439791-28-3

Usage

Uses

Used in Biomedical Research:
CrAsH is used as a fluorescent labeling agent for the specific detection and visualization of recombinant proteins in living cells. Its low non-specific fluorescence allows for clear and accurate imaging, making it a valuable tool in various research applications.
Used in Drug Discovery and Development:
CrAsH can be employed as a biarsenical probe in the development of new drugs and therapeutic agents. Its ability to selectively label proteins of interest can aid in the identification of potential drug targets and the evaluation of drug efficacy.
Used in Diagnostic Applications:
In the field of diagnostics, CrAsH can be utilized for the detection and monitoring of specific proteins associated with various diseases. Its site-specific labeling capabilities can contribute to the development of more accurate and sensitive diagnostic tests.
Used in Bioimaging Techniques:
CrAsH's fluorescent properties make it suitable for use in various bioimaging techniques, such as fluorescence microscopy and flow cytometry. It can be employed to study protein dynamics, cellular processes, and other biological phenomena in living cells.

Upstream product

• 540-63-6 ethane-1,2-dithiol 
• 76823-03-5 5-carboxyfluoroscein 

Relevant academic research and scientific papers

Synthesis of Arylazide- and Diazirine-Containing CrAsH-EDT2 Photoaffinity Probes

Two photo-crosslinking biarsenical (CrAsH-EDT2)-modified probes were synthesized that are expected to be useful tools for tetracysteine-labeled proteins to facilitate the co-affinity purification of their DNA binding sequences and interacting proteins. In addition, improvements for the synthesis of CrAsH-EDT2 and N1-(4-azido-2-nitrophenyl)hexane-1,6-diamine are reported. Both photoprobes effectively entered HeLa cells (and the nucleus) and were dependent on the tetracysteine motif in recombinant DMRT1 (doublesex and Mab3-related transcription factor) to induce fluorescence, suggesting that their crosslinking abilities can be exploited for the identification of nucleic acids and proteins associated with a protein of interest.

A FlAsH-based cross-linker to study protein interactions in living cells

As you like it: xCrAsH, a dimeric derivative of the arsenical compound FlAsH, enables the highly specific, covalent cross-linking of two proteins containing a 12 amino acid peptide tag. This inducible and (by addition of dithiols) reversible system can be used to detect and manipulate protein-protein interactions both in vitro and in living cells (see picture). Copyright

New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: Synthesis and biological applications

We recently introduced a method (Griffin, B. A.; Adams, S. R.; Tsien, R. Y. Science 1998, 281, 269-272 and Griffin, B. A.; Adams, S. R.; Jones, J.; Tsien, R. Y. Methods Enzymol. 2000, 327, 565-578) for site-specific fluorescent labeling of recombinant proteins in living cells. The sequence Cys-Cys-Xaa-Xaa-Cys-Cys, where Xaa is an noncysteine amino acid, is genetically fused to or inserted within the protein, where it can be specifically recognized by a membrane-permeant fluorescein derivative with two As(III) substituents, FlAsH, which fluoresces only after the arsenics bind to the cysteine thiols. We now report kinetics and dissociation constants (～10-11 M) for FlAsH binding to model tetracysteine peptides. Affinities in vitro and detection limits in living cells are optimized with Xaa-Xaa = Pro-Gly, suggesting that the preferred peptide conformation is a hairpin rather than the previously proposed α-helix. Many analogues of FlAsH have been synthesized, including ReAsH, a resorufin derivative excitable at 590 nm and fluorescing in the red. Analogous biarsenicals enable affinity chromatography, fluorescence anisotropy measurements, and electron-microscopic localization of tetracysteine-tagged proteins.