Key facts
Cell type:HeLa,
Species or organism:Human,
Tissue:Cervix,
Knockout validation:Sanger Sequencing,Western blot,
Mutation description:Knockout achieved by using CRISPR/Cas9, Homozygous: 1 bp insertion in exon 2,
Disease:Adenocarcinoma
Product details:
A collection of 6 knockout cell lines involved in the apoptotic cell death pathways, in one kit for your convenience, with matching parental cell lines.
Find out more about our apoptosis assays
Included in this panel:
FAS knockout HeLa cell Line (ab265260) + recommended control (ab255928)
FADD knockout HeLa cell Line (ab261817) + recommended control (ab255928)
DAXX knockout HeLa cell Line (ab265233) + recommended control (ab255928)
CASP8 knockout HeLa cell Line (ab264958) + recommended control (ab255448)
BAX knockout HeLa cell Line (ab255363) + recommended control (ab255448)
RIPK2 (RIP2) knockout HeLa cell Line (ab264688) + recommended control (ab255448)
Parts of the panels can be purchased separately. For further details please contact
[email protected].
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-FAS, Gene editing type-Knockout, Gene editing method-CRISPR technology, Knockout validation-Sanger Sequencing, Western blot, 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.
FADD Bax Daxx Fas RIP2 and Caspase-8 are vital components in cell death processes. Mechanically these proteins interact to regulate apoptosis necroptosis and cellular stress responses. FADD (Fas-Associated protein with Death Domain) is a 23-kDa cytoplasmic adaptor protein actively engaged in transducing apoptotic signals. Caspase-8 often associated with initiator caspases exists primarily in the cytoplasm with an approximate mass of 55 kDa and initiates apoptosis by cleaving downstream effector caspases. Fas a cell surface receptor sometimes called CD95 triggers apoptosis upon ligand binding. Bax a pro-apoptotic member of Bcl-2 family facilitates mitochondrial membrane permeabilization. Daxx or Death-domain associated protein can shuttle between the nucleus and cytoplasm influencing apoptosis and transcription regulation. RIP2 (also known as RIPK2) is a serine/threonine-protein kinase that contributes to innate immune responses.
Biological function summary
FADD Bax Daxx Fas RIP2 and Caspase-8 play key roles in mediating apoptotic pathways. FADD forms complexes with death receptors like Fas to initiate apoptotic signaling cascades. Daxx reportedly binds death receptors modulating apoptotic activities. Caspase-8 freely catalyzes the activation of downstream caspase enzymes effectively driving the cell toward apoptotic execution. Bax integration into mitochondrial pathways disrupts membrane potential releasing cytochrome c that further supports caspase-9 activation. RIP2 while known for immune responses also synergizes with these apoptotic players in certain contexts. These proteins collectively orchestrate a balance of cell survival and death essential for normal cellular homeostasis and tissue development.
Pathways
FADD Bax Daxx Fas RIP2 and Caspase-8 are fundamental to the extrinsic apoptosis and necroptosis pathways. In the extrinsic pathway Fas ligation triggers FADD recruitment which then binds with death effector domain to activate Caspase-8 facilitating the apoptotic cascade. The involvement of Bax influences the mitochondrial apoptosis pathway by promoting cytochrome c release following intrinsic apoptotic signals. RIP2 though more common in inflammatory pathways may cross-interact with these proteins in the context of cellular stress responses. These interactions highlight a tight regulatory network with precise cross-communication between apoptotic and survival signals.
Disrupted regulation of FADD Bax Daxx Fas RIP2 and Caspase-8 connects significantly with cancer and autoimmune diseases. Deregulated Fas-mediated apoptosis often appears in various cancer forms where deficient apoptosis contributes to uncontrolled cell proliferation. Caspase-8 mutations or impaired expression link to neurodegenerative diseases and some cancers due to unregulated cell death. In autoimmune diseases like systemic lupus erythematosus abnormal expression of Fas and related apoptotic proteins like Daxx may participate in perpetuating an immune attack on self-cells. The core connection of these proteins to apoptosis and immune regulation underlines their potential as therapeutic targets in these pathological states.
