Abcam, ab213811, Human MMP-12 ELISA Kit

Size: 1 x 96Tests
Human MMP-12 ELISA Kit is a Sandwich (quantitative) ELISA for the measurement of Human MMP-12 in Human in Cell Culture Media, Biofluids samples.
Key facts
Detection method:Colorimetric,
Sample types:Cell culture supernatant, Heparin Plasma, Serum,
Reacts with:Human,
Assay type:Sandwich (quantitative),
Sensitivity:< 10 pg/mL,
Range:62.5 - 4000 pg/mL,
Assay time:3h 30m,
Assay Platform:Pre-coated microplate (12 x 8 well strips)

Product details:
The Human MMP-12 Enzyme-Linked Immunosorbent Assay (ELISA) kit (ab213811) is designed for the quantitative detection of Human MMP-12 in cell culture supernatants, serum and plasma (heparin).
The ELISA kit is based on standard sandwich enzyme-linked immunosorbent assay technology. A monoclonal antibody from mouse specific for MMP-12 has been pre-coated onto 96-well plates. Standards (Expression system for standard: NSO; Immunogen sequence: L17-C470) and test samples are added to the wells, a biotinylated detection polyclonal antibody from goat specific for MMP-12 is added subsequently and then followed by washing with PBS or TBS buffer. Avidin-Biotin-Peroxidase Complex was added and unbound conjugates were washed away with PBS or TBS buffer. HRP substrate TMB was used to visualize HRP enzymatic reaction. TMB was 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 Human MMP-12 amount of sample captured in plate.
Matrix metalloproteinase-12 (MMP12), also known as MME or ME, is an enzyme that in humans is encoded by the MMP12 gene. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.2. It is thought that the protein encoded by this gene is cleaved at both ends to yield the active enzyme, but this processing has not been fully described. The enzyme degrades soluble and insoluble elastin. It may play a role in aneurysm formation and studies in mice suggest a role in the development of emphysema. This gene may be involved in tissue injury and remodeling.

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.
Matrix metallopeptidase 12 commonly known as MMP12 or macrophage elastase is an enzyme with a molecular mass of approximately 54 kDa. Found mainly in macrophages MMP12 belongs to the matrix metallopeptidase family. It functions to break down extracellular matrix proteins specifically elastin. Besides macrophages it sees expression in other tissues including the lungs and skin but it holds particular importance in immune cell-related environments.
Biological function summary
MMP12 plays an important role in tissue remodeling and repair processes. It interacts with other proteases within the extracellular matrix. The degradation of elastin by MMP12 contributes to structural organization and it participates in immune response modulation. As part of the matrix metalloproteinase family MMP12 takes part in the larger proteolytic system which comprises multiple enzymes working in concert.
Pathways
MMP12 is an essential factor in the extracellular matrix degradation pathway. This pathway regulates tissue remodeling and inflammatory response. MMP12 independently breaks down elastin while it interacts with proteins like MMP2 and MMP9 which assist in remodeling processes. It also contributes to the regulation of cytokines that orchestrate immune functions.
Overexpression of MMP12 is strongly linked to chronic obstructive pulmonary disease (COPD) and atherosclerosis. In COPD MMP12's breakdown of elastin contributes to tissue damage in the lung. In atherosclerosis the enzyme accelerates plaque destabilization impacting cardiovascular health. Additionally MMP12 shares functional relationships with proteins such as TIMPs (tissue inhibitors of metalloproteinases) which regulate its activity and play roles in disease pathogenesis.