Lyophilized Peridinin-Chlorophyll Protein Complex (Lyo-PerCP)
Product Overview
Lyo-PerCP is a high-purity, lyophilized form of Peridinin-Chlorophyll Protein, a tandem fluorescent protein derived from marine dinoflagellates, purpose-built for antibody conjugation in flow cytometry-based in vitro diagnostic assays. With excitation at 481 nm and emission at 675 nm, PerCP is optimally excited by the 488 nm argon-ion laser and emits in the deep red channel, enabling clean multi-color panel design with minimal spectral spillover into PE and APC channels.
Flogen® Lyo-PerCP is supplied as a lyophilized powder in 10 mM potassium phosphate buffer with a cryoprotective sugar additive. The formulation contains no ammonium sulfate or other reagents that may interfere with downstream conjugation chemistry, ensuring compatibility with standard SMCC-based and other crosslinking protocols.
Optical Properties
Excitation Max / Emission Max: 481 nm / 675 nm
Purity: A481/A280 ≥ 4.2 | A620/A481 ≤ 0.005 (chlorophyll-free)
Storage & Shipping Store lyophilized product at 4°C in the dark with desiccant, preferably in a desiccator. Do not freeze. Shipped on blue ice. Upon reconstitution, handle as per standard phycobiliprotein protocols.
TDS/COA:Click here to see the corresponding document
Features
Ready-to-Conjugate Format Lyo-PerCP eliminates time-consuming upstream preparation steps, including buffer exchange, concentration, and incoming quality verification, that are required when working with liquid phycobiliprotein. Reconstitute, adjust to your target concentration, and proceed directly to conjugation.
Superior Long-Term Stability The lyophilized format delivers significantly improved storage and shipping stability compared to liquid PerCP, maintaining >95% fluorescence activity over 24 months at 4°C. This translates directly into reduced cold-chain risk, extended shelf life for your IVD kit components, and fewer stability-related failures during distribution.
Conjugation-Ready Purity A481/A280 ≥ 4.2 confirms that the vast majority of protein present is functional PerCP, minimizing non-specific binding and background signal in your final assay. The specification A620/A481 ≤ 0.005 guarantees freedom from free chlorophyll contamination, which can quench fluorescence and compromise assay sensitivity.
Flexible Formulation Reconstitute in any buffer of your choice at your required working concentration. No proprietary stabilizers or carrier proteins are present that could restrict downstream processing or introduce lot-to-lot variability in your conjugation workflow.
Lot-to-Lot Consistency Manufactured under tightly controlled bioprocess conditions with full quality documentation (TDS/COA/MSDS available). Each lot is tested against defined optical purity specifications before release, enabling high reproducibility across your production batches.
Scalable Supply Available in 20 mg standard pack size, with larger quantities available on inquiry. Suitable for both R&D-scale conjugation development and commercial IVD manufacturing scale-up.
Equivalent Performance to Liquid PerCP Lyo-PerCP reconstitutes to deliver the same high fluorescence intensity and labeling performance as Flogen® liquid phycobiliproteins, with the added advantages of the lyophilized format.
References and Citations
- Durban University of Technology, & Morgany, T. (2020, April). Extraction and purification of C-PC and genome analysis of an indigenour hypersaline cyanobaterium. https://scholarworks.uno.edu/cgi/viewcontent.cgi?article=1244&context=td
- Fluorophore. (n.d.). Wikipedia. Retrieved August 17, 2022, from https://en.wikipedia.org/wiki/Fluorophore
- Marinkovic, B., Delneri, A., Rabasovic, M., Terzic, M., Franko, M., & Sevic, D. (2014). Investigation and detection of cyanobacterial Cr-phycoerythrin by laser based techniques. Journal of the Serbian Chemical Society, 79(2), 185–198. https://doi.org/10.2298/jsc130417088m
- Protein Biomarkers of Cardiovascular Disease and Mortality in the Community. (n.d.). ResearchGate. Retrieved August 18, 2022, from https://www.researchgate.net/publication/326375426_Protein_Biomarkers_of_Cardiovascular_Disease_and_Mortality_in_the_Community/fulltext/5b48a3faa6fdccadaec770c6/Protein-Biomarkers-of-Cardiovascular-Disease-and-Mortality-in-the-Community.pdf
- Sekar, S., & Chandramohan, M. (2007). Phycobiliproteins as a commodity: trends in applied research, patents and commercialization. Journal of Applied Phycology, 20(2), 113–136. https://doi.org/10.1007/s10811-007-9188-1
- University of New Orleans, & Biswas, A. (2011, August). Identification and characterization of enzymes involved in the biosynthesis of diff biosynthesis of different phycobiliproteins in cyanobacteria. https://scholarworks.uno.edu/cgi/viewcontent.cgi?article=1244&context=td


