化驗
≥95%
形狀
liquid
儲存溫度
−20°C
應用
Enantioprobe (R)-5 is one of 16 fully functionalized, enantiomeric fragment probes developed in the Cravatt. Combining fragment-based ligand discovery (FBLD) with chemical proteomics, the enantioprobe library assesses ligandability across proteomes. Each enantioprobe contains a structurally variable fragment for interaction with proteins photoactivatable diazirine for UV-induced covalent protein labeling, and bioorthogonal alkyne handle for detection, enrichment, and identification. Of the eight enantiomeric pairs, each differs by one stereocenter, and comparing stereoselective fragment-protein interactions between the pairs simplifies validation of authentic protein-binding events. Enantioprobe (R)-5′s paired fragment is available as Enantioprobe (S)-5 (cat# 912689).
Together, the 16 enantioprobes support ligandability studies in living cells, a significant method for development of chemical probes and lead discovery efforts to find binders for traditionally ″undruggable″ protein targets. This strategy is also compatible with multiplexing for higher throughput.
Together, the 16 enantioprobes support ligandability studies in living cells, a significant method for development of chemical probes and lead discovery efforts to find binders for traditionally ″undruggable″ protein targets. This strategy is also compatible with multiplexing for higher throughput.
Supporting reagents:
- Fluorophore-conjugated azide tags for SDS-PAGE in-gel profiling: 910147, 760757, 760765, 777315, 777323
- Azide-biotin tags for enrichment: 901765, 914134, 914460, 762024, 900912, 900891, QBD10825)
- Azide capture solid supports: 900957, 742627
- Streptavidin for biotin enrichment: S6940, E5529, E2513, 69203, 16-126, S1638
- Mass spectrometry and Multiplexing
相關產品
产品编号
说明
价格
儲存類別代碼
11 - Combustible Solids
水污染物質分類（WGK）
WGK 3
閃點（°F）
Not applicable
閃點（°C）
Not applicable
Yujia Wang et al.
Nature chemistry, 11(12), 1113-1123 (2019-10-30)
A fundamental challenge in chemical biology and medicine is to understand and expand the fraction of the human proteome that can be targeted by small molecules. We recently described a strategy that integrates fragment-based ligand discovery with chemical proteomics to
相关内容
Ligandability describes the propensity of a protein target to bind a small molecule with high affinity. It is a precursor to evaluating druggability, which requires more advanced translational pharmacological effects and drug-like properties in vivo.
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