4 Results for "

ClpC1P1P2

" in MedChemExpress (MCE) Product Catalog:
Products (4)

4 Results for "ClpC1P1P2" in MCE Product Catalog:

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Cat. No.: HY-153575
Target:  

PROTACs Bacterial

Research Areas:  

Infection

BacPROTAC-1 is a BacPROTAC degrader that induces the degradation of the target protein mSA by recruiting ClpC/ClpC1. BacPROTAC-1 binds to mSA, Bacillus subtilis ClpCNTD and Mycobacterium smegmatis ClpC1NTD with Kd values of 3.9, 2.8 and 0.69 μM, respectively. BacPROTAC-1 forms a ternary complex between the substrate and ClpC, promotes ClpC reassembly and activation, and induces ATP-dependent degradation of mSA and mSA fusion model substrates via the ClpCP or ClpC1P1P2 protease system. BacPROTAC-1 can be used in studies on bacterial targeted protein degradation, bacterial protein homeostasis and antibacterial target discovery .
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Cat. No.: HY-153574
Synonyms: pArg-JQ1
Research Areas:  

Infection

BI01826025 (pArg-JQ1) is a BacPROTAC-type bifunctional degrader that induces the degradation of BRDTBD1-containing substrates by recruiting the ClpC1P1P2 protease system. BI01826025 binds to the BRDTBD1 substrate via its JQ1 moiety and to ClpC1 via its pArg moiety; it delivers the substrate to ClpC1, where the substrate undergoes ClpC1-mediated unfolding followed by proteolysis by ClpP1P2. BI01826025 can be used to study ClpC1P1P2-mediated targeted protein degradation and ClpC2-regulated bacterial protein homeostasis .
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Cat. No.: HY-153573
Synonyms: dCym-JQ1
Research Areas:  

Infection

SRG-II-19F (dCym-JQ1) is a BRDTBD1 PROTAC degrader. Its dCym moiety at one end binds to the N-terminal domain of ClpC1 (ClpC1NTD), while its JQ1 moiety at the other end binds to bromodomain 1 of BRDT (BRDTBD1). This molecule induces the degradation of BRDTBD1 by recruiting the BRDTBD1 substrate to the ClpC1P1P2 protease complex. SRG-II-19F serves as a research tool for studies related to mycobacterial protein degradation .
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Cat. No.: HY-189712
Target:  

ClpP Bacterial

Research Areas:  

Infection

ADEP 19 is a ClpP1P2 dysregulator with antibacterial activity against Mycobacterium tuberculosis and various Gram-positive bacteria. ADEP 19 binds to the ClpP2 subunit of Mycobacterium tuberculosis, disrupting ClpP1P2-ClpX/ClpC1 chaperone interactions. ADEP 19 inhibits ClpC1P1P2-mediated proteolytic activity (IC50 = 1.2 μM) while upregulating the ATP hydrolysis activity of ClpXP1P2. ADEP 19 exhibits synergistic effects with Bedaquiline (HY-14881) against Mycobacterium tuberculosis. ADEP 19 can be used in research related to bacterial infections, such as tuberculosis .
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