Anti-Human Decorin (Clone 115402)

Purified Recombinant Human Decorin (Accession # NP_598013.1)

This monoclonal antibody has been 0.2 µm filtered and lyophilized from modified Dulbecco's phosphate buffered saline (1X PBS) pH 7.2 - 7.3 containing 5.0% w/v trehalose with no calcium, magnesium or preservatives present.

The lyophilized antibody can be stored desiccated at -20°C to -70°C for up to twelve months. The reconstituted antibody can be stored for at least four weeks at 2-8°C. For long-term storage of the reconstituted antibody, aseptically aliquot into working volumes and store at -20°C to -70°C in a manual defrost freezer. Avoid repeated freeze thaw cycles. No detectable loss of activity was observed after six months.

Next Day Ambient

IHC (NBF/Par.): This antibody should give satisfactory staining results when used at a concentration of 25 µg/ml. The recommended secondary antibody for IHC is PN:M114. For chromogenic detection with high signal and low background use PN:D100 or PN:K107.

Mouse Anti-Human Decorin (Clone 115402) recognizes an epitope on Human Decorin and does not cross-react with recombinant mouse Decorin. This monoclonal antibody was purified using multi-step affinity chromatography methods such as Protein A or G depending on the species and isotype.

Decorin is a small cellular or pericellular matrix proteoglycan that belongs to the small leucine-rich proteoglycan (SLRP) family and consists of a protein core containing leucine repeats with a glycosaminoglycan chain consisting of either chondroitin sulfate or dermatan sulfate. It is known for its ability to bind, via its core protein, to interstitial collagens.
Decorin has been shown to have anti-tumorigenic properties in an experimental murine tumor model and is capable of suppressing the growth of various tumor cell lines. It is also shown as a powerful and effective therapeutic agent against breast cancer due to its inhibition of both primary tumor growth and metastatic spreading.

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.