In Stock Cell Lines
Homo sapiens (Human)
Kidney
Adherent
The STUB1 Knockout HEK293T Cell Line is a CRISPR/Cas9-edited knockout cell line in which the STUB1 gene has been disrupted in HEK293T cells. STUB1 encodes an E3 ubiquitin ligase and co-chaperone that targets misfolded proteins for proteasomal degradation by interacting with Hsp70/Hsc70 and BAG-family proteins, with downstream substrates including tau and p53. This knockout model is ideal for investigating protein quality control, ubiquitination, and degradation pathways in a highly transfectable human embryonic kidney host. Applications include ubiquitination assays, Western blot analysis of protein turnover, co-immunoprecipitation of chaperone complexes, and high-throughput screening for modulators of STUB1 activity.
MS4A7 Knockout TE1 Polyclonal Cells
Cat. No. ARG12157
PDHA1 Knockout 143B Polyclonal Cells
Cat. No. ARG11862
IL12RB1 Knockout HAP1 Polyclonal Cells
Cat. No. ARG22745
BTN3A2 Knockout A2780 Polyclonal Cells
Cat. No. ARG28929
ANKRD28 Knockout HT29 Polyclonal Cells
Cat. No. ARG32948
IDH1 Knockout HT29 Polyclonal Cells
Cat. No. ARG33407
The STUB1 Knockout HEK293T Cell Line is a CRISPR/Cas9-edited knockout cell line featuring targeted disruption of the STUB1 gene in the HEK293T human embryonic kidney host cell line. This product offers a stable loss-of-function model to investigate STUB1-dependent ubiquitylation and protein quality control mechanisms.
The HEK293T host is an adenovirus 5-transformed epithelial cell line that constitutively expresses the SV40 large T antigen, conferring high transfectability and episomal plasmid replication. Widely used for recombinant protein production and viral packaging, HEK293T provides a robust and scalable platform for gene-edited cell lines.
STUB1 encodes a co-chaperone and E3 ubiquitin ligase that bridges chaperone machinery and the ubiquitin-proteasome system. It directly binds Hsp70/Hsc70 (HSPA8, HSPA1A) and Hsp90 to recognize misfolded clients, and with E2 enzymes UBE2D1/2 and UBE2N, catalyzes substrate ubiquitination for proteasomal degradation. Activity is regulated by BAG-family co-chaperones (BAG1, BAG2, BAG3) and induced by HSF1-mediated transcription under heat shock, oxidative stress, or unfolded protein response. Targets include tau, p53, ErbB2, and CFTR-??F508, linking STUB1 to neurodegeneration, cancer, cardiac diseases, and aging-related proteotoxicity.
In HEK293T cells, STUB1 knockout disrupts the proteostasis network, leading to altered degradation of client proteins. The model is particularly suited to examine chaperone-assisted quality control and to study how loss of E3 ligase function affects protein accumulation and aggregation-prone substrates, without complications of tissue-specific factors.
This cell line enables ubiquitination assays, Western blot-based degradation monitoring, co-immunoprecipitation of Hsp70/Hsp90 complexes, and proteasome inhibition (MG132) experiments to assess proteasome-dependent turnover. Cycloheximide chase analysis can measure protein half-lives, and CETSA provides target engagement profiling. The knockout line supports investigation of how STUB1-mediated ubiquitylation intersects with other degradation pathways. Applications include mechanistic studies of protein quality control, drug target validation in cancer and neurodegeneration, and high-throughput screening for STUB1 activity modulators. For further details, please contact Ascent Research.
