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DDRGK1 Knockout HEK293 Cell Line
Cat.No.:
EDJ-KQ13111
Species:
Human
Cell Name:
HEK293
Gene:
DDRGK1
Gene ID:
65992
Size:
1×10⁶cells
DDRGK1 Knockout Cell Line (HEK293) 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-KQ13111 |
|---|---|
| Product Name | DDRGK1 Knockout Cell Line (HEK293) |
| 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 | |
| NCBI Gene ID | |
| Gene Synonyms | C20orf116|SEMDSH|UFBP1|dJ1187M17.3 |
| Summary |
The protein encoded by this gene interacts with components of the ubiquitin fold modifier 1 conjugation pathway and helps prevent apoptosis in ER-stressed secretory tissues. In addition, the encoded protein regulates nuclear factor-κB activity. [provided by RefSeq, Dec 2015]
|
| Associated Diseases | Non-tumor |
| Morphology | Adherent |
| Passage Ratio | 1/5，2days |
| Complete Culture Medium | DMEM + 10% FBS |
| Freezing Medium | 95% Complete culture medium+ 5% 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.
| Loci | STR Info (Sample Cell) Sample Cell Line: HEK293 | STR Info (Cell bank) Cell Line: HEK293 | ||
| Allele1 | Allele2 | Allele1 | Allele2 | |
| 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.
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.
Research Publications
Optimization of protein UFMylation modification method and its application in substrate identification in human cells.
IF=3.9
The Journal of biological chemistry
UFMylation plays an essential role in regulating intracellular physiological and pathological processes. Accumulating evidence has demonstrated that dysregulation of UFMylation is closely associated with the progression of various diseases, including cancers and developmental disorders. However, efficient and specific methods for detecting UFMylated substrate proteins remain challenging. In this study, we generated the UFM1-specific protease 1/2 knockout (UFSP1/UFSP2) human embryonic kidney 293T cell line and validated it as the most suitable cellular model for the screening, identification, and confirmation of UFMylated substrate proteins. Furthermore, exogenous expression of the E3 ligase components, UFM1-specific ligase 1 (UFL1) and DDRGK domain-containing protein 1 (DDRGK1), significantly enhanced protein UFMylation levels, enabling the large-scale enrichment of UFMylated substrates. Collectively, we have established a more efficient, specific, and reliable method for UFMylation substrate research, facilitating in-depth investigation into its biological functions and regulatory mechanisms.
This KO model may be useful for:
- Studying the role of DDRGK1 in UFMylation pathway regulation
- Identifying and validating UFMylation substrates in human cells
- Investigating UFMylation-dependent protein modification mechanisms
- Functional characterization of DDRGK1 in cellular stress responses
- Supporting drug screening efforts targeting the UFMylation system
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