The CD34 Knockout DLD-1 Polyclonal Cells product is a heterogeneous population of DLD-1 human colorectal adenocarcinoma cells in which the CD34 gene has been disrupted via CRISPR/Cas9 genome editing. This polyclonal knockout pool serves as a loss-of-function model, enabling investigation of CD34-dependent adhesion and signaling mechanisms in a cancer-relevant context without residual target protein expression.
The parental DLD-1 cell line, derived from a colorectal adenocarcinoma, is a commonly used epithelial cancer model characterized by mutations in APC, KRAS, and TP53. It is extensively applied in studies of tumor cell adhesion, migration, invasion, and therapeutic susceptibility. CD34 is normally absent in DLD-1, making this knockout a controlled system to dissect reconstituted CD34 functions.
CD34 encodes a heavily glycosylated type I transmembrane protein that functions as an L-selectin (SELL) ligand, mediating leukocyte and hematopoietic progenitor adhesion to vascular endothelium. Its transcriptional regulation involves RUNX1, GATA2, NOTCH1, and TGF-?? pathways. Upon engagement, CD34 associates with intracellular partners such as CRKL and influences integrin-mediated adhesion through ITGB2. CD34 cooperates with PECAM1 and other cell adhesion molecules to coordinate cell?Ccell and cell?Cmatrix interactions. Loss of CD34 disrupts these adhesive processes, potentially impairing cell tethering, rolling, and transmigration in vascular and tumor microenvironments.
In the colorectal adenocarcinoma context, CD34 knockout provides a focused tool to examine adhesion-mediated tumor cell behavior. CD34?CL-selectin interactions contribute to tumor cell attachment to the endothelium and stromal components, facilitating metastatic dissemination. The knockout model allows direct assessment of how CD34 deficiency alters migration, invasion, and crosstalk with the microenvironment, advancing understanding of adhesion-dependent mechanisms in colorectal cancer progression.
This polyclonal knockout product is applicable in flow cytometry?Cbased validation of CD34 ablation, quantitative adhesion assays using endothelial or extracellular matrix substrates, and Transwell migration/invasion experiments. Western blotting and immunofluorescence can confirm downstream signaling changes, while co-culture with immune or stromal cells recapitulates niche interactions. It is well-suited for screening inhibitors of L-selectin?Cmediated adhesion. For further details or to request a quotation, please contact Ascent Research.
