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Fluorescent-labeled Recombinant Proteins

Background

Fluorescent tag, also known as fluorescent label or fluorescent probe, is a molecule attached chemically to aid in detecting biomolecules such as a protein, antibody, or amino acid. Conjugating fluorescent labels to proteins or other biomolecules is a common means of studying the relative structure and function. Fluorescent proteins are advantageous due to the lack of free dye in solution, thus reducing the overall intensity changes observed with organic fluorophores. However, its large label size and limited labeling sites prevented efficient targeting.

Applications

Fluorescent proteins have a wide range of applications, including immunohistochemistry, fluorescence in situ hybridization (FISH), cell tracking, receptor labeling, and fluorescence spectroscopy.

  • Cell imaging: Fluorescently labeled proteins can be used to observe structural and dynamic changes within cells, such as the nucleus, organelles, signaling pathways, etc.
  • Protein interaction studies: By fusing fluorescently labeled proteins with target proteins, interactions between proteins and complex formation can be observed.
  • Quantitative PCR: Fluorescently labeled proteins can be used in real-time quantitative PCR experiments to quantify the expression level of target genes by detecting changes in the fluorescence signal.
  • Live cell sorting: Fluorescent-labeled proteins can be used for live cell sorting to separate cells or subcell populations by specifically binding to target molecules.
  • Immunofluorescence staining: Fluorescently labeled proteins can be used in immunofluorescence staining experiments to detect specific protein expression in tissues or cells by specifically binding antibodies.

Case Study

Case Study 1: CD19-3307HP

Recombinant Human CCL2 protein, His-Avi-tagged, Biotinylated

(Young-In Kim-Hoehamer, 2022)
Fig1. Percentage of CD19-CAR expression was determined by flow cytometry. Donor identifications are shown at the top of each column. Each column represents one donor.

Case Study 2: IL13RA2-765HP

Recombinant Human EGFR protein, His&Avi-tagged, Biotinylated

(Zelda Odé, 2020)
Fig2. IL-15.E2A.mClover3 transgene integration into TRAC locus. Gating strategy for detection of transgene expression in T cells by flow cytometry.

Case Study 3: TNFRSF17-2348HP

Recombinant Human CCL2 protein, His-Avi-tagged, Biotinylated

(Liang Lin, 2021)
Fig3. Using FCM analysis, cell viability after being thawed was evaluated by FSC-A and SSC-A at indicated time periods (4 hours to 12 days, 4h to 12d). CAR expression was determined by incubating CAR T cells with 0.4 µg/ml of PE-conjugated recombinant BCMA (Recombinant human BCMA/TNFRSF17 protein, Fc/His-tagged, R-PE labeled; Creative Biomart, Shirley, NY) for 20 min at room temperature.

Case Study 4: Cd47-647MF

Recombinant Human EGFR protein, His&Avi-tagged, Biotinylated

(Joshua Kim, 2017)
Fig4. Quantification of the uptake of 200 nm diameter model NCs consisting of green fluorescent polystyrene nanoparticles coated with anti-ICAM alone or 1:1 mass ratio mixtures of anti-ICAM and IgG, anti-ICAM and bovine serum albumin (BSA), or anti-ICAM and recombinant CD47.

Advantages

  • Wide Coverage: More than 2000 fluorescent-labeled recombinant proteins from over 20 different species and nearly 15 different sources.
  • High Quality: Identical binding capacity before and after conjugations, bioactivity verified by flow cytometry and protocol offered,and high batch-to-batch consistency.
  • Experienced: We have professional research team with experience of many years in the field of molecular and cell biology.
  • Fast turnaround: Under the premise of your protein expression and purification, as little as 4-6 weeks.

FAQ

  • Q: How should I store the recombinant proteins??

    A: Sample is stable for at least 12 months when stored at -20 to -80°C from date of manufacture. For longer storage, add equal volume of glycerol to the sample solution and store at -20 to -80°C. Avoid freeze-thaw cycles.

  • Q: How is the purity for the recombinant proteins determined?

    A: Protein purity is most often determined by SDS-PAGE; sometimes, it is analyzed by HPLC as well. Please refer to either the product manual, data sheet or certificate of analysis (CoA) for product-specific purity levels and methods.

References

  1. Kim-Hoehamer, Young-In et al. “Development of a cGMP-compliant process to manufacture donor-derived, CD45RA-depleted memory CD19-CAR T cells.” Gene therapy vol. 30,3-4 (2023): 222-231.
  2. Odé, Zelda et al. “CRISPR-Mediated Non-Viral Site-Specific Gene Integration and Expression in T Cells: Protocol and Application for T-Cell Therapy.” Cancers vol. 12,6 1704. 26 Jun. 2020.
  3. Lin, Liang et al. “Preclinical evaluation of CD8+ anti-BCMA mRNA CAR T cells for treatment of multiple myeloma.” Leukemia vol. 35,3 (2021): 752-763.
  4. Kim, Joshua et al. “Co-coating of receptor-targeted drug nanocarriers with anti-phagocytic moieties enhances specific tissue uptake versus non-specific phagocytic clearance.” Biomaterials vol. 147 (2017): 14-25.
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