Tetracysteine REASH Reagent *2 mM DMSO Solution*
REASH is a resorufin derivative, modified to contain two arsenic atoms at a set distance from each other. The biarsenical labeling technology works through the high-affinity interaction of arsenic for thiols. When REASH binds to tetracysteine sequences, its biarsenical group reacts rapidly with Cys-Cys moiety and the tag become highly fluorescent in red. The biarsenical labeling reagent REASH is one of the smallest expression tags for labeling a protein that contains a six-amino acid motif with a Cys-Cys-X1-X2-Cys-Cys amino acid sequence. The most commonly used tetracysteine is the six amino acid Cys-Cys-Pro-Gly-Cys-Cys sequence. As this sequence rarely appears in endogenous proteins, incorporating the sequence into target proteins generates a small but highly specific target for protein labeling. REASH generates a strong red fluorescent signal when binding to recombinant proteins containing the tetracysteine motif Cys-Cys-Pro-Gly-Cys-Cys. It can be used for monitoring protein localization, turnover and trafficking, receptor signaling and internalization.
Spectrum
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Product family
Name | Excitation (nm) | Emission (nm) | Extinction coefficient (cm -1 M -1) | Quantum yield | Correction Factor (260 nm) | Correction Factor (280 nm) |
Tetracysteine FLASH Reagent *2 mM DMSO Solution* | 498 | 517 | 800001 | 0.79001, 0.952 | 0.32 | 0.35 |
Tetracysteine REASH acetate *2 mM DMSO Solution* | 571 | 584 | 650001 | 0.751 | - | - |
References
View all 8 references: Citation Explorer
Discrete Virus Factories Form in the Cytoplasm of Cells Coinfected with Two Replication-Competent Tagged Reporter Birnaviruses That Subsequently Coalesce over Time.
Authors: Campbell, Elle A and Reddy, Vishwanatha R A P and Gray, Alice G and Wells, Joanna and Simpson, Jennifer and Skinner, Michael A and Hawes, Philippa C and Broadbent, Andrew J
Journal: Journal of virology (2020)
Authors: Campbell, Elle A and Reddy, Vishwanatha R A P and Gray, Alice G and Wells, Joanna and Simpson, Jennifer and Skinner, Michael A and Hawes, Philippa C and Broadbent, Andrew J
Journal: Journal of virology (2020)
Tetracysteine-based fluorescent tags to study protein localization and trafficking in Plasmodium falciparum-infected erythrocytes.
Authors: Crivat, Georgeta and Tokumasu, Fuyuki and Sa, Juliana Martha and Hwang, Jeeseong and Wellems, Thomas E
Journal: PloS one (2011): e22975
Authors: Crivat, Georgeta and Tokumasu, Fuyuki and Sa, Juliana Martha and Hwang, Jeeseong and Wellems, Thomas E
Journal: PloS one (2011): e22975
Hairpin structure of a biarsenical-tetracysteine motif determined by NMR spectroscopy.
Authors: Madani, Fatemeh and Lind, Jesper and Damberg, Peter and Adams, Stephen R and Tsien, Roger Y and Gräslund, Astrid O
Journal: Journal of the American Chemical Society (2009): 4613-5
Authors: Madani, Fatemeh and Lind, Jesper and Damberg, Peter and Adams, Stephen R and Tsien, Roger Y and Gräslund, Astrid O
Journal: Journal of the American Chemical Society (2009): 4613-5
Helix A stabilization precedes amino-terminal lobe activation upon calcium binding to calmodulin.
Authors: Chen, Baowei and Lowry, David F and Mayer, M Uljana and Squier, Thomas C
Journal: Biochemistry (2008): 9220-6
Authors: Chen, Baowei and Lowry, David F and Mayer, M Uljana and Squier, Thomas C
Journal: Biochemistry (2008): 9220-6
Preparation of the membrane-permeant biarsenicals FlAsH-EDT2 and ReAsH-EDT2 for fluorescent labeling of tetracysteine-tagged proteins.
Authors: Adams, Stephen R and Tsien, Roger Y
Journal: Nature protocols (2008): 1527-34
Authors: Adams, Stephen R and Tsien, Roger Y
Journal: Nature protocols (2008): 1527-34
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