GFP
Reactivity: Aequorea victoria
WB, ELISA, FM
Host: Chicken
Polyclonal
unconjugated
Application Notes
Optimal working dilution should be determined by the investigator.
Restrictions
For Research Use only
Concentration
1 mg/mL
Buffer
Phosphate buffered saline (PBS) with 15 mM sodium azide, approx. pH 7.4
Preservative
Sodium azide
Precaution of Use
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Handling Advice
Do not freeze.
Storage
4 °C
Storage Comment
Store at 2-8°C. Do not freeze. Do not use after expiration date stamped on vial label.
Porrero, Rubio-Garrido, Avendauno, Clascua: "Mapping of fluorescent protein-expressing neurons and axon pathways in adult and developing Thy1-eYFP-H transgenic mice." in: Brain research, (2010) (PubMed).
Valenta, Lukas, Doubravska, Fafilek, Korinek: "HIC1 attenuates Wnt signaling by recruitment of TCF-4 and beta-catenin to the nuclear bodies." in: The EMBO journal, Vol. 25, Issue 11, pp. 2326-37, (2006) (PubMed).
Green fluorescence protein (GFP) is a 27 KDa protein derived from the bioluminiscent jellyfish Aquorea victoria, emiting green light (λ,=509 nm) when excited (excitation by Blue or UV light, absorption peak λ,=395 nm). GFP is a useful tool in cell biology research, as its intrinsic fluorescence can be visualized in living cells. Light-stimulated GFP fluorescence is species-independent and a fluorescence has been reported from many different types of GFP-expressing hosts, including microbes, invertebrates, vertebrates and plants. No exogenous substrates and cofactors are required for the fluorescence of GFP, since GFP autocatalytically forms a fluorescent pigment from natural amino acids present in the nascent protein. GFP fluorescence is stable under fixation conditions and suitable for a variety of applications. GFP is widely used as a reporter (tag) for gene expression, enabling researchers to visualize and localize GFP-tagged proteins within living cells without any further staining. Other applications of GFP include measurement of distance between proteins through fluorescence energy transfer (FRET) protocols. To increase a fluorescence intensity of GFP, chomophore mutations have been created. The EnhancedGFP has a fluorescence 35 times more intense than the wt-GFP. Mutagenesis of GFP has produced also many mutants (e.g. Yellow Fluorescent Protein, Cyan Fluorescent Protein) with warying spectral properties. Antibodies raised against full-length GFP variants should also detect other variants of the protein.