Results for PEG ( 6581 )
BP Lipid 449 is a novel analog of the ionizable lipid LP01 whose key feature is the introduction of a bis cyclopropyl fatty acid tail. This alteration has been designed to investigate the effect on the dynamics of lipid nanoparticles as cyclopropane fatty acids have been reported to affect the fluidity and structure of lipid bilayers in response changes in temperature and pH (J. Phys. Chem. B 2014, 118, 48, 13838–13848). Reagent grade, for research purpose. Please contact us for GMP-grade inquiries.
N-Mal-N-bis(PEG4-acid-amido-PEG24-t butyl ester) serves as a branched maleimide ester. The maleimide group will react with a thiol group, enabling the connection of a biomolecule with a thiol. The t-butyl ester can be hydrolyzed under acidic conditions. The hydrophilic PEG spacers enhance the water-solubility of the molecule.
N-Mal-N-bis(PEG4-acid-amido-PEG24-acid) functions as a maleimide PEG reagent with two terminal carboxylic acids and a maleimide (Mal) group. Maleimide (Mal) reacts specifically with sulfhydryl groups to form a stable thioether linkage when the pH is between 6.5 and 7.5. The terminal carboxylic acids can conjugate with amine-containing molecules in the presence of activators (e.g. HATU). The PEG linkages improve the compound's water solubility.
DOTA-PEG8-amine, HCl salt represents a PEG linker possessing a DOTA moiety, which can be used as a chelating agent for cations and is commonly used for imaging diagnostics. The amine group is reactive toward carboxylic acids, activated NHS esters, etc. The hydrophilic PEG chain enhances the solubility of compounds in aqueous media.
CC-885 serves as a PROTAC which modulates the activity of cereblon (CRBN), a key protein involved in protein regulation. It facilitates the targeted ubiquitination and degradation of PLK1 by specifically engaging CRBN and the ATPase enzyme p97. Through this mechanism, CC-885 alters the stability and turnover of PLK1, a protein involved in cell cycle regulation.
Golcadomide (CC-99282) is a potent, orally active modulator of the CRBN E3 ligase. It engages with the CRL4-CRBN complex, promoting the recruitment and ubiquitin-dependent degradation of the transcription factors Ikaros and Aiolos. This selective modulation of protein degradation pathways highlights its utility for research in cell regulation and related fields.
ALV2 is a potent, selective degrader of the zinc-finger transcription factor Helios, which plays a role in maintaining Treg cell stability. By binding to cereblon (CRBN) with an IC50 of 0.57 μM, ALV2 promotes targeted Helios degradation, making it valuable for research involving transcriptional regulation and immune cell behavior.