Matrilin-4 / Unconjugated /
Product Details
| Description | Matrilin (MATNs) are a family of non-collagenous extracellular matrix proteins consisting of four known members that have been proposed to play key roles in the formation of both collagen-dependent and collagen-independent filamentous networks. Members of the matrilin family all share a structure made up of von Willebrand factor A domains, epidermal growth factor-like domains and a coiled coil alpha-helical module. MATN1 and MATN3 are expressed mainly in cartilage, while MATN2 and MATN4 occur in a wide variety of extracellular matrices such as embryonic kidney, lung, bone, cartilage and nervous system. The matrilin genes are strictly and differently regulated and their expression may serve as markers for cellular differentiation. MATN4 could serve as an odontoblast differentiation marker, e.g. in odontoblast stem cell research. | |
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| Conjugate | Unconjugated | |
| Clone | ||
| Target Species | Human, Mouse, Rat | |
| Applications | ELISA, WB, IHC | |
| Supplier | Aviva Systems Biology | |
| Catalog # | Sign in to view product details, citations, and spectra | |
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About Matrilin-4
This gene encodes a member of von Willebrand factor A domain-containing protein family. The proteins of this family are thought to be involved in the formation of filamentous networks in the extracellular matrices of various tissues. This family member is thought to be play a role in reorganizing and regenerating the corneal matrix in granular and lattice type I dystrophies. It may also be involved in wound healing in the dentin-pulp complex. Alternative splicing results in multiple transcript variants. [provided by RefSeq, May 2013]
This gene encodes a member of von Willebrand factor A domain-containing protein family. The proteins of this family are thought to be involved in the formation of filamentous networks in the extracellular matrices of various tissues. This family member is thought to be play a role in reorganizing and regenerating the corneal matrix in granular and lattice type I dystrophies. It may also be involved in wound healing in the dentin-pulp complex. Alternative splicing results in multiple transcript variants. [provided by RefSeq, May 2013]
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