电话:
+86 (0512) 65829739
传真:
+86 (010) 6788 5057
电子邮件:
orders@antibodies-online.cn

Antibodies Against Fluorescent Proteins

Fluorescent proteins such as GFP, RFP, and their derivatives are indispensable tools for visualizing and tracking biological processes across diverse experimental systems. To fully exploit their potential, reliable and application-validated detection and capture reagents are essential. Our portfolio of antibodies against fluorescent proteins is designed to support both analytical and preparative workflows, ranging from flow cytometry (FACS), flow cytometry–based sorting, and immunohistochemistry (IHC), to robust affinity-based capture strategies. You can use the following graphic to quickly navigate to antibodies against your desired fluorophore.

TagBFP BFP mCherry mCherry YFP YFP mNeonGreen mNeonGreen tdTomato tdTomato GFP GFP mScarlet ;fill-opacity:1;stroke-width:1;stroke-dasharray:none" /> id="circle10561" /> mScarlet mTurquoise mTurquoise RFP RFP

In addition to conventional detection antibodies, we offer a dedicated catcher product line: high-affinity antibodies optimized for pull-down applications, including immunoprecipitation (IP), co-immunoprecipitation (Co-IP), and chromatin immunoprecipitation (ChIP). Our catcher product line is based on recombinant single-domain antibodies (sdAbs) derived from llamas or alpacas. These reagents enable efficient and specific isolation of fluorescent protein–tagged targets, facilitating downstream biochemical and molecular analyses with minimal background.

All products are developed with a strong emphasis on specificity, reproducibility, and batch-to-batch consistency, supported by rigorous quality control and application-relevant validation. Learn more about the history of fluorescent proteins down below, how different variants emerged and about their characteristics; advantages and disadvantages for specific usecases.

Value of Fluorescent Proteins

Fluorescently conjugated antibodies are indispensable tools in modern life science research and biotechnology, enabling the sensitive, specific, and quantitative detection of biomolecules across a wide range of experimental platforms. By directly coupling antigen recognition with optical readout, fluorescent antibodies allow real-time visualization, multiparametric analysis, and high-throughput interrogation of complex biological systems, from single cells to heterogeneous populations and subcellular structures.

The value of fluorescent antibodies lies in their versatility across applications with fundamentally different experimental demands. FACS antibody conjugates enable simultaneous detection of multiple surface or intracellular markers at the single-cell level, supporting phenotypic profiling, population stratification, and physical isolation of defined cell subsets. Here, critical parameters include fluorophore brightness, photostability, and spectral separation, as these directly impact sensitivity, compensation, and panel complexity. In contrast, fluorescence-based pull-down or co-IP assays prioritize antibody affinity, epitope accessibility, and conjugation stability, as fluorescent signal is used to track protein–protein interactions or enrichment efficiency rather than to resolve complex spectral mixtures.

History of Green Fluorescent Protein (GFP)

The green fluorescent protein (GFP) is a protein from the jellyfish Aequorea victoria which fluoresces green upon excitation with blue or ultraviolet light. The discovery of green fluorescent protein in the early 1960s by Shimomura has laid the foundation for modern live cell imaging. GFP can be fused to other proteins of interest in a host cell as a noninvasive fluorescent marker in living cells and organisms. Since then, GFP has been engineered and further developed to produce a plethora of mutants coverving a wide range of colors, including enhanced green, cyan and yellow fluorescent proteins, which exhibit peak emission wavelengths ranging from 425 to 525 nm.

Comparison of GFP Variants

Spectroscopic properties of GFP variants, and respective Antibodies against GFP tagged proteins.
Protein Excitation [nm] Emission [nm] Extinct. Coeff. [M-1cm-1] Quantum yield [Φ] Brightness [nM-1cm-1] t [0,5] Maturation (37 °C) Structure Antibody
GFP (wt) 395 475 509 21,000 0.77 19.8 36 min Dimer ABIN100085
BFP 380 445 28,000 0.30 8.4 Weak Dimer
433 475 32,000 0.40 12.8 Monomer ABIN7273090
YFP 514 527 83,000 0.60 49.8 10 min Weak Dimer ABIN6254248
EGFP 484507 56,000 0.6 33,6 15 min Weak Dimer ABIN1169226
EBFP 383 445 29,000 0.31 6.9 Weak Dimer
439 476 32,500 0.4 13 Monomer ABIN3181526
EYFP 514 527 83,400 0.61 44.9 9 min Weak Dimer ABIN3181270
EYFP 514 527 83,400 0.61 44.9 9 min Weak Dimer ABIN3181270 YFP 514 527 83,000 0.60 49.8 10 min Weak Dimer ABIN6254248 GFP (wt) 395 475 509 21,000 0.77 19.8 36 min Dimer ABIN100085 EGFP 484 507 56,000 0.6 33.6 15 min Weak Dimer ABIN1169226
439 476 32,500 0.4 13 Monomer ABIN3181526
433 475 32,000 0.40 12.8 Monomer An Introduction to Fluorescence (Part 1)
  • An Introduction to Fluorescence (Part 2)
  • Excitation / Emission Maxima Poster for Popular Fluorophores
  • Catcher Product Line - High-Affinity Single-Domain Antibodies

  • References

    1. Kimple, Brill, Pasker: "Overview of affinity tags for protein purification." in: Current protocols in protein science, Vol. 73, pp. 9.9.1-9.9.23, (2014) (PubMed).
    2. Terpe: "Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems." in: Applied microbiology and biotechnology, Vol. 60, Issue 5, pp. 523-33, (2003) (PubMed).
    3. Nilsson, Ståhl, Lundeberg, Uhlén, Nygren: "Affinity fusion strategies for detection, purification, and immobilization of recombinant proteins." in: Protein expression and purification, Vol. 11, Issue 1, pp. 1-16, (1997) (PubMed).
    4. Matz, Fradkov, Labas, Savitsky, Zaraisky, Markelov, Lukyanov: "Fluorescent proteins from nonbioluminescent Anthozoa species." in: Nature biotechnology, Vol. 17, Issue 10, pp. 969-73, (1999) (PubMed).
    5. Kremers, Goedhart, van Munster, Gadella: "Cyan and yellow super fluorescent proteins with improved brightness, protein folding, and FRET Förster radius." in: Biochemistry, Vol. 45, Issue 21, pp. 6570-80, (2006) (PubMed).
    6. Balleza, Kim, Cluzel: "Systematic characterization of maturation time of fluorescent proteins in living cells." in: Nature methods, Vol. 15, Issue 1, pp. 47-51, (2019) (PubMed).
    7. Shaner, Campbell, Steinbach, Giepmans, Palmer, Tsien: "Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein." in: Nature biotechnology, Vol. 22, Issue 12, pp. 1567-72, (2005) (PubMed).
    8. Shcherbakova, Subach, Verkhusha: "Red fluorescent proteins: advanced imaging applications and future design." in: Angewandte Chemie (International ed. in English), Vol. 51, Issue 43, pp. 10724-38, (2013) (PubMed).
    9. Shcherbakova, Hink, Joosen, Gadella, Verkhusha: "An orange fluorescent protein with a large Stokes shift for single-excitation multicolor FCCS and FRET imaging." in: Journal of the American Chemical Society, Vol. 134, Issue 18, pp. 7913-23, (2012) (PubMed).
    10. Gurskaya, Verkhusha, Shcheglov, Staroverov, Chepurnykh, Fradkov, Lukyanov, Lukyanov: "Engineering of a monomeric green-to-red photoactivatable fluorescent protein induced by blue light." in: Nature biotechnology, Vol. 24, Issue 4, pp. 461-5, (2006) (PubMed).
    11. Chudakov, Lukyanov, Lukyanov: "Using photoactivatable fluorescent protein Dendra2 to track protein movement." in: BioTechniques, Vol. 42, Issue 5, pp. 553, 555, 557 passim, (2007) (PubMed).
    撰写 / 编辑者 Julian Pampel, BSc
    You are here: