EGFP/GFP/Venus antibody

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Immunohistochemistry (IHC), Western Blotting (WB)
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Immunogen Synthetic peptides (a pentamer) from EGFP/GFP/Venus conjugated to an immunogenic carrier protein was used as the antigen.
Specificity Specific for EGFP/GFP/Venus
Purification Whole serum
Background GFP is a  naturally fluorescent protein, discovered by chance in the 1960s by Shimomura et al. GFP makes green light out of aequorin’s blue light. The chromophore is a modified Ser-Tyr-Gly sequence. GFP can emit light once this short tripeptide has adopted a cyclic conformation with the help of a oxygen. BIOPHYSICOCHEMICAL PROPERTIES: Excitation max (nm): 488, Emission max (nm): 509, Extinction coefficient (Cm-1M-1): 61000. 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. Also known as: (Enhanced) Green Fluorescence Protein.
Application Notes A dilution of 1 : 300 to 1 : 3000 is recommended.
The optimal dilution should be determined by the end user.
Not yet tested in other applications.
Restrictions For Research Use only
Format Lyophilized
Reconstitution Reconstitute in 500 µL of sterile water. Centrifuge to remove any insoluble material.
Handling Advice Avoid freeze and thaw cycles.
Storage 4 °C/-20 °C
Storage Comment Maintain the lyophilised/reconstituted antibodies frozen at -20°C for long term storage and refrigerated at 2-8°C for a shorter term. When reconstituting, glycerol (1:1) may be added for an additional stability. Avoid freeze and thaw cycles.
Expiry Date 12 months
Background publications Bishop, Fielding, Dyson, Herron: "Systematic insertional mutagenesis of a streptomycete genome: a link between osmoadaptation and antibiotic production." in: Genome research, Vol. 14, Issue 5, pp. 893-900, 2004 (PubMed).

Elsliger, Wachter, Hanson, Kallio, Remington: "Structural and spectral response of green fluorescent protein variants to changes in pH." in: Biochemistry, Vol. 38, Issue 17, pp. 5296-301, 1999 (PubMed).

Tsien: "The green fluorescent protein." in: Annual review of biochemistry, Vol. 67, pp. 509-44, 1998 (PubMed).

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

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