USP1 KO cell lysate available now. Free of charge wild type control included. Knockout achieved by using CRISPR/Cas9, 1 bp deletion in exon3.
Deubiquitinating enzyme 1, UBP, UBP1_HUMAN, Ubiquitin carboxyl-terminal hydrolase 1, Ubiquitin specific peptidase 1, Ubiquitin specific protease 1, Ubiquitin thioesterase 1, Ubiquitin thiolesterase 1, Ubiquitin-specific-processing protease 1, hUBP
USP1 KO cell lysate available now. Free of charge wild type control included. Knockout achieved by using CRISPR/Cas9, 1 bp deletion in exon3.
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Lysate preparation: Our lysates are made using RIPA buffer to which we add a protease inhibitor cocktail and phosphatase inhibitor cocktail (ratio: 300:100:10). This means that the protein of interest is denatured. If you require a native form of the protein please use the live cell version. Please refer to our lysis protocol for further details on how our lysates are prepared.
User storage instructions: Lyophilizate may be stored at 4°C. After reconstitution, store at -20°C for short-term storage or -80°C for long-term storage.
This product is subject to limited use licenses from The Broad Institute and ERS Genomics Limited, and is developed with patented technology. For full details of the limited use licenses and relevant patents please refer to our limited use license and patent pages.
USP1 also known as ubiquitin-specific peptidase 1 is a deubiquitinating enzyme with a molecular mass of approximately 88 kDa. It removes ubiquitin from protein substrates especially those involved in DNA repair processes. USP1 is widely expressed in human tissues with high expression in the testis and moderate levels in the lungs brain and heart. It forms a complex with UAF1 which enhances its catalytic activity and stability.
USP1 plays a critical part in maintaining genomic stability by regulating key proteins in the DNA damage response. It specifically deubiquitinates FANCD2 and PCNA proteins important for the Fanconi anemia pathway and translesion DNA synthesis respectively. This action prevents the accumulation of ubiquitinated proteins ensuring proper progression of DNA repair processes. The interaction with UAF1 forms a functional complex important for its activity in vivo.
USP1 is significant in the Fanconi anemia (FA) and translesion synthesis pathways. Its interaction with FANCD2 involves DNA repair by promoting error-free replication across DNA lesions. USP1 also acts on proliferating cell nuclear antigen (PCNA) a protein important for translesion synthesis that enables DNA replication to occur past unrepaired lesions. These pathways highlight USP1’s importance in DNA repair and replication linking it to other proteins like RAD18 which is involved in PCNA ubiquitination.
Research implicates USP1 in cancer and Fanconi anemia. In certain cancers altered USP1 expression can lead to increased DNA repair activity contributing to chemoresistance. USP1’s interaction with FANCD2 makes it pertinent to Fanconi anemia where its malfunction can cause DNA repair defects associated with the disease. Understanding USP1’s role alongside proteins like BRCA1 which interacts with DNA damage repair mechanisms can guide targeted therapeutic strategies.
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Homozygous: 1 bp deletion in exon3
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