Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
host | rabbit |
isotype | IgG |
clonality | polyclonal |
concentration | 1 mg/mL |
applications | ICC/IF, WB |
reactivity | tagged fusion proteins |
available sizes | 1 mg, 100 µg, 25 µg |
rabbit anti-GFP polyclonal antibody 1290
$100.00 – $2,600.00
Antibody summary
- Rabbit polyclonal to GFP
- Suitable for: WB, ICC/IF
- Reacts with: tagged fusion proteins
- Isotype: IgG
- 100 µg, 25 µg, 1 mg
rabbit anti-GFP polyclonal antibody 1290
target relevance |
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Protein expression of GFP and GFP tagged proteins can be checked and quantified using this antibody in Western blotting. When imaging in situ, GFP fluorescence can be amplified by this antibody when used in conjunction with a suitable fluorescent label or secondary antibody. Click for more on: epitope tags and GFP |
Protein names Green fluorescent protein |
Gene names GFP,GFP |
Protein family GFP family |
Mass 26886Da |
Function 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. |
Tissues Photocytes. |
Structure Monomer. |
Post-translational modification Contains a chromophore consisting of modified amino acid residues. The chromophore is formed by autocatalytic backbone condensation between Ser-65 and Gly-67, and oxidation of Tyr-66 to didehydrotyrosine. Maturation of the chromophore requires nothing other than molecular oxygen. |
Biotechnology Green fluorescent protein has been engineered to produce a vast number of variously colored mutants, fusion proteins, and biosensors. Green fluorescent protein can be mutated to emit at different wavelengths such as blue for BFP (when Tyr-66 is replaced by His), cyan for CFP (when Tyr-66 is replaced by Trp), and yellow for YFP (when Thr-203 is replaced by Tyr). Further generation of mutants led to more stable proteins (at 37 degrees Celsius for example) with brighter fluorescence and longer fluorescence lifetimes. Fluorescent proteins and their mutated allelic forms 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 (PubMed:17685514, PubMed:17685554, PubMed:8578587, PubMed:8707053, PubMed:9145105, PubMed:9154981, PubMed:9759496, PubMed:9782051). Can also be used as a molecular thermometer, allowing accurate temperature measurements in fluids. The measurement process relies on the detection of the blinking of GFP using fluorescence correlation spectroscopy (PubMed:17685514). |
Target Relevance information above includes information from UniProt accession: P42212 |
The UniProt Consortium |
Publications
pmid | title | authors | citation |
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36323247 | The Rb/E2F axis is a key regulator of the molecular signatures instructing the quiescent and activated adult neural stem cell state. | Bensun C Fong, Imane Chakroun, Mohamed Ariff Iqbal, Smitha Paul, Joseph Bastasic, Daniel O'Neil, Edward Yakubovich, Anthony T Bejjani, Nastaran Ahmadi, Anthony Carter, Alysen Clark, Gustavo Leone, David S Park, Noël Ghanem, Renaud Vandenbosch, Ruth S Slack | Cell Rep 41:111578 |
30888667 | Histological Assessment of Cre-loxP Genetic Recombination in the Aging Subventricular Zone of Nestin-CreER(T2)/Rosa26YFP Mice. | Saad Omais, Nour N Halaby, Karl John Habashy, Carine Jaafar, Anthony T Bejjani, Noël Ghanem | Methods Mol Biol 2045:187-199 |
13911999 | Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea. | O SHIMOMURA, F H JOHNSON, Y SAIGA | J Cell Comp Physiol 59:223-39 |
12693991 | A colourless green fluorescent protein homologue from the non-fluorescent hydromedusa Aequorea coerulescens and its fluorescent mutants. | Nadya G Gurskaya, Arkady F Fradkov, Natalia I Pounkova, Dmitry B Staroverov, Maria E Bulina, Yurii G Yanushevich, Yulii A Labas, Sergey Lukyanov, Konstantin A Lukyanov | Biochem J 373:403-8 |
11988576 | Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. | David A Zacharias, Jonathan D Violin, Alexandra C Newton, Roger Y Tsien | Science 296:913-6 |
relevant to this product |
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Western blot ICC |
# | SDS | Certificate | |
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