Descrition & Target

Casein, FITC-conjugated

Descrition & Target

Casein, TAMRA-conjugated

Descrition & Target

Caspase-3 DEVD-R110 Fluorometric HTS Assay Kit is specifically designed for HTS-based assays. The kit provides a homogenous assay system for fast and highly sensitive detection of caspase-3 activity by fluorescence in enzymatic reaction or mammalian cells. The fluorogenic substrate (Ac-DEVD)₂-R110 contains two DEVD tetrapeptides and is completely hydrolyzed by the enzyme in two successive steps. Cleavage of the first DEVD peptide results in the monopeptide Ac-DEVD-R110 intermediate, which has absorption and emission wavelengths similar to those of R110 (Ex/Em= 496/520 nm) but has only about 10% of the fluorescence of the latter. Hydrolysis of the second DEVD peptide releases the dye R110, leading to a substantial fluorescence increase.

The assay kit includes Ac-DEVD-CHO, which is a caspase-3 inhibitor and can be used as a negative control. Also, R110 is provided in the kit for generating a standard curve, which can be used for quantifying caspase-3 activity. One mL cell lysis/assay buffer is sufficient for 10 assays in 96-well format.

Note: While caspase-3 preferentially cleaves the consensus sequence DEVD compared to other substrate sequences, other caspases also can cleave DEVD efficiently. Overlapping caspase substrate recognition limits the usefulness of caspase substrate peptides for distinguishing between different caspase activities in cell lysates.

<strong>Kit Components: </strong>
<ul>
<li>Cell lysis/assay buffer</li>
<li>Enzyme substrate (Ac-DEVD)₂-R110</li>
<li>Enzyme inhibitor Ac-DEVD-CHO</li>
<li>R110</li>
</ul>
<strong>Features:</strong>
<ul>
<li><b>HTS-compatible:</b> Single-step homogenous assay specifically designed for HTS-based detection.</li>
<li><b>Fast:</b> Fast enzyme kinetics.</li>
<li><b>Sensitive:</b> Green fluorescent readout</li>
</ul>
For real-time detection of caspase-3 activity in intact cells, see our novel NucView&reg; Caspase-3 Substrates.

Descrition & Target

Caspase-3 DEVD-R110 Fluorometric HTS Assay Kit is specifically designed for HTS-based assays. The kit provides a homogenous assay system for fast and highly sensitive detection of caspase-3 activity by fluorescence in enzymatic reaction or mammalian cells. The fluorogenic substrate (Ac-DEVD)₂-R110 contains two DEVD tetrapeptides and is completely hydrolyzed by the enzyme in two successive steps. Cleavage of the first DEVD peptide results in the monopeptide Ac-DEVD-R110 intermediate, which has absorption and emission wavelengths similar to those of R110 (Ex/Em= 496/520 nm) but has only about 10% of the fluorescence of the latter. Hydrolysis of the second DEVD peptide releases the dye R110, leading to a substantial fluorescence increase.

The assay kit includes Ac-DEVD-CHO, which is a caspase-3 inhibitor and can be used as a negative control. Also, R110 is provided in the kit for generating a standard curve, which can be used for quantifying caspase-3 activity. One mL cell lysis/assay buffer is sufficient for 10 assays in 96-well format.

Note: While caspase-3 preferentially cleaves the consensus sequence DEVD compared to other substrate sequences, other caspases also can cleave DEVD efficiently. Overlapping caspase substrate recognition limits the usefulness of caspase substrate peptides for distinguishing between different caspase activities in cell lysates.

<strong>Kit Components: </strong>
<ul>
<li>Cell lysis/assay buffer</li>
<li>Enzyme substrate (Ac-DEVD)₂-R110</li>
<li>Enzyme inhibitor Ac-DEVD-CHO</li>
<li>R110</li>
</ul>
<strong>Features:</strong>
<ul>
<li><b>HTS-compatible:</b> Single-step homogenous assay specifically designed for HTS-based detection.</li>
<li><b>Fast:</b> Fast enzyme kinetics.</li>
<li><b>Sensitive:</b> Green fluorescent readout</li>
</ul>
For real-time detection of caspase-3 activity in intact cells, see our novel NucView&reg; Caspase-3 Substrates.

Descrition & Target

Caspase-3 DEVD-R110 Fluorometric HTS Assay Kit is specifically designed for HTS-based assays. The kit provides a homogenous assay system for fast and highly sensitive detection of caspase-3 activity by fluorescence in enzymatic reaction or mammalian cells. The fluorogenic substrate (Ac-DEVD)₂-R110 contains two DEVD tetrapeptides and is completely hydrolyzed by the enzyme in two successive steps. Cleavage of the first DEVD peptide results in the monopeptide Ac-DEVD-R110 intermediate, which has absorption and emission wavelengths similar to those of R110 (Ex/Em= 496/520 nm) but has only about 10% of the fluorescence of the latter. Hydrolysis of the second DEVD peptide releases the dye R110, leading to a substantial fluorescence increase.

The assay kit includes Ac-DEVD-CHO, which is a caspase-3 inhibitor and can be used as a negative control. Also, R110 is provided in the kit for generating a standard curve, which can be used for quantifying caspase-3 activity. One mL cell lysis/assay buffer is sufficient for 10 assays in 96-well format.

Note: While caspase-3 preferentially cleaves the consensus sequence DEVD compared to other substrate sequences, other caspases also can cleave DEVD efficiently. Overlapping caspase substrate recognition limits the usefulness of caspase substrate peptides for distinguishing between different caspase activities in cell lysates.

<strong>Kit Components: </strong>
<ul>
<li>Cell lysis/assay buffer</li>
<li>Enzyme substrate (Ac-DEVD)₂-R110</li>
<li>Enzyme inhibitor Ac-DEVD-CHO</li>
<li>R110</li>
</ul>
<strong>Features:</strong>
<ul>
<li><b>HTS-compatible:</b> Single-step homogenous assay specifically designed for HTS-based detection.</li>
<li><b>Fast:</b> Fast enzyme kinetics.</li>
<li><b>Sensitive:</b> Green fluorescent readout</li>
</ul>
For real-time detection of caspase-3 activity in intact cells, see our novel NucView&reg; Caspase-3 Substrates.

Descrition & Target

Caspase-3 is an active cell-death protease involved in the execution phase of apoptosis, during which cells undergo morphological changes such as DNA fragmentation, chromatin condensation and apoptotic body formation. Caspase-3 DEVD-R110 Fluorometric and Colorimetric Assay Kit provides a simple assay system for fast and highly sensitive detection of caspase-3 activity either by fluorescence or absorbance in mammalian cells. The fluorogenic and chromogenic substrate (Ac-DEVD)2-R110 contains two DEVD tetrapeptides and is completely hydrolyzed by the enzyme in two successive steps. Cleavage of the first DEVD peptide results in the monopeptide Ac-DEVD-R110 intermediate, which has absorption and emission wavelengths similar to those of R110 (Ex/Em= 496/520 nm) but has only about 10% of the fluorescence of the latter. Hydrolysis of the second DEVD peptide releases the dye R110, leading to a substantial fluorescence increase.

Although fluorometric detection of the end products is preferred because of the superior sensitivity, detection by absorbance is also possible. In fact, the extinction coefficient ofR110 is 10 times higher than that of p-nitroaniline (pNA), a dye commonly used in chromogenic substrates, making R110-based substrates significantly more sensitive than pNA-based substrates, even by colorimetric detection.

The assay kit includes Ac-DEVD-CHO, which is a caspase-3 inhibitor and can be used as a negative control. Also, R110 is provided in the kit for generating a standard curve, which can be used for quantifying caspase-3 activity.

Note: While caspase-3 preferentially cleaves the consensus sequence DEVD compared to other substrate sequences, other caspases also can cleave DEVD efficiently. Overlapping caspase substrate recognition limits the usefulness of caspase substrate peptides for distinguishing between different caspase activities in cell lysates.

<strong>Kit Components: </strong>
<ul>
<li>Cell lysis buffer</li>
<li>Assay buffer</li>
<li>Enzyme substrate (Ac-DEVD)2-R110</li>
<li>Enzyme inhibitor Ac-DEVD-CHO</li>
<li>R110</li></ul>

<strong>Features:</strong>
<ul><li><b>Fast: </b>Fast enzyme kinetics.</li>
<li><b>Sensitive: </b>The enzymatic reaction forms intensely yellow colored and highly green fluorescent rhodamine 110 (R110) product.</li>
<li><b>Versatile:</b> Compatible with both fluorometric and colorimetric detection systems.</li>
</ul>

9689c5aa-6556-4b3c-b5d1-1e693715ba07 also offers the Caspase-3 DEVD-R110 Fluorometric HTS Assay Kit, a one step homogenous assay for high throughput screening (HTS) using fluorescent-based measurement. For real-time detection of caspase-3 activity in intact cells, see our novel NucView&reg;488 Caspase-3 Substrate.

Descrition & Target

Caspase-3 is an active cell-death protease involved in the execution phase of apoptosis, during which cells undergo morphological changes such as DNA fragmentation, chromatin condensation and apoptotic body formation. Caspase-3 DEVD-R110 Fluorometric and Colorimetric Assay Kit provides a simple assay system for fast and highly sensitive detection of caspase-3 activity either by fluorescence or absorbance in mammalian cells. The fluorogenic and chromogenic substrate (Ac-DEVD)2-R110 contains two DEVD tetrapeptides and is completely hydrolyzed by the enzyme in two successive steps. Cleavage of the first DEVD peptide results in the monopeptide Ac-DEVD-R110 intermediate, which has absorption and emission wavelengths similar to those of R110 (Ex/Em= 496/520 nm) but has only about 10% of the fluorescence of the latter. Hydrolysis of the second DEVD peptide releases the dye R110, leading to a substantial fluorescence increase.

Although fluorometric detection of the end products is preferred because of the superior sensitivity, detection by absorbance is also possible. In fact, the extinction coefficient ofR110 is 10 times higher than that of p-nitroaniline (pNA), a dye commonly used in chromogenic substrates, making R110-based substrates significantly more sensitive than pNA-based substrates, even by colorimetric detection.

The assay kit includes Ac-DEVD-CHO, which is a caspase-3 inhibitor and can be used as a negative control. Also, R110 is provided in the kit for generating a standard curve, which can be used for quantifying caspase-3 activity.

Note: While caspase-3 preferentially cleaves the consensus sequence DEVD compared to other substrate sequences, other caspases also can cleave DEVD efficiently. Overlapping caspase substrate recognition limits the usefulness of caspase substrate peptides for distinguishing between different caspase activities in cell lysates.

<strong>Kit Components: </strong>
<ul>
<li>Cell lysis buffer</li>
<li>Assay buffer</li>
<li>Enzyme substrate (Ac-DEVD)2-R110</li>
<li>Enzyme inhibitor Ac-DEVD-CHO</li>
<li>R110</li></ul>

<strong>Features:</strong>
<ul><li><b>Fast: </b>Fast enzyme kinetics.</li>
<li><b>Sensitive: </b>The enzymatic reaction forms intensely yellow colored and highly green fluorescent rhodamine 110 (R110) product.</li>
<li><b>Versatile:</b> Compatible with both fluorometric and colorimetric detection systems.</li>
</ul>

9689c5aa-6556-4b3c-b5d1-1e693715ba07 also offers the Caspase-3 DEVD-R110 Fluorometric HTS Assay Kit, a one step homogenous assay for high throughput screening (HTS) using fluorescent-based measurement. For real-time detection of caspase-3 activity in intact cells, see our novel NucView&reg;488 Caspase-3 Substrate.

Descrition & Target

Caspase-8 IETD-R110 Fluorometric HTS Assay Kit is specifically designed for HTS-based assays. The kit provides a homogenous assay system for fast and highly sensitive detection of caspase-8 activity by fluorescence in enzymatic reaction or mammalian cells. The fluorogenic substrate (Ac-IETD)₂-R110 contains two IETD tetrapeptides and is completely hydrolyzed by the enzyme in two successive steps. Cleavage of the first IETD peptide results in the monopeptide Ac-IETD-R110 intermediate, which has absorption and emission wavelengths similar to those of R110 (λ_Ex/λ_Em = 496/520 nm) but has only about 10% of the fluorescence of the latter. Hydrolysis of the second IETD peptide releases the dye R110, leading to a substantial fluorescence increase.
<p class="style5 style11"><strong>Note:</strong> While caspase-8 preferentially cleaves the consensus sequence IETD compared to other substrate sequences, other caspases such as caspase-3 also can cleave IETD efficiently. Overlapping caspase substrate recognition limits the usefulness of caspase substrate peptides for distinguishing between different caspase activities in cell lysates.</p>
The assay kit includes Ac-IETD-CHO, which is a caspase-8 inhibitor and can be used as a negative control. Also, R110 is provided in the kit for generating a standard curve, which can be used for quantifying caspase-8 activity.
<p class="style5 style11"><strong>Kit Components: </strong></p>

<ul>
<li>Cell lysis/assay buffer</li>
<li>Enzyme substrate (Ac-IETD)2-R110</li>
<li>Enzyme inhibitor Ac-IETD-CHO</li>
<li>R110</li>
</ul>
<p class="style5 style11"><strong>Features:</strong></p>

<ul>
<li><b>HTS-compatible:</b> Single-step homogenous assay specifically designed for HTS-based detection.</li>
<li><b>Fast: </b>Fast enzyme kinetics.</li>
<li><b>Sensitive:</b> The enzymatic reaction forms intensely green fluorescent rhodamine 110 (R110) product.</li>
</ul>

Descrition & Target

Caspase-8 IETD-R110 Fluorometric HTS Assay Kit is specifically designed for HTS-based assays. The kit provides a homogenous assay system for fast and highly sensitive detection of caspase-8 activity by fluorescence in enzymatic reaction or mammalian cells. The fluorogenic substrate (Ac-IETD)₂-R110 contains two IETD tetrapeptides and is completely hydrolyzed by the enzyme in two successive steps. Cleavage of the first IETD peptide results in the monopeptide Ac-IETD-R110 intermediate, which has absorption and emission wavelengths similar to those of R110 (λ_Ex/λ_Em = 496/520 nm) but has only about 10% of the fluorescence of the latter. Hydrolysis of the second IETD peptide releases the dye R110, leading to a substantial fluorescence increase.
<p class="style5 style11"><strong>Note:</strong> While caspase-8 preferentially cleaves the consensus sequence IETD compared to other substrate sequences, other caspases such as caspase-3 also can cleave IETD efficiently. Overlapping caspase substrate recognition limits the usefulness of caspase substrate peptides for distinguishing between different caspase activities in cell lysates.</p>
The assay kit includes Ac-IETD-CHO, which is a caspase-8 inhibitor and can be used as a negative control. Also, R110 is provided in the kit for generating a standard curve, which can be used for quantifying caspase-8 activity.
<p class="style5 style11"><strong>Kit Components: </strong></p>

<ul>
<li>Cell lysis/assay buffer</li>
<li>Enzyme substrate (Ac-IETD)2-R110</li>
<li>Enzyme inhibitor Ac-IETD-CHO</li>
<li>R110</li>
</ul>
<p class="style5 style11"><strong>Features:</strong></p>

<ul>
<li><b>HTS-compatible:</b> Single-step homogenous assay specifically designed for HTS-based detection.</li>
<li><b>Fast: </b>Fast enzyme kinetics.</li>
<li><b>Sensitive:</b> The enzymatic reaction forms intensely green fluorescent rhodamine 110 (R110) product.</li>
</ul>

Descrition & Target

Caspase-8 IETD-R110 Fluorometric HTS Assay Kit is specifically designed for HTS-based assays. The kit provides a homogenous assay system for fast and highly sensitive detection of caspase-8 activity by fluorescence in enzymatic reaction or mammalian cells. The fluorogenic substrate (Ac-IETD)₂-R110 contains two IETD tetrapeptides and is completely hydrolyzed by the enzyme in two successive steps. Cleavage of the first IETD peptide results in the monopeptide Ac-IETD-R110 intermediate, which has absorption and emission wavelengths similar to those of R110 (λ_Ex/λ_Em = 496/520 nm) but has only about 10% of the fluorescence of the latter. Hydrolysis of the second IETD peptide releases the dye R110, leading to a substantial fluorescence increase.
<p class="style5 style11"><strong>Note:</strong> While caspase-8 preferentially cleaves the consensus sequence IETD compared to other substrate sequences, other caspases such as caspase-3 also can cleave IETD efficiently. Overlapping caspase substrate recognition limits the usefulness of caspase substrate peptides for distinguishing between different caspase activities in cell lysates.</p>
The assay kit includes Ac-IETD-CHO, which is a caspase-8 inhibitor and can be used as a negative control. Also, R110 is provided in the kit for generating a standard curve, which can be used for quantifying caspase-8 activity.
<p class="style5 style11"><strong>Kit Components: </strong></p>

<ul>
<li>Cell lysis/assay buffer</li>
<li>Enzyme substrate (Ac-IETD)2-R110</li>
<li>Enzyme inhibitor Ac-IETD-CHO</li>
<li>R110</li>
</ul>
<p class="style5 style11"><strong>Features:</strong></p>

<ul>
<li><b>HTS-compatible:</b> Single-step homogenous assay specifically designed for HTS-based detection.</li>
<li><b>Fast: </b>Fast enzyme kinetics.</li>
<li><b>Sensitive:</b> The enzymatic reaction forms intensely green fluorescent rhodamine 110 (R110) product.</li>
</ul>

Descrition & Target

Caspase-8 is the most upstream caspase in the CD95/Fas apoptotic pathway and is activated by the signaling pathways for CD95/Fas and TNF. Caspase-8 Fluorometric and Colorimetric Assay Kit provides a simple assay system for fast and sensitive detection of caspase-8 activity either by fluorescence or absorbance. The kit includes the fluorogenic substrate (Ac-IETD)₂-R110, the enzyme inhibitor Ac-IETD-CHO as a negative control, R110 as a standard and optimized lysis and assay buffers. The substrate(Ac-IETD)₂-R110 contains two IETD tetrapeptides and is completely hydrolyzed by the enzyme in a two-step process. Cleavage of the first IETD results in the monopeptide Ac-IETD-R110 intermediate, which has absorption and emission wavelengths similar to those of R110 (λ_Ex/λ_Em = 496/520 nm)but has only about 10% of the fluorescence of the latter. Hydrolysis of the second IETD peptide releases the dye R110, leading to a substantial fluorescence increase.

Although fluorometric detection of the end products is preferred because of the superior sensitivity, detection by absorbance is also possible. In fact, the extinction coefficient of R110 is 10 times higher than that of p-nitroaniline (pNA), a dye commonly used in chromogenic substrates, making R110-based substrates significantly more sensitive than pNA-based substrates, even by colorimetric detection.
<p class="style5 style11"><strong>Note:</strong> While caspase-8 preferentially cleaves the consensus sequence IETD compared to other substrate sequences, other caspases such as caspase-3 also can cleave IETD efficiently. Overlapping caspase substrate recognition limits the usefulness of caspase substrate peptides for distinguishing between different caspase activities in cell lysates.</p>
<p class="style5 style11"><strong>Kit Components: </strong></p>

<ul>
<li>Cell lysis buffer</li>
<li>Assay buffer</li>
<li>Enzyme substrate (Ac-IETD)2-R110</li>
<li>Enzyme inhibitor Ac-IETD-CHO</li>
<li>R110
<p class="style5 style11"><strong>Features:</strong></p>

<ul>
<li><b>Fast:</b> Fast enzyme kinetics.</li>
<li><b>Sensitive:</b> The enzymatic reaction forms intensely yellow colored and highly green fluorescent rhodamine 110 (R110) product.</li>
<li><b>Versatile: </b>Compatible with both fluorometric and colorimetric detection systems.</li>
</ul>
</li>
</ul>

Descrition & Target

Caspase-8 is the most upstream caspase in the CD95/Fas apoptotic pathway and is activated by the signaling pathways for CD95/Fas and TNF. Caspase-8 Fluorometric and Colorimetric Assay Kit provides a simple assay system for fast and sensitive detection of caspase-8 activity either by fluorescence or absorbance. The kit includes the fluorogenic substrate (Ac-IETD)₂-R110, the enzyme inhibitor Ac-IETD-CHO as a negative control, R110 as a standard and optimized lysis and assay buffers. The substrate(Ac-IETD)₂-R110 contains two IETD tetrapeptides and is completely hydrolyzed by the enzyme in a two-step process. Cleavage of the first IETD results in the monopeptide Ac-IETD-R110 intermediate, which has absorption and emission wavelengths similar to those of R110 (λ_Ex/λ_Em = 496/520 nm)but has only about 10% of the fluorescence of the latter. Hydrolysis of the second IETD peptide releases the dye R110, leading to a substantial fluorescence increase.

Although fluorometric detection of the end products is preferred because of the superior sensitivity, detection by absorbance is also possible. In fact, the extinction coefficient of R110 is 10 times higher than that of p-nitroaniline (pNA), a dye commonly used in chromogenic substrates, making R110-based substrates significantly more sensitive than pNA-based substrates, even by colorimetric detection.
<p class="style5 style11"><strong>Note:</strong> While caspase-8 preferentially cleaves the consensus sequence IETD compared to other substrate sequences, other caspases such as caspase-3 also can cleave IETD efficiently. Overlapping caspase substrate recognition limits the usefulness of caspase substrate peptides for distinguishing between different caspase activities in cell lysates.</p>
<p class="style5 style11"><strong>Kit Components: </strong></p>

<ul>
<li>Cell lysis buffer</li>
<li>Assay buffer</li>
<li>Enzyme substrate (Ac-IETD)2-R110</li>
<li>Enzyme inhibitor Ac-IETD-CHO</li>
<li>R110
<p class="style5 style11"><strong>Features:</strong></p>

<ul>
<li><b>Fast:</b> Fast enzyme kinetics.</li>
<li><b>Sensitive:</b> The enzymatic reaction forms intensely yellow colored and highly green fluorescent rhodamine 110 (R110) product.</li>
<li><b>Versatile: </b>Compatible with both fluorometric and colorimetric detection systems.</li>
</ul>
</li>
</ul>

Descrition & Target

Protein Purification: Traces of detergent in purified protein samples. Environment: Detergent determination in water and soil.

Descrition & Target

Cell Explorer&trade; Fixable Live Cell Tracking Kit *Green Fluorescence*

Descrition & Target

Cell Explorer&trade; Fixable Live Cell Tracking Kit *Red Fluorescence*