| Weight | 1 lbs |
|---|---|
| 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 |
|---|
| 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 |
Data
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| Immunofluorescent analysis of transfected HEK293 cells with a GFP construct, in green, and stained with rabbit pAb to GFP, 1290, dilution 1:2,000 in red. The blue is Hoechst staining of nuclear DNA. The 1290 antibody reveals GFP protein expressed only in transfected cells, and as a result these cells appear orange-yellow in color. |
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| Chromogenic immunostaining of formalin fixed paraffin embedded section of GFP injected mouse brain with rabbit pAb to GFP, 1290, dilution 1:2,000, detected with DAB (brown) using the Vector Labs ImmPRESS method and reagents with citra buffer retrieval. Hematoxylin (blue) was used as the counterstain. 1290 specifically detected GFP at the injection site. Mouse select image for larger view.PROT-r-AcGFP1 MVSKGAELFT GIVPILIELN GDVNGHKFSV SGEGEGDATY GKLTLKFICT TGKLPVPWPT 61 LVTTLSYGVQ CFSRYPDHMK QHDFFKSAMP EGYIQERTIF FEDDGNYKSR AEVKFEGDTL 121 VNRIELTGTD FKEDGNILGN KMEYNYNAHN VYIMTDKAKN GIKVNFKIRH NIEDGSVQLA 181 DHYQQNTPIG DGPVLLPDNH YLSTQSALSK DPNEKRDHMI YFGFVTAAAI THGMDELYK |
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| Western blot analysis of lysates of transfected HEK293 using rabbit pAb to GFP, 1290 in green, dilution 1:2,000. [1] protein standard, [2] non-transfected control cells, [3] cells transfected with a GFP construct, and [4] cells transfected with mCherry construct. Strong band at ~27kDa corresponds to GFP protein detected only in cells transfected with GFP construct, the antibody does not recognize mCherry. The same blot was simultaneously probed with mouse mAb to beta-tubulin, 1222, dilution 1:10,000, in red. The single band ~50kDa represents beta-tubulin protein expressed in all preparations. |
Publications
Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.There are 11 publications in our database for this antibody or clone. Here are the latest 5, for more click below.
| pmid | title | authors | citation |
|---|---|---|---|
| 36323247 | The Rb/E2F axis is a key regulator of the molecular signatures instructing the quiescent and activated adult neural stem cell state | Fong BC, Chakroun I, Iqbal MA, Paul S, Bastasic J, O'Neil D, Yakubovich E, Bejjani AT, Ahmadi N, Carter A, Clark A, Leone G, Park DS, Ghanem N, Vandenbosch R, Slack RS. | Cell Rep. 2022 Nov 1;41(5):111578. doi: 10.1016/j.celrep.2022.111578. |
| 30888667 | Histological Assessment of Cre-loxP Genetic Recombination in the Aging Subventricular Zone of Nestin-CreER(T2)/Rosa26YFP Mice | Omais S, Halaby NN, Habashy KJ, Jaafar C, Bejjani AT, Ghanem N. | Methods Mol Biol. 2019;2045:187-199. doi: 10.1007/7651_2019_214. |
| 13911999 | Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea | SHIMOMURA O, JOHNSON FH, SAIGA Y. | J Cell Comp Physiol. 1962 Jun;59:223-39. doi: 10.1002/jcp.1030590302. |
| 12693991 | A colourless green fluorescent protein homologue from the non-fluorescent hydromedusa Aequorea coerulescens and its fluorescent mutants | Gurskaya NG, Fradkov AF, Pounkova NI, Staroverov DB, Bulina ME, Yanushevich YG, Labas YA, Lukyanov S, Lukyanov KA. | Biochem J. 2003 Jul 15;373(Pt 2):403-8. doi: 10.1042/BJ20021966. |
| 11988576 | Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells | Zacharias DA, Violin JD, Newton AC, Tsien RY. | Science. 2002 May 3;296(5569):913-6. doi: 10.1126/science.1068539. |
Protocols
| relevant to this product |
|---|
| Western blot ICC |
Documents
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