GFP-Booster (Atto 488)

Details for Product No. ABIN1082212
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Target Name (Antigen)
Reactivity
Aequorea victoria
Conjugate
Atto 488
Application
Immunofluorescence (IF), Fluorescence Microscopy (FM)
Pubmed 9 references available
Catalog no. ABIN1082212
Quantity 50 µg
Price
178.20 $   Plus shipping costs $45.00
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Purpose With our Booster you reactivate, boost, stabilizate the signals of your fusion proteins.
Specificity GFP-Booster efficiently detects and labels most common GFP derivates. No binding to red fluorescent proteins derived from DsRed can be detected.
Characteristics - Enhance, stabilize and reactivate your fl uorescent proteins
- GFP-Booster highly specifi c for GFP fusion proteins (and derivatives thereof e.g. YFP or Venus)
- Coupled to bright and photostable chemical dyes from ATTO-TEC
Components GFP-Trap® coupled to fluorescent dye ATTO 488
Alternative Name GFP
Background Green fluorescent proteins (GFP) and variants thereof are widely used to study protein localization and dynamics in living cells. However, photo stability and quantum efficiency of GFP are not sufficient for Super-Resolution Microscopy (e.g. 3D-SIM or STED) of fixed samples. In addition, many cell biological methods such as BrdU-staining, EdU-Click-iT™ treatment or Fluorescent In Situ Hybridization result in disruption of the GFP signal.The GFP-Booster_Atto488, a specific GFP-binding protein coupled to the fluorescent dye ATTO 488, reactivates, boosts and stabilizes your GFP signal.
Research Area Tags/Labels
Application Notes For the immunofluorescence staining of GFP-fusion proteins in fixed cells

ATTO 488:
Excitation range 480 - 510 nm (λabs= 501 nm)
Emission range 520 - 560 nm (λfl= 523 nm)
Comment

Booster are very small, highly specific GFP- or RFP-binding proteins covalently coupled to the superior fluorescent dyes from ATTO-TEC.

Assay Procedure 1. Fixation: 4% paraformaldehyde (PFA) or 1:10 formalin (37% formaldehyde, 10-15% MetOH) in PBS, 10 min., RT.
2. Wash 3x with PBS containing 0.1% Tween 20 (PBST). Critical: do not let coverslips “dry”.
3. Permeabilisation: PBS containing 0.5% Triton X-100, 5 min., RT. Alternatively permeabilise by incubating in 100% methanol for 5min at -20°C.
4. Wash 2x with PBST.
5. Blocking: 4% BSA in PBST, 10 min, RT.
6. GFP-Booster incubation: dilute GFP-Booster 1:200 in blocking buffer and incubate 1 h, RT. Note: For multiplexing protocols you can combine GFP-Booster with any other antibody.
7. Wash 3x 5-10 min in PBST.
8. If required counterstain with DNA fluorescent dyes, e.g. DAPI.
9. Before mounting coverslips can be very briefly rinsed in water to prevent salt crystals to form.
10. Mount in VectaShield (Vector Labs) or other mounting media with anti-fading agents and seal mounted coverslips with clear nail polish. Please note: Optimal dilutions/ concentrations should be determined by the end user
Restrictions For Research Use only
Concentration 1 mg/ml
Buffer PBS, 0.01% Sodium azide
Preservative Sodium azide
Handling Advice Do not freeze. Protect from light.
Storage 4 °C
Expiry Date 6 months
Supplier Images
GFP-Booster (Atto 488) Visualization of GFP signal with GFP-Booster after EdU-Click-iT™ treatment.EdU-Click-iT™ treament leads to disruption of GFP signal. GFP-Booster labels GFP fusion proteins and thus reactivates and boosts the fluorescence (dilution 1/200,1 h at RT).(GFP-Booster with EdU-Click-iT™ protocol)
GFP-Booster (Atto 488) (2) Enhancement of GFP signal with GFP-Booster_Atto488. Comparison of signal intensity of a HeLa cell line stably expressing a nuclear GFP-fusion protein before and after GFP-Booster treatment.
Product cited in: Guizetti, Schermelleh, Mäntler et al.: "Cortical constriction during abscission involves helices of ESCRT-III-dependent filaments." in: Science (New York, N.Y.), Vol. 331, Issue 6024, pp. 1616-20, 2011 (PubMed).

Cordes, Maiser, Steinhauer et al.: "Mechanisms and advancement of antifading agents for fluorescence microscopy and single-molecule spectroscopy." in: Physical chemistry chemical physics : PCCP, Vol. 13, Issue 14, pp. 6699-709, 2011 (PubMed).

Ridzuan, Moon, Knuepfer et al.: "Subcellular location, phosphorylation and assembly into the motor complex of GAP45 during Plasmodium falciparum schizont development." in: PLoS ONE, Vol. 7, Issue 3, pp. e33845, 2012 (PubMed).

Mikeladze-Dvali, von Tobel, Strnad et al.: "Analysis of centriole elimination during C. elegans oogenesis." in: Development (Cambridge, England), Vol. 139, Issue 9, pp. 1670-9, 2012 (PubMed).

Ries, Kaplan, Platonova et al.: "A simple, versatile method for GFP-based super-resolution microscopy via nanobodies." in: Nature methods, Vol. 9, Issue 6, pp. 582-4, 2012 (PubMed).

Yüce, West: "Senataxin, defective in the neurodegenerative disorder ataxia with oculomotor apraxia 2, lies at the interface of transcription and the DNA damage response." in: Molecular and cellular biology, Vol. 33, Issue 2, pp. 406-17, 2012 (PubMed).

Heimer-McGinn, Murphy, Kim et al.: "Decreased dendritic spine density as a consequence of tetanus toxin light chain expression in single neurons in vivo." in: Neuroscience letters, Vol. 555, pp. 36-41, 2013 (PubMed).

Hall, Keighren, Ford et al.: "Acute versus chronic loss of Mammalian azi1/cep131 results in distinct ciliary phenotypes." in: PLoS genetics, Vol. 9, Issue 12, pp. e1003928, 2014 (PubMed).

Linkner, Witte, Zhao et al.: "The inverse BAR-domain protein IBARa drives membrane remodelling to control osmoregulation, phagocytosis and cytokinesis." in: Journal of cell science, 2014 (PubMed).

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