Recombinant Human Decorin

Decorin is a small, ubiquitous cellular or pericellular matrix proteoglycan that belongs to the small leucine-rich proteoglycan (SLRP) family. It has a protein core containing leucine repeats with a glycosaminoglycan chain consisting of either chondroitin sulfate or dermatan sulfate. As a component of connective tissue, decorin interacts with several extracellular matrix components, such as type I collagen and fibronectin, and plays a role in matrix assembly (1). The decorin core protein also binds to interact with thrombospondin, C1q, EGFR, TGF beta and the decorin endocytosis receptor. It is capable of suppressing the growth and the metastasis of a wide range of cancer cells in vitro through attenuation of the EGFR -mediated intracellular signaling and induction of apoptosis (2). Multiple alternatively spliced transcript variants for the decorin gene have been described. Mutations or deficiency of the decorin gene are associated with Marfan syndrome (3). It is believed that decorin also plays a role in the cell cycle of chondrocytes.

The biological activity of Human Decorin was determined by its ability to modulate collagen fibrillogenesis (Ge, G. et al., 2004, J. Biol. Chem. 279:41626). At 5 μg/ml, rhDecorin can significantly delay the rate of type I collagen fibrillogenesis.

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Gly17

Lyophilized

The predicted molecular weight of Recombinant Human DCN is Mr 38 kDa. However, the actual molecular weight as observed by migration on SDS-PAGE is Mr 40-42 kDa.

38

This recombinant protein was 0.2 µm filtered and lyophilized from modified Dulbecco’s phosphate buffered saline (1X PBS) pH 7.2 – 7.3 with no calcium, magnesium, or preservatives.

This lyophilized protein is stable for six to twelve months when stored desiccated at -20°C to -70°C. After aseptic reconstitution, this protein may be stored at 2°C to 8°C for one month or at -20°C to -70°C in a manual defrost freezer. Avoid Repeated Freeze Thaw Cycles. See Product Insert for exact lot specific storage instructions.

Next Day Ambient

1. Iozzo, RV. et al.(1997) J Cell Biol. 136(3):729-43.
2. Reed, CC. and Iozzo, RV. (2002) Glycoconj J. 19(4-5):249-55.