Solid Phase Sandwich ELISA
96-well strip plate
0.156 - 10 ng/mL
Natural and recombinant rat MMP-9 (Pro-, active, and TIMP-complexed)
< 0.5% cross-reactivity observed with available related molecules.< 50% cross-species reactivity observed with species tested.
No significant interference observed with available related molecules.
The Quantikine Rat Total MMP-9 Immunoassay is a 4.5 hour solid phase ELISA designed to measure total rat MMP-9 (Pro-, active, and TIMP-complexed MMP-9) in cell culture supernates, serum, and plasma. It contains NS0-expressed recombinant rat MMP-9 and antibodies raised against the recombinant factor. This immunoassay has been shown to accurately quantitate the recombinant protein. Results obtained using natural rat MMP-9 showed dose-response curves that were parallel to the standard curves obtained using the Quantikine kit standards. These results indicate that this kit can be used to determine relative mass values for natural rat MMP-9.
Intra-Assay Precision (Precision within an assay) Three samples of known concentration were tested in separate assays to assess inter-assay precision.
Inter-Assay Precision (Precision between assays Three samples of known concentration were tested on one plate to assess intra-assay precision.Cell Culture Supernates, Serum, Platelet-poor Heparin Plasma
|Standard Deviation||0.027||0.068||0.238||0.035||0.046||0.153 |
The recovery of rat MMP-9 spiked into various matrices was evaluated.
|Sample Type ||Average % Recovery ||Range % |
|Cell Culture Samples (n=4) ||94 ||87-107 |
|Platelet-poor Heparin Plasma (n=4) ||92 ||80-103 |
|Serum (n=4) ||97 ||90-115 |
To assess the linearity of the assay, samples containing high concentrations of rat MMP-9 were serially diluted with Calibrator Diluent to produce samples with values within the dynamic range of the assay.
Background: Matrix Metalloproteinase 9
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).
Related Research Areas
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