
FITC-C6-PLALWAR-Lys(Biotin)-NH2
| Catalog Number | A18-0027 |
| Category | Fluorescent Enzyme Substrates |
| Molecular Formula | C83H112N18O16S2 |
| Molecular Weight | 1682.0 |
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Product Introduction
FITC-C6-PLALWAR-Lys(Biotin)-NH2 is a fluorescent probe that incorporates fluorescein isothiocyanate (FITC) as its chromophore, known for its bright green fluorescence and excitation/emission maxima compatible with common fluorescence microscopy setups. This compound features a biotinylated peptide sequence, enabling specific binding interactions with avidin or streptavidin, which are often utilized in affinity-based detection assays. The inclusion of a hexanoic acid linker (C6) provides flexibility, facilitating efficient conjugation to biomolecules and enhancing the probe's accessibility in complex biological environments.
Chemical Information
Product Specification
Application
Chemical Information
| Synonyms | MMP-1/MMP-2/MMP-3 Fluorogenic Substrate |
| Purity | ≥95% |
Product Specification
| Storage | Store at -20°C |
Application
FITC-C6-PLALWAR-Lys(Biotin)-NH2 is a fluorescein (FITC)-labeled, peptide-based bioconjugation reagent that combines a reactive peptide scaffold with a terminal biotin handle for downstream streptavidin/avidin coupling. The fluorescein fluorophore enables direct fluorescence readout in microscopy and fluorescence assays, while the biotin moiety supports modular attachment to biotin-binding surfaces, beads, and affinity platforms. This dual-function design is commonly used in chemical biology workflows that require both fluorescent tracking and affinity immobilization.
1. Fluorescent Peptide Tracking
FITC-C6-PLALWAR-Lys(Biotin)-NH2 is used as a fluorescent peptide probe to visualize binding, uptake, or localization in cell-based and protein interaction studies where peptide behavior needs to be tracked by fluorescence. Researchers incorporate the FITC signal for qualitative imaging and quantitative fluorescence readouts, while the biotin tag provides an additional handle for correlating peptide association with affinity-capture steps. This format is frequently chosen for experiments that benefit from a single reagent carrying both a reporter dye and a secondary immobilization/affinity functionality.
2. Streptavidin Bead Immobilization
FITC-C6-PLALWAR-Lys(Biotin)-NH2 supports workflows that immobilize peptide ligands on streptavidin-coated beads, plates, or biosensor surfaces to enable controlled presentation and wash-resistant assays. In these formats, the biotin moiety drives attachment to avidin/streptavidin materials, and the FITC label provides a convenient fluorescence reporter for monitoring surface loading, reagent distribution, and assay execution. Chemical biology and biomaterials laboratories often use this approach to build affinity-captured peptide layers for binding studies, pull-down experiments, and fluorescence-based endpoint measurements.
3. Fluorescence-Based Binding Assays
FITC-C6-PLALWAR-Lys(Biotin)-NH2 is employed in fluorescence assays that quantify peptide-biomolecule or peptide-surface interactions using the FITC emission as the readout. The reagent's peptide architecture allows it to function as a labeled ligand in binding experiments, while the biotin functionality enables parallel strategies such as affinity capture onto biotin-binding matrices to separate bound from unbound fractions. This makes it a practical choice for developing assay formats where fluorescent signal tracking and affinity-enabled handling are both required.
4. Multimodal Probe Conjugation
FITC-C6-PLALWAR-Lys(Biotin)-NH2 is used as a modular building block for constructing multimodal fluorescent conjugates in which FITC provides optical reporting and biotin enables orthogonal attachment to biotin-binding components. Researchers commonly couple the reagent to streptavidin/avidin systems to generate fluorescently labeled probe assemblies for downstream imaging, flow-based readouts, or immobilized assay platforms. This dual-tag strategy is particularly useful when a single peptide reagent must be integrated into larger experimental designs that combine fluorescence detection with affinity-based organization.
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