Technical Data
G8965-10B
Green Fluorescent Protein (GFP)
Description:
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.

Applications:
Suitable for use in Immunofluorescence, Immunoprecipitation, Western Blot, Immunohistochemistry and Immunocytochemistry. Other applications not tested.

Recommended Dilution:
Immunocytochemistry( IF): 1:100-1:1000
Immunohistochemistry: 1:100- 1:1500.
Western Blot: 1:250-1:2500
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4°C for short-term only. For long-term storage, aliquot and store at -20°C. Aliquots are stable for at least 12 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
TypeIsotypeCloneGrade
PabIgGAffinity Purified
SizeStorageShippingSourceHost
50ug4°C (-20°C Glycerol)Blue IceRabbit
Concentration:
~0.5mg/ml
Immunogen:
GFP fusion protein corresponding to the full length amino acid sequence (246aa) derivied from the jellyfish Aequorea victoria.
Purity:
Purified by affinity chomatography.
Form
Supplied as a liquid in PBS, pH 7.4, 0.1 sodium azide, before the addition of glycerol to 40%.
Specificity:
Recognizes GFP. Species reactivity: Reacts against all variants of Aequorea victoria GFP such as S65T-GFP, RS-GFP and EGFP.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1.McCabe, et al. ìFunctional roles for fatty Acylated Amino-terminal domains in subcellular localizationî. Mol Biol Cell. 10: 3771-3786, 1999. 2.Jasinska, et al. Lipid phosphate phosphohydrolase-1 degrades exogenous glycerolipid and sphingolipid phosphate esters J Biochem. 340: 677-686, 1999. 3.Zhang, et al. Identification of structurally important domains of lipid phosphate phosphatase-1: implications for sites of action J Biochem. 345: 181-184, 2000. 4. Mesaeli, N., et al. Calreticulin is essential for cardiac development. J. Cell Biology. 144(5): 857-68, 1999.