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1122484-77-8

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1122484-77-8 Usage

General Description

The chemical [2-(2-aminoethoxy)ethoxy]acetic acid tert-butyl ester, also known as Tert-butyl ([2-(2-aminoethoxy)ethoxy]acetyl)carbamate, is a compound with the molecular formula C10H21NO5. It is a tert-butyl ester derivative of [2-(2-aminoethoxy)ethoxy]acetic acid, and is commonly used as a reagent in organic synthesis and as a building block for the creation of other organic compounds. The compound has potential applications as a pharmaceutical intermediate or in the development of new materials. It is important to handle this chemical with caution and adhere to safety protocols as it may pose hazards if not properly managed.

Check Digit Verification of cas no

The CAS Registry Mumber 1122484-77-8 includes 10 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 7 digits, 1,1,2,2,4,8 and 4 respectively; the second part has 2 digits, 7 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 1122484-77:
(9*1)+(8*1)+(7*2)+(6*2)+(5*4)+(4*8)+(3*4)+(2*7)+(1*7)=128
128 % 10 = 8
So 1122484-77-8 is a valid CAS Registry Number.

1122484-77-8Relevant articles and documents

TARGET PROTEIN EED DEGRADATION-INDUCING DEGRADUCER, PREPARATION METHOD THEREOF, AND PHARMACEUTICAL COMPOSITION FOR PREVENTING OR TREATING DISEASES RELATED TO EED, EZH2, OR PRC2, COMPRISING SAME AS ACTIVE INGREDIENT

-

, (2021/12/23)

The present invention relates to a target protein degradation-inducing Degraducer, a preparation method thereof, and a pharmaceutical composition for preventing or treating diseases related to EED, EZH2, or PRC2 comprising same as an active ingredient. A novel compound represented by formula 1, according to the present invention is a Degraducer compound that induces degradation of a target protein, i.e., embryonic ectoderm development (EED) or polycomb repressive complex 2 (PRC2), utilizing cereblon E3 ubiquitin ligase, von Hippel-Lindau tumor suppressor (VHL) E3 ubiquitin ligase, mouse double minute 2 homolog (MDM2) E3 ubiquitin ligase, and cellular inhibitor of apoptosis protein 1 (cIAP) E3 ubiquitin ligase, wherein the compound has an aspect of remarkably achieving target protein degradation-inducing activity through a ubiquitin proteasome system (UPS), and therefore there is a useful effect in that it is possible to provide a pharmaceutical composition for preventing or treating diseases or conditions related to a target protein, and a functional health food composition for preventing or improving same, comprising said compound as an active ingredient.

Design, characterization and cellular uptake studies of fluorescence-labeled prototypic cathepsin inhibitors

Kohl, Franziska,Schmitz, Janina,Furtmann, Norbert,Schulz-Fincke, Anna-Christina,Mertens, Matthias D.,Küppers, Jim,Benkhoff, Marcel,Tobiasch, Edda,Bartz, Ulrike,Bajorath, Jürgen,Stirnberg, Marit,Gütschow, Michael

, p. 10310 - 10323 (2015/10/28)

Besides their extracellular activity crucial for several pathophysiological conditions, human cysteine cathepsins, in particular cathepsins K and S, represent important intracellular targets for drug development. In the present study, a prototypic dipeptide nitrile inhibitor structure was equipped with a coumarin moiety to function as a fluorescent reporter group. In a second inhibitor, a PEG linker was introduced between the dipeptide nitrile and the fluorophore. These tool compounds 6 and 7 were characterized by kinetic investigations as covalent reversible inhibitors of human cathepsins L, S, K and B. Probe 6 showed a pronounced inhibitory activity against cathepsins K and S, which was corroborated by modeling of inhibition modes. Probe 7 was highly potent (Ki = 93 nM) and selective for cathepsin S. To examine the ability of both probes to enter living cells, human embryonic kidney 293 cells were targeted. At a concentration of 10 μM, cellular uptake of probe 6 was demonstrated by fluorescence measurement after an incubation time of 30 min and 3 h, respectively. The probe's concentration in cell lysates was ascertained on the basis of the emission at 492 nm upon excitation at 450 nm, and the results were expressed as concentrations of probe 6 relative to the protein concentration originating from the lysate. After incubation of 10 μM of probe 6 for 3 h, the cellular uptake was confirmed by fluorescence microscopy. HPLC was used to assess the probes' lipophilicity, and the obtained log:D7.4 value of 2.65 for probe 6 was in agreement with the demonstrated cellular uptake.

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