Description
Key facts
Cell type:HeLa,
Species or organism:Human,
Tissue:Cervix,
Form:LiquidSee storage information,
Knockout validation:Sanger Sequencing,
Mutation description:Knockout achieved by using CRISPR/Cas9, Homozygous: 1 bp insertion in exon 6,
Disease:Adenocarcinoma
Product details:
We will provide viable cells that proliferate on revival.
This product is subject to limited use licenses from The Broad Institute, ERS Genomics Limited and Sigma-Aldrich Co. LLC, and is developed with patented technology. For full details of the licenses and patents please refer to our
limited use license
patent pages
Properties and Storage Information:
Gene name-CBLL1, Gene editing type-Knockout, Gene editing method-CRISPR technology, Knockout validation-Sanger Sequencing, Zygosity-Homozygous, Shipped at conditions-Dry Ice, Appropriate short-term storage conditions--196°C, Appropriate long-term storage conditions--196°C
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
CBLL1 also known as Hakai is an E3 ubiquitin ligase. Its molecular weight is approximately 65 kDa and it functions by mediating ubiquitination which leads to the controlled degradation of target proteins. CBLL1 is expressed in several tissues including heart liver and kidney. The protein predominantly functions within the cytoplasm but can also translocate to the nucleus to exert its enzymatic activities.
Biological function summary
CBLL1 plays a significant role in cellular processes such as endocytosis cell adhesion and regulation of epithelial-mesenchymal transition (EMT). CBLL1 functions as part of a complex that helps target proteins for degradation through the ubiquitin-proteasome system. This activity is especially relevant in the regulation of cell signaling pathways where it targets various substrates such as E-cadherin for ubiquitination.
Pathways
CBLL1 is important in modulating signaling cascades like the Wnt and TGF-beta pathways. By influencing these pathways CBLL1 interacts with proteins like beta-catenin and SMADs. The degradation of E-cadherin by CBLL1 facilitates cellular detachment and migration a critical step in cellular processes regulated by these pathways.
CBLL1's involvement in the ubiquitin-proteasome system links it to cancer development and progression. The protein's regulation of EMT and cell adhesion implicates it in cancers such as gastric and colon cancers. Additionally CBLL1 interacts with proteins like beta-catenin in Wnt signaling which is often dysregulated in these cancers. Understanding the function of CBLL1 may offer potential therapeutic targets for combating these malignancies.
