Description
This Mouse Matrilin 4 ELISA Kit is intended for quantitative detection of mouse Matrilin-4 in cell culture supernates, serum and plasma (heparin, EDTA). Strip well format. Reagents for up to 96 tests.
This mouse Matrilin-4 ELISA Kit is based on standard sandwich enzyme-linked immune-sorbent assay technology. A monoclonal antibody from rat specific for Matrilin-4 has been precoated onto 96-well plates. Standards (Expression system for standard: NSO, Immunogen sequence: Q22-K624) and test samples are added to the wells, a biotinylated detection polyclonal antibody from goat specific for Matrilin-4 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 are 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 mouse Matrilin-4 amount of sample captured in plate.
The capture antibody is a monoclonal antibody from rat, the detection antibody is a biotinylated polyclonal antibody from goat. Expression system for standard: Matrilin-4 is a 73 kDa secreted glycoprotein that is a member of the matrilin family of the von Willebrand Factor-A (vWA) domain-containing superfamily. This gene is mapped to 2 H3; 2 85.16 cM. Matrilins are modular extracellular matrix proteins that serve as adaptors and linkers for other matrix proteins. Matrilin-4, like Matrilin-2, has a broad distribution in both cartilage and in loose connective tissue such as dermis, lung and kidney, while Matrilins 1 and 3 are limited to cartilage. Matrilin-4 is present in nervous tissue and is abundant in the brain. Mature mouse Matrilin-4 shares 98%, 90%, 89% and 66% amino acid (aa) identity with rat, human, canine and chicken Matrilin-4, respectively. The 624 aa mouse Matrilin-4 contains a 22 aa signal sequence, two potential glycosylation sites, and four cysteine-rich EGF-like domains placed between two vWA domains. A short isoform lacks the N-terminal vWA domain (aa 28-217). A C-terminal alpha-helix/coiled-coil region (aa 590-623) by which multimers are formed is often proteolytically removed so that Matrilin-4 is found as a mixture of monomers with homo- or hetero- dimers and trimers. Matrilin-4 forms multimers with Matrilins 1 and 2 but not with Matrilin-3. The N-terminal vWA domains of Matrilins associate with collagen IV microfibrils via the proteoglycans biglycan and decorin, linking the fibrils with other matrix constituents aggrecan and collagen II. Matrilins also show calcium-dependent binding to the cartilage oligomeric matrix protein (COMP); this interaction is of high affinity for oligomeric Matrilin-4 and somewhat lower affinity for monomeric Matrilin-4. Functions and distributions of Matrilins overlap enough so that knockouts of Matrilins 1, 2 and 3 lack obvious phenotypes