FUS Knockout HEK293 Cell Line

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FUS Knockout HEK293 Cell Line
Cat.No.:

EDC07631

Species:

Human

Cell Name:

HEK293

Gene:

FUS

Gene ID:

2521

Size:

1×10⁶cells

FUS Knockout HEK293 Cell Line is an exclusive upgraded CRISPR/Cas9 system-mediated gene knockout cell, with the advantages of Optimized Strategy Design, Efficient Cell Transfection, High-Performotion Cas9 Protein and Hassle-Free Cell Selection.
Cat.No. EDC07631
Product Name FUS Knockout HEK293 Cell Line
Species Human
Cell Line HEK293
Cellosaurus ID CVCL_0045
Cell Line Synonyms Hek293, HEK-293, HEK/293, (HEK)293, HEK 293, HEK,293, 293, 293 HEK, 293 Ad5, Graham 293, Graham-293, Human Embryonic Kidney 293
Gene ID
Gene FUS
Gene Synonyms ALS6|ETM4|FUS1|HNRNPP2|POMP75|TLS|altFUS
Summary
This gene encodes a multifunctional protein component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complex. The hnRNP complex is involved in pre-mRNA splicing and the export of fully processed mRNA to the cytoplasm. This protein belongs to the FET family of RNA-binding proteins which have been implicated in cellular processes that include regulation of gene expression, maintenance of genomic integrity and mRNA/microRNA processing. Alternative splicing results in multiple transcript variants. Defects in this gene result in amyotrophic lateral sclerosis type 6. [provided by RefSeq, Sep 2009]
Digestion Time ~1 min
Associated Diseases Non-tumor
Morphology Adherent
Passage Ratio 1:3
Complete Culture Medium DMEM+10% FBS
Freezing Medium 95% complete culture medium + 5% DMSO
* 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: HEK293		STR Info (Cell bank)
Cell Line: HEK293
Allele1Allele2Allele1Allele2
Amelogenin X X
CSF1P0 12 11 12
D2S1338 19 19
D3S1358 15 17 15 17
D5S818 8 8 9
D7S820 11 12 11 12
D8S1179 12 14 12 14
D13S317 12 14 12 14
D16S539 9 13 9 13
D18S51 17 18 17 18
D19S433 15 18 15 18
D21S11 28 30.2 28 30.2
FGA 23 23
Penta D 9 10 9 10
Penta E 7 15 7 15
TH01 7 9.3 7 9.3
TPOX 11 11
vWA 16 19 16 19
D6S1043 11 11
D12S391 19 21 11 15
D2S441 11 15 11 15
* 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.

FAQ

The choice depends on whether you are studying FUS (fused in sarcoma)'s role as a multifunctional RNA-binding protein or modeling FUS-related amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). The Knockout line is the standard tool for asking whether FUS is required for these processes — FUS is a nuclear RNA/DNA-binding protein that participates in RNA processing, DNA damage response, and biomolecular condensate formation (through its low-complexity prion-like domain); FUS is one of the canonical ALS/FTD genes with mutations causing cytoplasmic FUS aggregation and motor neuron degeneration. Overexpression of mutant FUS is useful for studying gain-of-function ALS mutations. For ALS/FTD research, the EDITGENE FUS Knockout in HEK293 is highly informative — FUS loss-of-function phenotypes contribute to disease alongside aggregate-mediated gain-of-function mechanisms. Rescue with wild-type or ALS-associated mutant (R521C, R521H, P525L — these are NLS mutations that cause cytoplasmic FUS aggregation) FUS enables disease genotype-function studies. The knockout is valuable for studying RNA-binding protein biology, biomolecular condensate formation, stress granule dynamics, and emerging FUS-targeted therapeutic approaches in ALS/FTD.
Primary applications: • RNA-binding protein function: CLIP-seq or PAR-CLIP analysis to characterize FUS-bound RNAs in the absence/presence of FUS. • Stress granule dynamics: G3BP1+ stress granule formation following stress stimuli (sodium arsenite, heat shock) given FUS's role in stress granule assembly. • ALS modeling: rescue with R521C, R521H, P525L NLS mutations for genotype-function studies of FUS-ALS — these mutations cause cytoplasmic aggregation. • Biomolecular condensate biology: in vitro phase separation and condensate analysis using FUS prion-like domain mutants. • DNA damage response: γH2AX foci kinetics and DNA repair efficiency given FUS's role in DDR. EDITGENE recommends this model for researchers investigating FUS biology, ALS/FTD disease mechanisms, RNA-binding protein function, and biomolecular condensate biology.
Yes. FUS rescue experiments are uniquely powerful for ALS/FTD research: • Construct design: use a codon-modified FUS sequence with a small C-terminal tag (FLAG, HA). FUS has N-terminal QGSY-rich prion-like domain (low-complexity), RGG1, RRM (RNA-binding), zinc finger, RGG2/3 (RNA-binding), and C-terminal NLS — preserve all elements. • ALS NLS mutation rescue: R521C, R521H, P525L NLS mutations introduce cytoplasmic FUS aggregation, modeling FUS-ALS gain-of-function — invaluable for disease mechanism studies. • RNA-binding-deficient rescue: RRM mutations abolish RNA binding without affecting prion-like domain function. • Prion-like domain mutant rescue: ALS-associated G156E and other prion-like domain mutations affect phase separation and condensate formation. • Functional readout: rescue should restore RNA processing functions; ALS mutation rescue should reproduce cytoplasmic aggregation phenotypes. HEK293 transduces efficiently with lentivirus and supports stable rescue line generation for systematic ALS mutation analysis.
* Research Use Disclaimer: Content is generated from publicly available research data, bioinformatic resources, and computational analyses for research reference only.

Related Publications

IF=3.9
Scientific reports
FUS is a multifunctional protein involved in many aspects of RNA metabolism, including transcription, splicing, translation, miRNA processing, and replication-dependent histone gene expression. In this work, we show that FUS depletion results in the differential expression of numerous small nucleolar RNAs (snoRNAs) that guide 2'-O methylation (2'-O-Me) and pseudouridylation of specific positions in ribosomal RNAs (rRNAs) and small nuclear RNAs (snRNAs). Using RiboMeth-seq and HydraPsiSeq for the profiling of 2'-O-Me and pseudouridylation status of rRNA species, we demonstrated considerable hypermodification at several sites in HEK293T and SH-SY5Y cells with FUS knockout (FUS KO) compared to wild-type cells. We observed a similar direction of changes in rRNA modification in differentiated SH-SY5Y cells with the FUS mutation (R495X) related to the severe disease phenotype of amyotrophic lateral sclerosis (ALS). Furthermore, the pattern of modification of some rRNA positions was correlated with the abundance of corresponding guide snoRNAs in FUS KO and FUS R495X cells. Our findings reveal a new role for FUS in modulating the modification pattern of rRNA molecules, that in turn might generate ribosome heterogeneity and constitute a fine-tuning mechanism for translation efficiency/fidelity. Therefore, we suggest that increased levels of 2'-O-Me and pseudouridylation at particular positions in rRNAs from cells with the ALS-linked FUS mutation may represent a possible new translation-related mechanism that underlies disease development and progression.
This KO model may be useful for: - Investigating the role of FUS in regulating site-specific 2'-O-methylation and pseudouridylation of ribosomal RNAs (rRNAs) and small nuclear RNAs (snRNAs) - Studying ribosome heterogeneity and its impact on translation efficiency and fidelity - Modeling the molecular mechanisms of amyotrophic lateral sclerosis (ALS) linked to the FUS R495X mutation - Profiling snoRNA-guided rRNA modification changes using RiboMeth-seq and HydraPsiSeq assays - Exploring the link between altered rRNA hypermodification and disease development in ALS

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