Human MMP-3 DTSet enzyme-linked immunoassay kit
| Specification | 96*5 Test；96T*15 Test |
|---|---|
| Standard Curve Range | 31.25pg/ml-2000pg/ml |
| Standard Curve Gradient | 7 Points |
| Number of Incubations | 2 |
| Detectable sample | Liquid phase sample of soluble substances. For example: serum, plasma, cell culture supernatant, tissue grinding liquid, etc. |
| Sample Volume | 50 μl |
| Type | Not Ready-to-Use |
| Test Duration | 120min |
| pg/ml | O.D. | Average | Corrected | |
|---|---|---|---|---|
| 0.00 | 0.0204 | 0.0154 | 0.0179 | |
| 31.25 | 0.0857 | 0.0900 | 0.0879 | 0.0700 |
| 62.50 | 0.1462 | 0.1598 | 0.1530 | 0.1351 |
| 125.00 | 0.2553 | 0.3022 | 0.2788 | 0.2609 |
| 250.00 | 0.5585 | 0.4198 | 0.4892 | 0.4713 |
| 500.00 | 1.0360 | 1.1080 | 1.0720 | 1.0541 |
| 1000.00 | 1.8810 | 1.9720 | 1.9265 | 1.9086 |
| 2000.00 | 3.1200 | 2.9650 | 3.0425 | 3.0246 |
Product Features
- 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
Kit Content
- Capture Antibody
- Detection Antibody
- Recombinant Standard
- Streptavidin conjugated to horseradish-peroxidase (Streptavidin-HRP)
Other Reagents Required
DTSet Ancillary Reagent Kit (5 plates): containing 96 well microplates, plate sealers, substrate solution, stop solution, plate coating buffer (PBS), wash buffer, and assay buffer.
- 96 well microplates: YOUKE Life, Catalog # DSEP01. Plate Sealers: YOUKE Life, Catalog # DSSF01.
- Coating Buffer: 137 mM NaCl, 2.7 mM KCl, 8.1 mM Na2HPO4, 1.5 mM KH2PO4, pH 7.2-7.4, 0.2μm filtered . YOUKE Life, Catalog # DSCB01.
- Blocking Buffer: YOUKE Life, Catalog # DSBB01.
- Wash Buffer: 0.05% Tween® 20 in PBS, pH 7.2-7.4. YOUKE Life, Catalog # DSWB01.
- Assay Buffer: 0.5% BSA，0.05% Tween® 20，PBS Solution.YOUKE Life, Catalog # DSAB01
- Substrate Solution: Tetramethylbenzidine. YOUKE Life, Catalog # DSTS01.
- Stop Solution: 0.5mol/ml H2SO4. YOUKE Life, Catalog # DSSS01.
Product Data Sheet
Background: MMP-3
Matrix metalloproteinases (MMPs), also called matrixins, constitute a family of zinc and calcium dependent endopeptidases that function in the breakdown of extracellular matrix (ECM). They play an important role in many normal physiological processes such as embryonic development, morphogenesis, reproduction and tissue remodeling. They also participate in many pathological processes such as arthritis, cancer and cardiovascular disease. While the amounts of newly synthesized MMPs are regulated mainly at the levels of transcription, the proteolytic activities of existing MMPs are controlled through both the activation of proenzymes or zymogens and the inhibition of active enzymes by endogenous inhibitors, alpha -macroglobulins and tissue inhibitors of metalloproteinases (TIMPs).
MMP-3 (also referred to as stromelysin-1) may be expressed in fibroblasts, chondrocytes, endothelial cells, macrophages, vascular smooth muscle cells, osteoblasts, and keratinocytes in response to appropriate stimuli. Various agents regulate its biosynthesis. Inflammatory cytokines such as IL-1 and TNF-alpha, epidermal growth factor, platelet-derived growth factor, phorbol and oncogenic cellular transformation are the inductive agents. In comparison, retinoic acid, glucocorticoids, estrogen, progesterone and TGF-beta suppress MMP-3 synthesis.
MMP-3 is secreted from the cells as a proenzyme. The proenzyme has been shown to stimulate plasminogen activation. The N-terminal pro-domain contains the cysteine switch motif conserved in MMPs that maintains MMP-3 in the latent state. Activation of the proenzyme results in the removal of the pro-domain. MMP-3 activation can be achieved in vitro by proteases such as itself, chyrotrypsin, neutrophil elastase and plasma kallikrein, and by mercury compounds. The resulting active enzyme consists of a catalytic domain with a zinc-binding motif conserved in metzincins. A short hinge peptide links the catalytic domain to the C-terminal hemopexin-like domain. The active MMP-3 is capable of cleaving types III, IV, IX and X collagen, aggrecan, fibronectin, laminin, IGFBP-3, serpins, and IL-1 beta. The active enzyme also activates proMMP-1, -8, -9, and -13. Therefore, it is suggested that MMP-3 may participate in physiological matrix turnover and pathological destruction of the tissue. For example, MMP-3 is required for the generation of a macrophage chemoattractant in a model of herniated disc resorption.
