| New Fluorescence-Quenching
Substrate for ADAM17/TNF-alpha Converting Enzyme (TACE) New substrate
now available from Peptides International |
The use of fluorescence quenching peptide substrates for the
determination of protease enzyme activity is now widely used for screening new potential
therapeutic protease inhibitors. Particularly, continuous assays are especially desirable
for the collection of enzyme activity data. The specificity of such substrates is critical
in the tandem development of a specific inhibitor of interest. The inhibition of Tumor
Necrosis Factor-a
Converting Enzyme (TACE/ADAM17) is of particular importance since TNF-a is a key immunomodulator
involved in the protective inflammatory response. Release of the mature TNF-a cytokine occurs when TACE
cleaves the membrane-anchored 233-residue precursor between Ala76 and Val77.
Overproduction of TNF-a can lead to severe tissue damage as seen in chronic rheumatoid arthritis.
Existing assay methods for the determination of TACE activity based on HPLC are
non-continuous and time consuming. Our new specific substrate developed will allow for the
accurate determination of TACE activity and also help monitor the effectiveness and
specificity of potential inhibitors.
G. Jin, X. Huang, R.
Black, M. Wolfson , C. Rauch, H. McGregor, G. Ellestad, R. Cowling, Anal. Biochem., 302,
269-275 (2002).
|
| Reaction conditions used (taken from G. Jin, X. Huang, et
al.)
Increase in fluorescence can be monitored at lex =
320 nm and lem
= 420 nm |
| new substrate for tace |
