There are 2+ publications for this product available. The Rabbit Polyclonal anti-GFP antibody is suitable to detect GFP in samples from Aequorea victoria. It has been validated for WB, IP and ICC.
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).
Target
GFP
(Green Fluorescent Protein (GFP))
Alternative Name
GFP
Background
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.