Matrix Metalloproteinase-2 (MMP-2) Biotrak^™ Activity Assay System

Biotrak^™ MMP-2, Activity Assay System provides a simple, specific and precise quantitative determination of active or pro MMP-2 in tissue culture supernatants, serum, plasma, urine, synovial fluid and tissue homogenates. Active MMP-2 may be measured in the range 0.75 to 12 ng/mL and the sensitivity of the assay is 0.5 ng/mL. A longer incubation protocol enables an assay range of 0.19 to 3 ng/mL with a sensitivity of 190 pg/mL, should higher sensitivity be required. The assay uses the pro form of a detection enzyme that can be activated by captured active MMP-2, into an active detection enzyme, through a single proteolytic event. The natural activation sequence in the pro detection enzyme has been replaced using Protein engineering, with an artificial sequence recognised by specific matrix metalloProteinases. MMP activated detection enzyme can then be measured using a specific chromogenic peptide substrate. Standards and samples are incubated in microplate wells precoated with anti-MMP-2 antibody. Any MMP-2 present will be bound to the wells, other components of the sample being removed by washing and aspiration. Either the endogenous levels of free active MMP-2, or the total levels of free MMP-2 in a sample, can be detected. In order to measure the total MMP-2 content, any bound MMP-2 in its pro form is activated using p-aminophenylmercuric acetate (APMA). The standard is pro MMP-2 which is activated in parallel for both types of sample. Active MMP-2 is detected without APMA treatment. The resultant colour is read at 405 nm in a microplate spectrophotometer. The concentration of active MMP-2 in a sample is determined by interpolation from a standard curve. Each pack contains reagents for 96 determinations. This allows the construction of a standard curve plus the measurement of 42 samples in duplicate. The Biotrak^™ MMP-2 activity assay has been specifically designed for research purposes.

Matrix Metalloproteinase-2, Biotrak^™ Assay.

Matrix metalloproteinase-2 (MMP-2), also known as gelatinase or type IV collagenase, is a 72 kDa protein. MMP-2 is a member of matrix metalloproteinase (MMP) family of enzymes. The basic structure of MMP2 contains a signal peptide domain that targets the enzyme for secretion, the pro-peptide domain, which is removed when the enzyme is activated and the catalytic site containing gelatin-binding domain.

Matrix metalloproteinase-2 (MMP-2) cleaves gelatin, type IV, V, VII, X, and XI collagens, fibronectin, elastin, laminin, proteoglycans and a range of non-extracellular matrix (ECM) components. Both MMP-2 and MMP9 play an essential role in matrix degradation and they are implicated in the maintenance of neovascularization. MMP-2 activity is associated with human ovarian follicular development. Its expression is elevated in human myocardial infarction and dilated cardiomyopathy. Wound fluid from chronic leg ulcers show elevated expression of MMP2. Overexpression of active MMP-2 affects wound healing in chronic leg ulcers. MMP2 activity is inhibited by tissue inhibitor of metalloproteinase-2 (TIMP-2). Human follicular fluid MMP-2 level acts as a potential biomarker of oocyte maturation in in vitro fertilization and intracytoplasmic sperm injection (ICSI) cycles.

To view the Certificate of Analysis for this product, please visit www.cytiva.com.

Biotrak MMP-2 and TIMP-2 Human ELISAs
These products are manufactured by FUJI CHEMICAL INDUSTRIES, Ltd. (Japan).

Biotrak is a trademark of Cytiva