ADAM10 Selective Substrate (Fluorogenic) – PEPMCA001

Specifications and Use

Fluorescent Substrate: MCA-PRYEAYKMGK(DNP)-NH2

Catalog Number:          PEPMCA001, 1mg, 150 USD

Catalog Number:          PEPMCA001m005, 5mg, 500 USD

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Use:

This ADAM10 substrate is extremely selective and is used only to assess activity of ADAM10. The ADAM10 substrate has a kcat/Km of 3 x 104M-1s-1 making it the most sensitive one available on the market. The ADAM10  substrate does not process any ADAM or MMP family members except for ADAM10. The ADAM10 substrate is based on the TENtide sequence discussed in “Active site determinants of substrate recognition by the metalloproteinases TACE and ADAM10. Biochemical Journal, Cristina I. Caescu, Grace R. Jeschke, and Benjamin E. Turk (2009), 424(1), 79-88″.   For information concerning its substrate specificity profile, see our Product Sheets. Typically, the ADAM10 substrate is dissolved in DMSO to make a stock solution of about 2mM concentration. When used for in vitro assays, the substrate is often used at about 2uM concentration. Remember to keep the DMSO concentration in the final reaction at 1% or below, to avoid DMSO effects on the reaction, and remember to have an equivalent percentage of DMSO in the background wells. For use with ADAM 10, the buffer should consist of 25mM Tris, pH 8, 6 x 10-4 Brij detergent, and 10mM CaCl2. Excitation and emission wavelengths are 325 and 393 nm respectively.

 

Molecular Weight:

1623.8 g/mol

Purity:

Greater than 94% as assessed by HPLC and Mass Spectrometry.

Solubility:

1 mg/ml in water with 30% ACN

Appearance:

Yellow lyophilized powder

Counter Ion:

Trifluoroacetate

Shipping:

The peptide powder is shipped at room temperature.

Storage:

Upon receiving, the peptide should be stored at -20 oC or lower. If dissolved in liquid (such as DMSO), aliquot into separate tubes to minimize the number of freeze-thaw cycles.

Stability:

Samples are sensitive to light and stable up to 6 months at -20oC.

References:

Active site determinants of substrate recognition by the metalloproteinases TACE and ADAM10. Biochemical Journal, Cristina I. Caescu, Grace R. Jeschke, and Benjamin E. Turk (2009), 424(1), 79-88.