ERLEC1 Knockout Raji Polyclonal Cells represent a CRISPR/Cas9-edited polyclonal cell population designed for targeted disruption of the ERLEC1 gene in a human B lymphocyte background. This loss-of-function model is generated through CRISPR/Cas9-mediated gene disruption, yielding a heterogeneous pool of Raji cells with diverse mutations at the ERLEC1 locus. The polyclonal format avoids clonal selection artifacts, providing a robust system for interrogating gene function in endoplasmic reticulum (ER) biology and protein quality control without the biases inherent in single-cell-derived clones.
The host Raji cell line is an EBV-positive human Burkitt’s lymphoma B cell line that retains key features of mature antibody-producing B lymphocytes. These cells exhibit a well-developed ER network and active secretory pathway, making them particularly suited for studying ER stress and protein homeostasis. The EBV transformation ensures continuous proliferation while preserving immune cell characteristics, allowing for reproducible experimentation in pathways central to B cell physiology and malignancy.
ERLEC1 encodes an ER-resident lectin that recognizes N-glycans on misfolded glycoproteins, tagging them for ER-associated degradation (ERAD). Mechanistically, ERLEC1 interacts with OS9, SEL1L, and HRD1 to form a complex that facilitates retrotranslocation of substrates into the cytosol, where VCP/p97 extracts them for delivery to the 26S proteasome. This process is tightly regulated by ER stress sensors??ATF6, IRE1, and PERK??linking ERLEC1 to the unfolded protein response (UPR). Downstream effectors include Derlin-1 and the proteasome, which execute degradation and maintain ER homeostasis.
In the Raji B cell context, ERLEC1 knockout provides a physiologically relevant tool to dissect ERAD mechanisms that are critical for antibody secretion and immune function. B lymphocytes face high biosynthetic demands, and disruption of protein quality control can trigger apoptosis or contribute to lymphomagenesis. This model enables investigation of how ERLEC1 loss influences ER stress responses, misfolded protein accumulation, and cell survival under proteotoxic conditions, offering insights into Burkitt’s lymphoma biology and potential therapeutic vulnerabilities.
This product supports a wide array of research applications, including ER stress studies, protein quality control analysis, cancer biology, and drug discovery for ERAD-related disorders. Compatible assays include Western blotting and RT-qPCR for expression profiling, flow cytometry for apoptosis detection, proteasome activity and ubiquitination assays to monitor degradation pathways, immunofluorescence for ER markers, and cell viability tests under chemically induced ER stress. For additional details, please contact Ascent Research.
