*Optimal dilutions/concentrations should be determined by the researcher.
Not tested in other applications.
Anti-GFP assayed by ELISA for direct binding of antigen recognizes wild type, recombinant and enhanced forms of GFP
0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2, containing 0.01% sodium azide
Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
1.03 mg/ml (Please refer to the vial label for the specific concentration.)
Green Fluorescent Protein (GFP) fusion protein corresponding to the full length amino acid sequence (246aa) derived from the jellyfish Aequorea victoria
From polyclonal serum
For laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
The jellyfish Aequorea victoria contains green fluorescent protein (GFP) that emits light in the bioluminescence reaction of the animal. GFP has been used widely as a reporter protein for gene expression in eukaryotic and prokaryotic organisms, and as a protein tag in cell culture and in multicellular organisms. As a fusion tag, GFP can be used to localize proteins, to study their movement or to research the dynamics of the subcellular compartments where these proteins are targeted. GFP technology has revealed considerable new insights into the physiological activities of living cells. GFP is a 27 kDa monomeric protein, which autocatalytically forms a fluorescent pigment. The wild type protein absorbs blue light (maximally at 395nm) and emits green light (peak emission 508nm) in the absence of additional proteins, substrates, or co-factors. GFP fluorescence is stable, species independent and is suitable for a variety of applications. GFP has been used extensively as a fluorescent tag to monitor gene expression and protein localization. Moreover, other applications for GFP include its use in assessing protein protein interactions in the yeast two hybrid system, and in measuring distances between proteins in fluorescence energy transfer (FRET) experiments.