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, 10 bp deletion in exon 11 and 1 bp deletion in exon 11 and 25 bp deletion in exon 11
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-FCSK, Gene editing type-Knockout, Gene editing method-CRISPR technology, Knockout validation-Sanger Sequencing, 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 protein FUK also known as fucokinase functions mechanistically as an enzyme that catalyzes the phosphorylation of L-fucose a monosaccharide involved in various metabolic processes. The molecular mass of FUK is approximately 131 kDa. FUK is primarily expressed in the liver but also in other tissues like the kidney and brain where it performs its enzymatic role as part of cellular metabolism.
Biological function summary
FUK plays a role in the salvage pathway of L-fucose metabolism. This pathway recycles free L-fucose into GDP-fucose which becomes essential for glycoprotein and glycolipid synthesis. FUK operates not as part of a larger protein complex but individually facilitating the utilization of fucose derived from dietary sources or breakdown of glycoproteins. The enzyme regulates intracellular concentrations of fucose impacting cell surface glycoconjugates important for cell signaling.
Pathways
FUK integrates into the fucose salvage pathway that links to glycosylation processes. This situates FUK within the larger context of glycan biosynthesis pathways where it intersects with enzymes such as GDP-fucose synthase. These pathways significantly influence the modification and function of proteins and lipids on cell surfaces affecting cellular communication and host-pathogen interactions.
FUK has connections to congenital disorders of glycosylation and cancer. Deficiencies in FUK enzyme activity can lead to disrupted fucosylation which contributes to clinical features seen in glycosylation disorders. In cancer abnormal fucose metabolism affects tumor progression and metastasis involving interactions with proteins such as fucosyltransferases which modify glycans on cell surfaces. Understanding FUK's role could provide insights into therapeutic approaches for glycol-related diseases.
