产品名称
Iodoacetamide Alkyne-C3, ≥95% (HPLC), powder, acysteine-reactive ABPP benchmark probe
SMILES string
O=C(CI)NCC#C
assay
≥95% (HPLC)
form
powder
color
white to beige
solubility
DMSO: 2 mg/mL, clear
storage temp.
-10 to -25°C
Quality Level
Application
Iodoacetamide Alkyne-C3 is suitable for use in isotopic tagging strategies for quantitative cysteine-reactivity profiling in various biological samples.
Biochem/physiol Actions
Iodoacetamide alkyne-C3 (IPM, IAA-C3, IA-alkyne-C3, IAM-alkyne-C3) is a bifunctional, thiol-reactive probe engineered for activity-based protein profiling (ABPP) of reactive cysteine residues in live cells, tissue homogenates, and tissues. This probe combines an iodoacetamide group, functioning as a covalent warhead for selective cysteine labeling, with a C3 alkyne moiety that acts as a click-chemistry handle. This alkyne allows for the subsequent conjugation of fluorophores or biotin-linked azido reporters, facilitating either the visualization or enrichment of labeled proteins. The IAA-C3 probe, the gold standard in the cysteinomics field, facilitates site-specific analysis of cysteine accessibility, reactivity, redox modification status, and covalent engagement in biological samples by allowing researchers to treat cell homogenates with varying concentrations of IA-alkyne C3, identifying highly reactive cysteines-such as those in enzyme active sites or redox-sensitive regions-that remain reactive despite dilution effects.
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John S Coukos et al.
ACS chemical biology, 18(1), 91-101 (2022-12-24)
Methylglyoxal (MGO), a reactive metabolite byproduct of glucose metabolism, is known to form a variety of posttranslational modifications (PTMs) on nucleophilic amino acids. For example, cysteine, the most nucleophilic proteinogenic amino acid, forms reversible hemithioacetal and stable mercaptomethylimidazole adducts with
Masahiro Abo et al.
Molecular pharmaceutics, 15(3), 743-749 (2017-11-28)
Cysteine residues on proteins serve a variety of catalytic and regulatory functions due to the high nucleophilicity and redox activity of the thiol group. Quantitative proteomic platforms for profiling cysteine reactivity can provide valuable information related to the post-translational modification
Ling Fu et al.
Nature protocols, 15(9), 2891-2919 (2020-07-22)
Cysteine is unique among all protein-coding amino acids, owing to its intrinsically high nucleophilicity. The cysteinyl thiol group can be covalently modified by a broad range of redox mechanisms or by various electrophiles derived from exogenous or endogenous sources. Measuring
Romain Tessier et al.
Angewandte Chemie (International ed. in English), 59(27), 10961-10970 (2020-04-02)
Current approaches to introduce terminal alkynes for bioorthogonal reactions into biomolecules still present limitations in terms of either reactivity, selectivity, or adduct stability. We present a method for the ethynylation of cysteine residues based on the use of ethynylbenziodoxolone (EBX)
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