DAPA
| 9-DAPA | Vial | 1 mg |
Formulation : Dansylarginin, N-(3-ethyl-1.5-pentanediyl)amid, HCl C25H39O3N6SCl
DAPA is routinely used as a protease inhibitor during the isolation of proteins that are susceptible to thrombin cleavage. Furthermore, by eliminating the feedback of thrombin activity during prothrombin activation, the isolation of reaction intermediates such as fragment 1.2, and meizothrombin have been made possible
Description of the DAPA
MW(Da) : 539 and Extinction coef. : 4010
Dansylarginine N-(3-ethyl-1,5-pentanediyl)amide, more commonly referred to as DAPA, is a potent (Ki=10-7M) and specific synthetic thrombin inhibitor. Of special interest are the unique fluorescent properties contributed by the dansyl moiety of DAPA. When bound to thrombin, the fluorescence intensity and lifetime of the dansyl moiety are increased three fold. The enhancement of fluorescence intensity, coupled with its inhibitory properties, have made this compound extremely useful for studies involving thrombin generation. In addition to an increase in fluorescence intensity and lifetime, there is a decrease in depolarization of the excitation signal which also supports fluorescence polarization studies
- Bos, M., et al., Blood. 2009 114: 686-692.
- Majumder, R., et al., Blood. 2008 112: 2795-2802.
Advantages
Supplied frozen -80°C. Expiry date > 1 year. Glass vial or plastic tubes. Discount according to quantities.
Informations
DAPA is synthesized according the procedure described by Nesheim, et al. HPLC, TLC and spectral analyses are used to determine the purity of the final product. DAPA is supplied in water. When properly stored at -20°C and protected from light, the compound is stable for many years.
Detection and determination of proteinases, studies on their interactions with substrates and effectors and the investigation of their physiological role are greatly facilitated by the use of proteinase inhibitors. In this context, especially synthetic, low-molecular weight inhibitors of different selectivity are very useful. They are widely applied during purification and characterization of proteinases. Furthermore, synthetic inhibitors are useful tools for suppression of undesired proteolytic activity. Depending upon the manner in which the inhibitor is attached to the enzyme, one distinguishes reversible and irreversible inhibitors.
