The B4GALT7 Knockout Jurkat Polyclonal Cells represent a CRISPR/Cas9-mediated polyclonal knockout cell population designed for loss-of-function studies of the B4GALT7 gene in a human T-cell leukemia background. This product consists of a heterogeneous pool of Jurkat cells that have undergone targeted gene disruption, eliminating functional B4GALT7 expression. The polyclonal format provides a robust model system that preserves the genetic diversity of the edited population, enabling researchers to investigate gene function in a context that mimics the natural variability of cellular responses.
Jurkat cells are an immortalized human T lymphocyte line originally derived from the peripheral blood of a 14-year-old male with acute lymphoblastic leukemia. These suspension-growing lymphoblastoid cells serve as a cornerstone model in T-cell biology, being extensively utilized for the study of T-cell receptor signaling, apoptosis, and leukemogenesis. Their well-characterized signaling networks and ease of genetic manipulation make Jurkat cells an ideal host for CRISPR-based gene editing, allowing for detailed dissection of molecular pathways governing lymphocyte function.
B4GALT7 encodes beta-1,4-galactosyltransferase 7, a critical enzyme in proteoglycan biosynthesis that catalyzes the transfer of galactose to xylose residues within the tetrasaccharide linker region of glycosaminoglycan chains. This step is essential for the subsequent elongation of chondroitin sulfate, heparan sulfate, and dermatan sulfate chains. The enzymatic activity of B4GALT7 is transcriptionally regulated by SP1 and TGFB1 signaling, and it functions in concert with xylosyltransferases XYLT1 and XYLT2, as well as beta-1,3-glucuronyltransferase 3 (B3GAT3). Downstream, B4GALT7 activity enables the proper modification of core proteins such as syndecans and glypicans, which are pivotal for cell-surface presentation of proteoglycans involved in extracellular matrix interactions and growth factor sequestration.
Disruption of B4GALT7 in Jurkat cells abrogates the galactosylation of xylose, thereby blocking glycosaminoglycan chain elongation and leading to a deficiency in mature cell-surface proteoglycans. This loss impairs the ability of Jurkat T cells to interact with extracellular matrix components and respond normally to environmental cues, potentially altering adhesion, migration, and signaling cascades. The model is particularly relevant for studying the molecular pathology of Ehlers-Danlos syndrome spondylodysplastic type 2 and related skeletal dysplasias, where mutations in B4GALT7 lead to defective proteoglycan synthesis and connective tissue abnormalities.
Researchers can employ this B4GALT7 knockout polyclonal population to investigate proteoglycan-dependent mechanisms in T-cell activation, adhesion, and migration. Representative applications include flow cytometric analysis of cell surface heparan sulfate and chondroitin sulfate levels, RT-qPCR profiling of proteoglycan core protein expression, metabolic labeling with [3H]-galactose to trace GAG synthesis, and HPLC-based disaccharide composition analysis. Functional adhesion assays to extracellular matrix proteins and migration assays further elucidate the role of B4GALT7 in lymphocyte trafficking and interaction with the tumor microenvironment. For additional details and technical support, please contact Ascent Research.
