Why Choose One Antibody Format Over Another?

Jackson ImmunoResearch als Spezialist für secondary antibodies, fragments and conjugates kurz vorstellen.

Whole IgG antibodies: the versatile standard

strong signal generation
broad signal generation
Western blot, ELISA, IHC, ICC, IF
Indication of potential Fc-receptor interactions

F(ab')₂ fragments for reduced background

reduced Fc-mediated interactions
lower background
besonders relevant bei Fc-receptor-expressing cells
Flow Cytometry, FACS, Live Cell Imaging

Fab fragments for greater experimental flexibility

monovalent
reduced steric hindrance
avoids cross-linking
Multiplex IF / sequential staining / blocking

VHH antibodies and nanobodies

small size
access to difficult epitopes
tissue penetration
high-resolution / super-resolution imaging

Choosing the right antibody format

Kurzer Quick Guide:

Whole IgG: versatile choice for routine applications
F(ab')₂: reduced Fc receptor interactions and background
Fab: greater flexibility for complex staining and multiplexing
VHH / Nanobodies: compact format for advanced imaging

More than your standard secondary

Jackson ImmunoResearch – More than your standard secondary

Explore high-quality secondary antibodies, fragments and conjugates for a wide range of research applications.

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With the SZABO-SCANDIC Antibody Promise, you can choose the right antibodies for your research with added confidence.

Based on Why use a particular antibody format?

References

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Heim R, Cubitt AB, Tsien RY. Improved green fluorescence. Nature. 1995;373(6516):663-664. doi:10.1038/373663b0 https://pubmed.ncbi.nlm.nih.gov/7854443/

Heim R, Prasher DC, Tsien RY. Wavelength mutations and posttranslational autoxidation of green fluorescent protein. Proc Natl Acad Sci USA. 1994;91(26):12501-12504. doi:10.1073/pnas.91.26.12501 https://pubmed.ncbi.nlm.nih.gov/7809066/

Cormack BP, Valdivia RH, Falkow S. FACS-optimized mutants of the green fluorescent protein (GFP). Gene. 1996;173(1 Spec No):33-38. doi:10.1016/0378-1119(95)00685-0 https://pubmed.ncbi.nlm.nih.gov/8707053/

Romei MG, Boxer SG. Split Green Fluorescent Proteins: Scope, Limitations, and Outlook. Annu Rev Biophys. 2019;48:19-44. doi:10.1146/annurev-biophys-051013-022846 https://pubmed.ncbi.nlm.nih.gov/30786230/

Kodama Y, Hu CD. Bimolecular fluorescence complementation (BiFC): a 5-year update and future perspectives. Biotechniques. 2012;53(5):285-298. doi:10.2144/000113943 https://pubmed.ncbi.nlm.nih.gov/23148879/

Ghosh I, Hamilton AD, Regan L. Antiparallel Leucine Zipper-Directed Protein Reassembly: Application to the Green Fluorescent Protein. J Am Chem Soc. 2000;122:5658-5659. DOI:10.1021/JA994421W https://www.semanticscholar.org/paper/Antiparallel-Leucine-Zipper-Directed-Protein-to-the-Ghosh-Ham…

Cabantous S, Nguyen HB, Pedelacq JD, et al. A new protein-protein interaction sensor based on tripartite split-GFP association. Sci Rep. 2013;3:2854. doi:10.1038/srep02854 https://pubmed.ncbi.nlm.nih.gov/24092409/

Pham, TD, Poletti, C, Tientcheu, TMN et al. FAST, a method based on split-GFP for the detection in solution of proteins synthesized in cell-free expression systems. Sci Rep. 2024;14:8042. https://doi.org/10.1038/s41598-024-58588-5

Why Choose One Antibody Format Over Another?