Sandwich ELISA, HRP-labelled antibody
At ambient temperature. Upon receipt, store the product at the temperature recommended below.
Store the complete kit at 2–8°C. Under these conditions, the kit is stable until the expiration date (see label on the box).
0.2 – 10 ng/ml
Limit of Detection
n = 8, CV = 4.6%
n = 6, CV = 8.9%
- It is intended for research use only
- The total assay time is less than 3 hours
- The kit measures human matrix metalloproteinase-3 in human serum and saliva.
- Assay format is 96 wells
- Standard is recombinant protein based
- Components of the kit are provided ready to use, concentrated or lyophilized
Bone and cartilage metabolism, Cardiovascular disease, Coronary artery disease, Oncology
Matrix metalloproteinases (MMPs) are a group of enzymes engaged in the degradation and remodeling of extracellular matrix (ECM). Nowadays six groups of these enzymes have been distinguished (collagenases, gelatinases, stromelysins, matrilysins, membrane-type, and a sixth group encompassing several other MMPs not classified in the previous categories), differing in structure, cellular localization, and substrate specificity. Since these enzymes are involved in connective tissue remodeling occurring in the course of morphogenetic processes, therefore, they are a subject of a very strict regulation, which is executed, among others, by the expression of their specific inhibitors—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-α, 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-β 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 stat. 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.MMP-3 hydrolyzes components of the extracellular matrix like proteoglycan, laminin, fibronectin, gelatin and collagen types III, IV and IX. It also activates pro-MMP-9 and pro-MMP-8 and superactivates plasmin activated MMP-1. MMP-3 is secreted as a latent proenzyme and is activated by a variety of proteinases, e.g. plasmin, trypsin, chymotrypsin, cathepsin G or human neutrophil elastase. MMP-3 was found to be capable of activating the precursor of IL1-beta.