Abcam, ab213910, Rat MMP-2 ELISA Kit

Size: 1 x 96Tests
Rat MMP-2 ELISA Kit is a Sandwich (quantitative) ELISA for the measurement of Rat MMP-2 in Rat in Cell Culture Media, Biofluids samples.
Key facts
Detection method:Colorimetric,
Sample types:Cell culture supernatant, Heparin Plasma, Serum,
Reacts with:Rat,
Assay type:Sandwich (quantitative),
Sensitivity:< 10 pg/mL,
Range:625 - 40000 pg/mL,
Assay time:3h 30m,
Assay Platform:Pre-coated microplate (12 x 8 well strips)

Product details:
The MMP-2 Enzyme-Linked Immunosorbent Assay (ELISA) kit (ab213910) is designed for the quantitative measurement of MMP-2 in cell culture supernatants, serum and plasma (heparin).
The ELISA kit is based on standard sandwich enzyme-linked immune-sorbent assay technology. A monoclonal antibody from mouse specific for MMP-2 has been pre-coated onto 96-well plates. Standards and test samples are added to the wells; a biotinylated detection polyclonal antibody from goat specific for MMP-2 is added subsequently and then followed by washing with PBS or TBS buffer. Avidin-Biotin-Peroxidase Complex is added and unbound conjugates are washed away with PBS or TBS buffer. HRP substrate TMB is used to visualize HRP enzymatic reaction. TMB is catalyzed by HRP to produce a blue color product that changed into yellow after adding acidic stop solution. The density of yellow is proportional to the MMP-2 amount of sample captured in plate. The detected MMP-2 includes zymogen and active enzyme.
Type IV collagenase, 72-kD, is officially designated matrix metalloproteinase-2 (MMP2). It is also known as gelatinase, 72-kD. MMP-2 plays an essential role in angiogenesis and arteriogenesis, two processes critical to restoration of tissue perfusion after ischemia. MMP-2 expression is increased in tissue ischemia, but the responsible mechanisms remain unknown. Matrix metalloproteinases (MMPs) catalyze extracellular matrix degradation. Control of their activity is a promising target for therapy of diseases characterized by abnormal connective tissue turnover. MMPs are expressed as latent proenzymes that are activated by proteolytic cleavage that triggers a conformational change in the propeptide (cysteine switch). The structure of proMMP-2 reveals how the propeptide shields the catalytic cleft and that the cysteine switch may operate through cleavage of loops essential for propeptide stability. The gene is localized to 16q21 using somatic cell hybrids and in situ hybridization.

Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C, Storage information--20°C

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
The MMP-2 protein also known as matrix metalloproteinase-2 or gelatinase A is an enzyme involved in the breakdown of extracellular matrix components. It plays a critical role in tissue remodeling and cell migration. Comprised of a molecular weight of approximately 72 kDa this metalloproteinase is secreted as an inactive proenzyme that requires activation. MMP2 is expressed in various tissues including the brain heart and blood vessels where it contributes to normal physiological processes and pathological conditions.
Biological function summary
Matrix metalloproteinase-2 is mainly involved in the degradation of type IV and V collagens gelatin and fibronectin. As part of the metalloproteinase family it works alongside other MMPs to maintain tissue homeostasis and repair. MMP-2 forms part of a complex network that ensures the timely degradation of matrix components balancing synthesis and breakdown. It remains regulated by tissue inhibitors of metalloproteinases (TIMPs) preventing excessive degradation that could lead to tissue damage.
Pathways
MMP-2 plays a significant role within the extracellular matrix (ECM) remodeling and angiogenesis pathways. It interacts with various proteins including integrins and TIMP-2 to modulate cellular behaviors such as migration and invasion. MMP-2 contributes to processes like wound healing and embryonic development through its involvement in ECM degradation and new tissue formation.
Matrix metalloproteinase-2 is linked to cancer progression and cardiovascular diseases. In cancer abnormal MMP-2 activity facilitates tumor invasion and metastasis by breaking down matrix barriers. Increased MMP-2 expression associates with poor prognosis in cancers like breast and prostate. In cardiovascular diseases such as atherosclerosis it contributes to plaque destabilization and vascular remodeling. The imbalance in MMP-2 activity and its regulation by proteins like TIMP-1 are involved in the pathology of these disorders.