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, 23 bp deletion in exon 1 and Insertion of the selection cassette 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, 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-FKBP10, 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.
FKBP10 also known as FKBP65 is a protein that functions as a peptidyl-prolyl cis-trans isomerase (PPIase). This protein with a mass of approximately 65 kDa is involved in protein folding by catalyzing the isomerization of proline residues in polypeptide chains. FKBP10 is expressed in the endoplasmic reticulum of cells and it contributes to the synthesis and maturation of collagens which are essential for the structural integrity of various tissues.
Biological function summary
FKBP10 plays a critical role in ensuring proper collagen biosynthesis. It forms part of a complex involved in stabilizing the collagen triple-helix structure during its assembly in the endoplasmic reticulum. This action by FKBP10 is necessary for maintaining tissue strength and flexibility due to its involvement in cross-linking collagen fibers. This activity highlights the importance of FKBP10 in connective tissue development and maintenance.
Pathways
FKBP10 is deeply embedded in the collagen synthesis and folding processes. It interacts within the pathways that incorporate transforming growth factor-beta (TGF-β) influencing extracellular matrix formation and maintenance. FKBP10's function is linked to proteins like prolyl 4-hydroxylase which are vital for collagen modification impacting the maturation and structural stability of collagen fibrils.
FKBP10 mutations have associations with connective tissue disorders such as osteogenesis imperfecta and Ehlers-Danlos syndrome. These diseases result from defects in collagen formation and stability. FKBP10's dysfunction can lead to compromised structural properties of tissues correlating with irregularities linked to the protein HSP47 another chaperone involved in collagen processing. Understanding FKBP10's role in these diseases aids in identifying potential therapeutic targets for correcting defects in collagen biosynthesis.
