Product Overview
The Carboxyfluorescein Multi-Caspase Activity Kit detects apoptosis through the covalent binding of a green fluorescent probe to active caspase enzymes in living cells. The carboxyfluorescein-labeled caspase inhibitor probe (FAM-VAD-FMK; excitation at 490 nm and emission at 520 nm), comprising a carboxyfluorescein derivative of valylalanylaspartic acid fluoromethyl ketone (VAD-FMK), covalently binds to the reactive cysteine (Cys 285) on the large subunit of active caspase heterodimers. This probe is both cell permeable and non-cytotoxic during the time of the labeling procedure and allows detection of apoptosis by fluorescence microscopy, flow cytometry, and 96-well-plate based fluorometry. Use of the fluorescence microscope provides a qualitative view of the level of apoptosis induced as compared to the use of a fluorometer or a flow cytometer which will generate quantitative data. The Sulforhodamine Multi-Caspase Activity Kit for Apoptosis Detection is a related kit that contains a sulforhodamine-labeled probe (Ex: 550, Em: 595).
Features
Ready-to-use product, accelerating research progress, enhancing application performance.
Applications
Research Use
Storage
Store the unopened kit (and each unopened component) at 2-8°C until the expiration date. Protect the FAM-VAD-FMK reagent from light at all times. Once reconstituted, the 150X FAM-VAD-FMK stock should be stored at -20°C protected from light. This reagent is stable for up to 6 months and may be thawed twice during that time.
Instruction
RUO - Research Use Only
Shipping
Shipped on Blue Ice
Recommendation
Colorimetric detection, HTS,Activity assay
Contents
FAM-VAD-FMK Reagent, 10X Wash Buffer, Fixative, Propidium Iodide.
Compatibility
This product is compatible with the Absorbance 96 Plate Reader.
Specification
Standard Specifications
Description
Caspases are a group of proteases with similar structure present in the cytoplasm.An important common denominator is that they all contain cysteines in their active sites, which are able to specifically cleave peptide bonds on aspartic acid residues of target proteins, allowing caspases to cleave certain proteins with a high degree of selectivity. This cleavage occurs at only a few (usually only 1) sites, mainly at sites between structural domains, and results in either activation or inactivation of a protein, but never complete degradation of a protein.Caspases are responsible for the selective cleavage of certain proteins that cause apoptosis, and they play an important role in programmed cell death (including apoptosis, apoptosis and necroptosis) and inflammation.
