Canine Matrix metalloproteinase 2/Gelatinase A (MMP-2) ELISA Kit
| Product Name | Canine Matrix metalloproteinase 2/Gelatinase A (MMP-2) ELISA Kit |
|---|---|
| Description | Canine Matrix metalloproteinase 2/Gelatinase A (MMP-2) ELISA Kit has high sensitivity and excellent specificity for detection of Canine MMP2. No significant cross-reactivity or interference between Canine MMP2 and analogues was observed. MMP-2 is a member of the matrix metalloproteinase (MMP) gene family, that are zinc-dependent enzymes capable of cleaving components of the extracellular matrix and molecules involved in signal transduction. Matrix metalloproteinase 2/Gelatinase A is a gelatinase A, type IV collagenase, that contains three fibronectin type II repeats in its catalytic site that allow binding of denatured type IV and V collagen and elastin. Unlike most MMP family members, activation of this protein can occur on the cell membrane. Matrix metalloproteinase 2/Gelatinase A can be activated extracellularly by proteases, or, intracellulary by its S-glutathiolation with no requirement for proteolytical removal of the pro-domain. Matrix metalloproteinase 2/Gelatinase A is thought to be involved in multiple pathways including roles in the nervous system, endometrial menstrual breakdown, regulation of vascularization, and metastasis. Mutations in MMP-2 have been associated with Winchester syndrome and Nodulosis-Arthropathy-Osteolysis (NAO) syndrome. Alternative splicing results in multiple transcript variants encoding different isoforms. This Canine Matrix metalloproteinase 2/Gelatinase A (MMP-2) ELISA Kit employs a two-site sandwich ELISA to quantitate MMP2 in samples. An antibody specific for MMP2 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anyMMP2 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for MMP2 is added to the wells. After washing, Streptavidin conjugated Horseradish Peroxidase (HRP) is added to the wells. Following a wash to remove any unbound avidin-enzyme reagent, a substrate solution is added to the wells and color develops in proportion to the amount of MMP2 bound in the initial step. The color development is stopped and the intensity of the color is measured. |
| Synonyms | MMP2, CLG4, CLG4A, MMP-II, MONA, TBE-1, collagenase type IV-A, matrix metalloproteinase 2, matrix metalloproteinase-II, neutrophil gelatinase |
| Method | Sandwich ELISA |
| Detection Range | Please inquire |
| Sensitivity | Please inquire |
| Reactivity | Canine |
| Sample Types | Cell culture supernatants, Serum, Plasma, Other biological fluids |
| Storage | 2-8°C |
| Background | MMP-2 is a member of the matrix metalloproteinase (MMP) gene family, that are zinc-dependent enzymes capable of cleaving components of the extracellular matrix and molecules involved in signal transduction. Matrix metalloproteinase 2/Gelatinase A is a gelatinase A, type IV collagenase, that contains three fibronectin type II repeats in its catalytic site that allow binding of denatured type IV and V collagen and elastin. Unlike most MMP family members, activation of this protein can occur on the cell membrane. Matrix metalloproteinase 2/Gelatinase A can be activated extracellularly by proteases, or, intracellulary by its S-glutathiolation with no requirement for proteolytical removal of the pro-domain. Matrix metalloproteinase 2/Gelatinase A is thought to be involved in multiple pathways including roles in the nervous system, endometrial menstrual breakdown, regulation of vascularization, and metastasis. Mutations in MMP-2 have been associated with Winchester syndrome and Nodulosis-Arthropathy-Osteolysis (NAO) syndrome. Alternative splicing results in multiple transcript variants encoding different isoforms. |
| Supplier | Abbkine |
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