Technical Data
Green Fluorescent Protein (GFP)
The Green Fluorescent Protein (GFP) from the jellyfish Aequorea victoria is used as a fluorescent indicator for monitoring gene expression in a variety of cellular systems, including living organisms and fixed tissues. Unlike other bioluminescent reporters, GFP fluoresces in the absence of substrates, cofactors, or other intrinsic or extrinsic proteins. Purified GFP is a 27kD monomer consisting of 238 amino acids and emits green light (emission maximum at 509nm) when excited with blue or UV light.

Suitable for use in ELISA, Western Blot and Immunohistochemistry. Other applications have not been tested.

Recommended Dilutions:
ELISA: 1:40,000. Sandwich or capture for detection of wild type, recombinant and enhanced forms of GFP.
Western Blot: 1:400-1:2000; A 33kD band is detected from HeLa cells expressing recombinant GFP.
Immunohistochemistry: 1:200-1:1000; works on frozen sections fixed with ice cold methanol.
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for 12 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
PabIgGAffinity Purified
1mg-20CBlue IceGoat
Purified recombinant GFP fusion protein corresponding to the full length amino acid sequence (246aa) derived from Aequorea victoria.
Purified by immunoaffinity chromatography.
Supplied as a liquid in PBS, pH 7.2, 0.01% sodium azide. No stabilizing proteins added.
Recognizes Green Fluorescent Protein (GFP) and its variants. Assay by IEP resulted in a single precipitin arc against anti-goat serum and purified and partially purified Green Fluorescent Protein (Aequorea victoria). No reaction was observed against human, mouse or rat serum proteins.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
Rousseau J., et al. 2010. Targeted Inactivation of Mapk4 in Mice Reveals Specific Nonredundant Functions of Erk3/Erk4 Subfamily Mitogen-Activated Protein Kinases. Mol. Cell. Biol. 30: 5752 - 5763.