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GFP (N-Term) antibody

Antigen

GFP

Binding Site
Alternatives

N-Term

Clonality Polyclonal
Host
Alternatives

Rabbit

Reactivity
Alternatives

Aequorea victoria

Conjugate
Alternatives Un-conjugated
Application
Alternatives Immunohistochemistry (IHC)
7 references available
Catalog no. ABIN966201
Quantity 0.1mg
Price 397.38 $   Plus shipping costs $45.00
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Additional Information

Immunogen Polyclonal antibody produced in rabbits immunizing with a synthetic peptide corresponding to N-terminal residues of Aequorea victoria GFP (Green fluorescent protein)
Description GFP(Green fluorescent protein) is an energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin. It contains a chromophore consisting of modified amino acid residues. The chromophore is formed by autocatalytic backbone condensation between Xaa-N and Gly-(N+2), and oxidation of Tyr-(N+1) to didehydrotyrosine. Maturation of the chromophore requires nothing other than molecular oxygen. Fluorescent proteins have become a useful and ubiquitous tool for making chimeric proteins, where they function as a fluorescent protein tag. Typically they tolerate N- and C-terminal fusion to a broad variety of proteins. They have been expressed in most known cell types and are used as a noninvasive fluorescent marker in living cells and organisms. They enable a wide range of applications where they have functioned as a cell lineage tracer, reporter of gene expression, or as a measure of protein-protein interactions.

Application Details

Application Notes ELISA, Western blotting: 1µg/ml for 2hrs.
Purification Purified by antigen-specific affinity chromatography.
Buffer This antibody is stored in PBS, 50% glycerol
Preservative 0.01% Sodium Azide
Storage Store at -20°C.
Research Area Tags/Labels
Restrictions For Research Use only

Publications

Product Prasher, Eckenrode, Ward et al.: "Primary structure of the Aequorea victoria green-fluorescent protein." in: Gene, Vol. 111, Issue 2, pp. 229-33, 1992 (PubMed).

Inouye, Noguchi, Sakaki et al.: "Cloning and sequence analysis of cDNA for the luminescent protein aequorin." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 82, Issue 10, pp. 3154-8, 1985 (PubMed).

Inouye, Tsuji: "Aequorea green fluorescent protein. Expression of the gene and fluorescence characteristics of the recombinant protein." in: FEBS letters, Vol. 341, Issue 2-3, pp. 277-80, 1994 (PubMed).

Cody, Prasher, Westler et al.: "Chemical structure of the hexapeptide chromophore of the Aequorea green-fluorescent protein." in: Biochemistry, Vol. 32, Issue 5, pp. 1212-8, 1993 (PubMed).

Ormö, Cubitt, Kallio et al.: "Crystal structure of the Aequorea victoria green fluorescent protein." in: Science (New York, N.Y.), Vol. 273, Issue 5280, pp. 1392-5, 1996 (PubMed).

Yang, Moss, Phillips: "The molecular structure of green fluorescent protein." in: Nature biotechnology, Vol. 14, Issue 10, pp. 1246-51, 1998 (PubMed).

Wachter, Elsliger, Kallio et al.: "Structural basis of spectral shifts in the yellow-emission variants of green fluorescent protein." in: Structure (London, England : 1993), Vol. 6, Issue 10, pp. 1267-77, 1998 (PubMed).