CASP8 Knockout HCT 116 Cell Line

CASP8 Knockout HCT 116 Cell Line
Cat.No.:

EDJ-KQ21053

Species:

Human

Cell Name:

HCT 116

Gene:

CASP8

Gene ID:

841

Size:

1×10⁶cells

CASP8 Knockout Cell Line (HCT116) is an exclusive upgraded CRISPR/Cas9 system-mediated gene knockout cell, with the advantages of Optimized Strategy Design, Efficient Cell Transfection, High-Performance Cas9 Protein and Hassle-Free Cell Selection.
Cat.No. EDJ-KQ21053
Product Name CASP8 Knockout HCT 116 Cell Line
Cell Line HCT 116
Cellosaurus ID CVCL_0291
Cell Line Synonyms HCT-116, HCT.116, HCT_116, HCT116, HCT116wt, HCT-116/P, HCT-116/parental, CoCL2
Gene CASP8
NCBI Gene ID
841
Gene Synonyms ALPS2B|CAP4|Casp-8|FLICE|MACH|MCH5
Summary
This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes composed of a prodomain, a large protease subunit, and a small protease subunit. Activation of caspases requires proteolytic processing at conserved internal aspartic residues to generate a heterodimeric enzyme consisting of the large and small subunits. This protein is involved in the programmed cell death induced by Fas and various apoptotic stimuli. The N-terminal FADD-like death effector domain of this protein suggests that it may interact with Fas-interacting protein FADD. This protein was detected in the insoluble fraction of the affected brain region from Huntington disease patients but not in those from normal controls, which implicated the role in neurodegenerative diseases. Many alternatively spliced transcript variants encoding different isoforms have been described, although not all variants have had their full-length sequences determined. [provided by RefSeq, Jul 2008]
Associated Diseases Colorectal Carcinoma
Morphology Adherent
Passage Ratio 1/5-1/4,2days
Complete Culture Medium mcCoy5A+10%FBS
Freezing Medium 90%FBS/Complete culture medium+10% DMSO
QC Indels validated by Sanger sequencing; sterility confirmed via microbial testing.
* For research use only. Not intended for use in humans or animals, including clinical, therapeutic, or diagnostic purposes.
LociSTR Info (Sample Cell)
Sample Cell Line: HCT 116
STR Info (Cell bank)
Cell Line: HCT 116
Allele1Allele2Allele3Allele4Allele1Allele2Allele3Allele4
Amelogenin X X
CSF1PO 7 10 7 9 10 11
D2S1338 16 16
D3S1358 12 17 18 19 12 18 19
D5S818 10 11 10 11
D7S820 11 12 11 12
D8S1179 10 12 14 15 10 12 14 15
D13S317 10 12 10 12
D16S539 11 13 11 12 13 14
D18S51 16 17 16 17
D19S433 12 13 12
D21S11 29 30 29 30
FGA 18 23 18 23
Penta D 9 13 9 13
Penta E 12 13 14 12 13 14
TH01 8 9 8 9
TPOX 8 8
vWA 17 21 22 23 17 21 22 23
D6S1043 13
D12S391 17 21 22
D2S441 11 12
* STR authentication data of this cell line matches with that of cell lines sourced from ATCC, DSMZ, JCRB, and RIKEN databases.
Conclusion: The STR identification of this cell is correct.
* Research Use Disclaimer: Content is generated from publicly available research data, bioinformatic resources, and computational analyses for research reference only.

Related Publications

IF=5.1
Communications biology
Mind bomb 2 (MIB2) is an E3 ligase involved in Notch signalling and attenuates TNF-induced apoptosis through ubiquitylation of receptor-interacting protein kinase 1 (RIPK1) and cylindromatosis. Here we show that MIB2 bound and conjugated K48- and K63-linked polyubiquitin chains to a long-form of cellular FLICE-inhibitory protein (cFLIP), a catalytically inactive homologue of caspase 8. Deletion of MIB2 did not impair the TNF-induced complex I formation that mediates NF-κB activation but significantly enhanced formation of cytosolic death-inducing signalling complex II. TNF-induced RIPK1 Ser phosphorylation, a hallmark of RIPK1 death-inducing activity, was enhanced in MIB2 knockout cells, as was RIPK1 kinase activity-dependent and -independent apoptosis. Moreover, RIPK1 kinase activity-independent apoptosis was induced in cells expressing cFLIP mutants lacking MIB2-dependent ubiquitylation. Together, these results suggest that MIB2 suppresses both RIPK1 kinase activity-dependent and -independent apoptosis, through suppression of RIPK1 kinase activity and ubiquitylation of cFLIP, respectively.

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