Calpain Substrate, Fluorogenic, (Z-AA)2Rh110 – 5 mg

Overview

When precision and sensitivity matter in protease studies, the Calpain Substrate, Fluorogenic, (Z-AA)2Rh110 is your go-to choice. This fluorogenic calpain substrate transforms from a colorless, nonfluorescent compound into a highly fluorescent product, rhodamine 110, upon hydrolysis. Its remarkable sensitivity outperforms traditional AMC/AFC-based substrates, making it an essential reagent for researchers focusing on calpain activity.

Key Features

• Fluorogenic calpain substrate with high sensitivity
• Transformative hydrolysis yielding brightly fluorescent rhodamine 110
• Excellent spectral properties for optimal instrument detection
• Ideal for protease activity assays
• Easy to incorporate into various experimental protocols

Specifications

FAQ

What is the main application of (Z-AA)2Rh110?

(Z-AA)2Rh110 is primarily used as a highly sensitive substrate for calpain activity assays. Its ability to fluoresce upon hydrolysis allows for the detection of calpain enzymes in various biological samples.

How does the sensitivity of (Z-AA)2Rh110 compare to other substrates?

This substrate demonstrates superior sensitivity when compared to traditional AMC/AFC-based substrates. The enhanced fluorescence of the enzymatic product significantly improves detection limits, making it ideal for challenging samples.

Can (Z-AA)2Rh110 be used in live-cell imaging?

While (Z-AA)2Rh110 is designed for assaying protease activity, its fluorescent product may have applications in live-cell imaging, provided that appropriate controls are in place to manage potential interference.

Whether you’re studying calpain’s role in cellular processes or developing new assays, the Calpain Substrate, Fluorogenic, (Z-AA)2Rh110 is an excellent addition to your research toolkit. Explore its capabilities alongside other innovative products like our PKG SubstrateAutocamtide-2and CREBtide. Experience the difference in calpain detection with this advanced substrate.

Browse more in Peptides.