular, and pulmonary research.

MMPs (matrix metalloproteinases), a family of zinc proteases responsible for the breakdown of extracellular matrix (ECM), play a key role in normal physiological processes, such as embryonic development and tissue morphogenesis, tissue and bone remodeling, wound healing, and angiogenesis. These processes rely on MMPs′ role in the cleavage of cell surface receptors, the release of apoptotic ligands, cell proliferation and differentiation, and chemokine activity modulation. Similar in structure, MMPs are synthesized and secreted as inactive pro-enzymes that require proteolytic cleavage for activation. This process can be mediated by serine proteases or other MMPs. An increase in MMP expression occurs in response to a wide range of stimuli, including adhesion molecules, growth factors, cytokines, and hormones. Regulation of MMP activity is controlled primarily by TIMPs (tissue inhibitors of metalloproteinases). Therefore, disruption of the MMP/TIMP balance can result in arthritis, cardiovascular disease and tumor growth and metastasis.