USP44 Protein, Human (GST)

The USP44 protein is a key deubiquitinase that regulates the spindle assembly checkpoint and prevents premature initiation of anaphase by deubiquitinating CDC20. This stabilizes the MAD2L1-CDC20-APC/C complex and enhances the spindle assembly checkpoint. USP44 Protein, Human (GST) is the recombinant human-derived USP44 protein, expressed by E. coli , with N-GST labeled tag. The total length of USP44 Protein, Human (GST) is 712 a.a., .

The USP44 Protein, featured in this description, assumes a pivotal role as a deubiquitinase in the regulation of the spindle assembly checkpoint or mitotic checkpoint, crucial for preventing premature anaphase onset during cell division. It achieves this by specifically mediating the deubiquitination of CDC20, a negative regulator of the anaphase-promoting complex/cyclosome (APC/C). This deubiquitination event stabilizes the MAD2L1-CDC20-APC/C ternary complex, forming the mitotic checkpoint complex, ultimately preventing premature activation of the APC/C and reinforcing the spindle assembly checkpoint. USP44 extends its regulatory reach by promoting the deubiquitination of histone H2A and H2B. Additionally, it is recruited to RNF8/RNF168-ubiquitinated chromatin surrounding double-stranded breaks, where it negatively regulates protein recruitment to damaged chromatin. USP44 also participates in the nucleotide excision repair pathway by deubiquitinating DDB2, preventing its premature degradation on damaged chromatin. Furthermore, it plays a role in promoting FOXP3 stabilization through 'Lys-48'-linked deubiquitination, enhancing regulatory T-cell lineage stability, and positively contributes to the innate immune response to DNA viruses by deubiquitinating STING1 and stabilizing it. This multifaceted role underscores the importance of USP44 in orchestrating key cellular processes.

Human

E. coli

N-GST

Q9H0E7 (M1-S712)

84101

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.