293T

Cat.No.: CSC-C3431

Species: Human

Source: Kidney

Morphology: epithelial

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Cat.No.
CSC-C3431
Description
The 293T cell line, originally referred as 293tsA1609neo, is a highly transfectable derivative of human embryonic kidney 293 cells, and contains the SV40 T-antigen
Species
Human
Source
Kidney
Recommended Medium
90% DMEM +10% h.i.FBS
Morphology
epithelial
STR DNA Profile
Amelogenin: X D19S433: 18 D5S818: 8,9 D21S11: 28,30.2 D18S51: 17,18 D6S1043: 11 D3S1358: 15,17 D13S317: 12,14 D7S820: 11 D16S539: 9,13 CSF1PO: 11,12 Penta D: 9,10 D2S441: 11,15 vWA: 16,19 D8S1179: 12,14 TPOX: 11 Penta E: 7,15 TH01: 7,9.3 D12S391: 19,21 D2S1338: 19 FGA: 23
Disease
Normal
Storage and Shipping
liquid nitrogen vapor phase
Citation Guidance
If you use this products in your scientific publication, it should be cited in the publication as: Creative Bioarray cat no. If your paper has been published, please click here to submit the PubMed ID of your paper to get a coupon.

The HEK293T cell line is a highly optimized derivative of the human embryonic kidney (HEK293) lineage, engineered through the stable integration of a temperature-sensitive variant of the Simian Virus 40 (SV40) Large T antigen. This genetic modification enables the episomal replication of transfected plasmids containing the SV40 origin of replication, significantly amplifying transient gene expression. Today, HEK293T stands as the industry standard for viral vector production and high-level recombinant protein expression.

  • Superior Viral Titers: HEK293T is the "gold standard" host for the packaging of lentiviral and retroviral vectors. Its high transfection efficiency and ability to support massive episomal replication ensure significantly higher viral titers compared to standard HEK293 or other mammalian lines, accelerating timelines for gene therapy and CAR-T research.
  • Exceptional Transfection Efficiency: These cells are remarkably amenable to a wide array of transfection methodologies, including calcium phosphate, lipofection, and electroporation. This robustness minimizes optimization efforts and ensures high-yield protein or viral production even with complex, multi-plasmid systems.
  • Scalable Growth & Rapid Doubling Time: Characterized by vigorous growth kinetics and adaptation to both adherent and suspension culture formats, HEK293T cells are easily scalable. This makes them ideal for transitioning from bench-top discovery to industrial-scale bioproduction.
  • Validated Performance in High-Throughput Screening (HTS): Due to their consistent response and ease of handling, HEK293T cells are a preferred platform for functional genomics, GPCR signaling assays, and drug-target validation studies.

Our HEK293T cells undergo stringent quality control, including authentication via STR profiling and rigorous screening for mycoplasma and adventitious agents. By providing a reliable, high-performance cellular factory, this product serves as an indispensable asset for biopharmaceutical companies and research institutions focused on viral vector engineering, vaccine development, and systemic protein production.

Optimization of Protein UFMylation Modification Method and Its Application in Substrate Identification in Human Embryonic Kidney 293T (HEK293T) Cells

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.

To address these limitations, we developed a systematic strategy to improve UFMylation detection and enable large-scale identification of substrates. In this study, we generated UFSP2 single-KO (UFSP2KO) and UFSP1/UFSP2 double-KO (UFSP1KO/UFSP2KO, DKO) human embryonic kidney 293T (HEK293T) cell lines, capitalizing on the role of UFSPs in UFM1 recycling to increase substrate modification levels. We subsequently optimized the transfection system through single-factor experiments, which revealed that exogenous expression of the E3 ligase components, UFL1 and DDRGK1, rather than the E1 enzyme UBA5 or the E2 enzyme UFC1, is critical for maximizing UFMylation efficiency. Most importantly, by integrating this optimized cellular system with a newly developed antibody specifically recognizing the UFM1 remnant motif (K-ε-Gly-Val [GV]), we achieved robust enrichment of UFMylated peptides and identified more than 600 UFMylation substrates using LC-MS/MS. Furthermore, we validated novel substrates, analyzed amino acid preferences surrounding UFMylation sites, and performed subcellular localization and functional annotation of the identified proteins.

Identification and validation of UFMylation substrates in HEK293T cells.

Fig. 1. Identification and validation of UFMylation substrates in UFSP1KO/UFSP2KO HEK293T cells (Fang, Yaoyao, et al., 2026).

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