DCN Mouse

The mouse Decorin protein is encoded by a cDNA that translates into a 354 amino acid precursor, which includes a 16 amino acid signal sequence and a 14 amino acid propeptide . The mature mouse Decorin contains twelve tandem LRRs and shares 80% and 87% amino acid sequence identity with human and rat Decorin, respectively . Decorin is an N-glycosylated protein that also carries a variably-sized hybrid chondroitin/dermatan sulfate chain at Ser34 .

Decorin is known for its ability to modulate collagen fibrillogenesis. It regulates the assembly of the extracellular collagen matrix and the bioactivity of matrix-associated growth factors such as FGF-2, GDF-8/Myostatin, TGF-beta, and WISP-1 . The activity of Decorin is measured by its ability to delay the rate of collagen fibrillogenesis, with studies showing that 5 µg/mL of recombinant mouse Decorin can significantly delay this process .

Recombinant mouse Decorin is typically produced using a mouse myeloma cell line, NS0-derived mouse Decorin protein, with a C-terminal 10-His tag . The protein is purified to a high degree, with a purity greater than 90% as determined by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining . The endotoxin level is kept below 0.10 EU per 1 µg of the protein by the LAL method .

Recombinant mouse Decorin is used in various research applications, particularly in studies related to extracellular matrix biology and collagen-related processes. It is also used to investigate the regulatory mechanisms of growth factors and their interactions with the extracellular matrix .

The recombinant mouse Decorin protein is typically lyophilized from a 0.2 μm filtered solution in PBS and should be reconstituted at 100 μg/mL in sterile PBS . It is shipped at ambient temperature and should be stored at -20 to -70 °C to maintain stability. After reconstitution, it can be stored at 2 to 8 °C for up to one month under sterile conditions, or at -20 to -70 °C for up to three months .

Decorin’s role in modulating collagen fibrillogenesis and its interactions with growth factors make it a valuable tool in the study of extracellular matrix biology and related fields.