Description
Key facts
Cell type:HEK-293T,
Species or organism:Human,
Tissue:Kidney,
Form:LiquidSee storage information,
Knockout validation:Sanger Sequencing,
Mutation description:Knockout achieved by using CRISPR/Cas9, Homozygous: 2 bp deletion in exon 1
Product details:
We will provide viable cells that proliferate on revival.
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
patent pages
Properties and Storage Information:
Gene name-FUCA2, 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.
The FUCA2 protein also known as plasma alpha-L-fucosidase 2 acts mechanically by hydrolyzing the alpha-16-linked fucose residues from glycoproteins and glycolipids. FUCA2 weighs approximately 53 kDa and localizes mainly to the human liver and blood plasma. Its enzymatic activity helps maintain proper cell surface carbohydrate structures which play important roles in cell-cell communication and adhesion.
Biological function summary
FUCA2 participates in the degradation of fucosylated glycoconjugates. It does not form part of a larger complex; however it operates in concert with other glycosidases to ensure efficient turnover of glycoproteins and glycolipids. This turnover is important in maintaining cellular and systemic homeostasis influencing processes like immune response and inflammatory regulation.
Pathways
FUCA2 is involved in the lysosomal degradation pathway and also interacts within the glycosphingolipid metabolism pathway. It cooperates with proteins like alpha-L-fucosidase 1 (FUCA1) to facilitate the catabolism of glycostructures. These metabolic pathways are essential for recycling cellular materials and processing complex sugar molecules highlighting their role in maintaining cellular efficiency.
FUCA2 presents a connection with fucosidosis and certain cancers such as hepatocellular carcinoma. Its dysfunction can lead to abnormal accumulation of fucosylated compounds contributing to the development of lysosomal storage disorders. In cancer its activity coupled with proteins like alpha-L-fucosidase 3 (FUCA3) may affect the tumor microenvironment influencing cancer cell proliferation and metastasis through altered glycosylation patterns.
