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Citations & References (36)
Invitrogen™
TC-ReAsH™ II In-Cell Tetracysteine Tag Detection Kit (Red Fluorescence), for live-cell imaging
TC-ReAsH™ II In-Cell Tetracysteine Tag Detection Kit contains an expression tag-based fluorescence labeling reagent for live-cell labeling. Mammalian cell linesRead more
| Catalog Number | Quantity |
|---|---|
| T34562 | 1 Kit |
Catalog number T34562
Price (EUR)
1.304,00
1 kit
Quantity:
1 Kit
Price (EUR)
1.304,00
1 kit
TC-ReAsH™ II In-Cell Tetracysteine Tag Detection Kit contains an expression tag-based fluorescence labeling reagent for live-cell labeling. Mammalian cell lines expressing a protein fused to a tetracysteine tag (CCPGCC) can be labeled with the red-fluorescent ReAsH-EDT2 reagent contained in the kit. The tagged protein is fluorescent only when the labeling reagent is added. BAL wash buffer replaces the previously supplied Disperse Blue 3 and EDT-based wash buffer as an olfactorily more agreeable reagent that yields superior signal to noise.
The kit contains ReAsH-EDT2 labeling reagent (store at -20°C, protected from light) and BAL wash buffer (stored at 4°C). When stored as directed, the kit is stable for 6 months.
The kit contains ReAsH-EDT2 labeling reagent (store at -20°C, protected from light) and BAL wash buffer (stored at 4°C). When stored as directed, the kit is stable for 6 months.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
ColorRed
Detection MethodFluorescence
For Use With (Equipment)Fluorescence Microscope
Label or DyeReAsH
Product LineTC-ReAsH II
Product TypeTetracysteine Tag Detection Kit
Quantity1 Kit
Shipping ConditionWet Ice
FormatKit
Unit Size1 kit
Contents & Storage
Store in freezer (-5 to -30°C).
Frequently asked questions (FAQs)
Can fluorescent protein-expressing cells be fixed?
Are the fluorescent proteins offered by Thermo Fisher Scientific (EmGFP, YFP, CFP, BFP and Cycle 3 GFP) humanized?
Citations & References (36)
Citations & References
Abstract
Resolution of de novo HIV production and trafficking in immature dendritic cells.
Journal:Nat Methods
PubMed ID:18059278
'The challenge in observing de novo virus production in human immunodeficiency virus (HIV)-infected dendritic cells (DCs) is the lack of resolution between cytosolic immature and endocytic mature HIV gag protein. To track HIV production, we developed an infectious HIV construct bearing a diothiol-resistant tetracysteine motif (dTCM) at the C terminus
Identification of an intracellular trafficking and assembly pathway for HIV-1 gag.
Journal:Traffic
PubMed ID:16683918
'Retroviral Gag proteins are membrane-bound polyproteins that are necessary and sufficient for virus-like particle (VLP) formation. It is not known how Gag traffics through the cell or how the site of particle production is determined. Here we use two techniques, biarsenical/tetracysteine (TC) labeling and release from a cycloheximide block, to
Real-time visualization of HIV-1 GAG trafficking in infected macrophages.
Journal:PLoS Pathog
PubMed ID:18369466
'HIV-1 particle production is driven by the Gag precursor protein Pr55(Gag). Despite significant progress in defining both the viral and cellular determinants of HIV-1 assembly and release, the trafficking pathway used by Gag to reach its site of assembly in the infected cell remains to be elucidated. The Gag trafficking
Site-specific, orthogonal labeling of proteins in intact cells with two small biarsenical fluorophores.
Journal:Bioconjug Chem
PubMed ID:20429545
'The fusion of fluorescent proteins to proteins of interest has greatly advanced fluorescence microscopy, but is often limited by their large size. Here, we report site-specific, orthogonal labeling of two cellular proteins in intact cells with two small fluorescent dyes: fluorescein arsenical hairpin binder, FlAsH, and its red analogue, ReAsH,
Fluorescence imaging of amyloid formation in living cells by a functional, tetracysteine-tagged alpha-synuclein.
Journal:Nat Methods
PubMed ID:17351621
'Alpha-synuclein is a major component of intraneuronal protein aggregates constituting a distinctive feature of Parkinson disease. To date, fluorescence imaging of dynamic processes leading to such amyloid deposits in living cells has not been feasible. To address this need, we generated a recombinant alpha-synuclein (alpha-synuclein-C4) bearing a tetracysteine target for