The KLHL36 Knockout Jurkat Polyclonal Cells are a heterogeneous population of human T lymphocyte cells derived from the Jurkat line that have been genetically modified using CRISPR/Cas9 to disrupt the KLHL36 locus, generating a loss-of-function model for functional studies. Unlike clonal cell lines, this polyclonal population contains a diverse array of editing events across individual cells, enabling robust and reproducible investigation of KLHL36-dependent biology without single-clone bias.
Jurkat cells are an immortalized T cell line originally isolated from the peripheral blood of a 14-year-old male with acute T cell leukemia (ATCC TIB-152). They retain many characteristics of malignant T lymphoblasts and are widely used as a model system to explore T cell receptor signaling, cytokine responses, and the molecular mechanisms driving T-cell acute lymphoblastic leukemia (T-ALL). The Jurkat background provides a relevant cellular context for studying how ubiquitin-mediated proteolysis influences leukemic cell growth and survival.
The KLHL36 gene encodes a substrate?specific adaptor for the Cullin3?RING E3 ubiquitin ligase complex (CRL3), where it directly interacts with the scaffold protein CUL3 and the RING finger protein RBX1 to recruit specific, yet largely unidentified, protein substrates for polyubiquitination. This tagging process directs the substrates to the 26S proteasome for degradation. Upstream, KLHL36 activity is thought to be modulated by cellular stress signals, allowing the CRL3 complex to respond to changing intracellular conditions. Disruption of KLHL36 therefore impairs the timely degradation of its target proteins, which may include factors that regulate cell cycle progression or apoptosis, leading to their stabilization and potential functional consequences in T lymphocytes.
In the context of Jurkat T-ALL cells, KLHL36 knockout serves as a valuable tool to dissect the role of CRL3-type E3 ligases in leukemic transformation and T cell biology. The accumulation of KLHL36 substrates due to adaptor loss could reveal novel oncogenic or tumor?suppressive nodes that depend on ubiquitin?dependent proteolysis. Because Jurkat cells already harbor aberrant signaling networks, the elimination of KLHL36 may uncover points of vulnerability, such as altered sensitivity to apoptotic stimuli or changes in proliferative capacity, making the model highly relevant for cancer research.
Researchers can employ these polyclonal knockout cells in a broad range of experiments, including co-immunoprecipitation and ubiquitination assays to identify and validate KLHL36 substrates, proteasome activity measurements to assess global degradation capacity, and Western blotting or RT-qPCR to monitor downstream pathway engagement. Functional readouts such as flow cytometry for apoptosis, cell viability assays, and NF-??B luciferase reporter assays enable phenotypic characterization, supporting studies of ubiquitin?proteasome system function in T?cell leukemia and high?throughput screening for CRL3 modulators. For further technical details, please contact Ascent Research.
