Solid Phase Sandwich ELISA
96-well strip plate
Sample Type & Volumne Required
31.20 - 2,000 pg/mL
For fifteen 96-well plates*
- * Following cell simulation.
* Provided that the recommended microplates, buffers, diluents, substrates and solutions
are used, and the assay is run as summarized in the Assay Procedure provided.
This DuoSet ELISA Development kit contains the basic components required for the development of sandwich ELISAs to measure natural and Recombinant . The suggested diluent is suitable for the analysis of most cell culture supernate samples. Diluents for complex matrices, such as serum and plasma, should be evaluated prior to use in this DuoSet.
* Provided that the recommended microplates, buffers, diluents, substrates and solutions are used, and the assay is run as summarized in the Assay Procedure provided.
- Optimized capture and detection antibody pairings with recommended concentrations save lengthy development time
- Development protocols are provided to guide further assay optimization
- Assay can be customized to your specific needs
- Economical alternative to complete kits
- Capture Antibody
- Detection Antibody
- Recombinant Standard
- Streptavidin conjugated to horseradish-peroxidase (Streptavidin-HRP)
Other Reagents Required
(Catalog # DY006
), or 137 mM NaCl, 2.7 mM KCl, 8.1 mM Na2
, 1.5 mM KH2
, pH 7.2 - 7.4, 0.2 µm filtered Wash Buffer:
(Catalog # WA126
), or equivalent Reagent Diluent* Blocking Buffer* Substrate Solution:
1:1 mixture of Color Reagent A (H2
) and Color Reagent B (Tetramethylbenzidine) (Catalog # DY999
) Stop Solution:
2 N H2
(Catalog # DY994
: R&D Systems (Catalog # DY990
), or equivalent Plate Sealers:
ELISA Plate Sealers (Catalog # DY992
), or equivalent
*For the Reagent Diluent and Blocking Buffer recommended for a specific DuoSet ELISA Development Kit, please see the product .
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).
Matrix Metalloproteinase 13
CLG 3; CLG3EC 3.4.24; collagenase 3; EC 3.4.24.-; EC 22.214.171.124; EC 126.96.36.199; EC 188.8.131.52; EC 184.108.40.206; EC 220.127.116.11; MANDP1; matrix metallopeptidase 13 (collagenase 3); matrix metalloproteinase 13 (collagenase 3); Matrix metalloproteinase-13; MMP-13
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