Technical Data
ADAMTS5, Recombinant, aa832-930, GST-Tag (Aggrecanase 2 A Disintegrin And Metalloproteinase with ThromboSpondin-3 motif)
Molecular Biology Storage: -70CShipping: Dry Ice
Aggrecanases are glutamyl-specific multidomain metalloproteinases of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) family. They hydrolyze aggrecan, the major proteoglycan of articular cartilage, causing osteoarthritis and other joint diseases. Recent studies using knockout mice have indicated that ADAMTS-5 (aggrecanase-2) plays an essential role in aggrecan degradation in mice.


Length with Tag: 332 aa with GST Tag

Molecular Weight: 36.52kD

Suitable to be used to study the degradation of extracellular matrix proteoglycans, to screen for inhibitors of proteoglycan hydrolysis and to characterize inhibitor actions. The enzyme can also serve as standard in enzymatic and immunological assays.

ADAMTS 5 is inhibited by tissue inhibitor of matrix metalloproteinase 3 (TIMP3) and by alpha2-macroglobulin. Enzyme activity is also suppressed by chelators of divalent cations such as EDTA and by synthetic metalloproteinase inhibitors.

Storage and Stability:
Aliquot to avoid repeated freezing and thawing and freeze at -70C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Aliquots are stable for at least 3 months.
Source: Recombinant human ADAMTS-5 is produced with the baculo-virus expression system and purified from insect cell culture supernatants.
Purity: Glutathione Sepharose 4 Fast Flow. 12.5% SDS-PAGE Stained with Coomassie Blue.
Concentration: ~0.1mg/ml
Form: Supplied as a liquid in 50 mM Tris-HCI, 10 mM reduced Glutathione, pH8 in the elution buffer.

Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.