Mouse Matrilin‑4 Alexa Fluor™ Plus 488‑conjugated Antibody

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 (1). 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 (2, 3). 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 (3, 4). 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 (5, 6). 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 (6). Functions and distributions of Matrilins overlap enough so that knockouts of Matrilins 1, 2 and 3 lack obvious phenotypes (1).