The ALPP Knockout DLD-1 Polyclonal Cells comprise a CRISPR/Cas9-edited polyclonal knockout cell population targeting the ALPP gene in the human DLD-1 colorectal adenocarcinoma cell line. This polyclonal format provides a heterogeneous pool of gene-disrupted cells, ideal for studying loss-of-function effects without clonal selection artifacts, and is suitable for population-based functional assays.
Host DLD-1 cells originate from a colorectal adenocarcinoma resected from a 45-year-old male and carry well-characterized mutations in APC, KRAS, and TP53. These mutations drive key cancer hallmarks and make DLD-1 a widely used model for colorectal tumorigenesis, metastasis, and drug resistance studies.
ALPP encodes placental alkaline phosphatase, a GPI-anchored cell surface enzyme that hydrolyzes phosphate esters, modulating extracellular phosphate availability and purinergic signaling. Transcription of ALPP is regulated by upstream factors including SP1, GATA family transcription factors, AP-2, and hypoxia-inducible factors. The enzyme operates within lipid rafts, physically interacting with other GPI-anchored proteins and extracellular matrix components, and its activity influences cell adhesion molecules. Knockout of ALPP is predicted to disrupt phosphate homeostasis and the organization of cell surface signaling complexes, making this model valuable for dissecting GPI-anchored enzyme function in cancer cells.
In colorectal adenocarcinoma cells with APC, KRAS, and TP53 mutations, ALPP disruption may alter phosphate metabolism, folate biosynthesis, and nucleotide metabolism, pathways often dysregulated in cancer. Because ALPP has been linked to cancer stem cell traits and immune evasion, this knockout model provides a platform to investigate its role in tumor aggressiveness and response to therapies.
This polyclonal knockout population supports a range of experimental applications, including alkaline phosphatase activity assays, western blotting, RT-qPCR, cell proliferation and migration assays, and flow cytometry for surface protein profiling. It is suitable for drug sensitivity screens, tumor microenvironment studies, and biomarker validation. For further information or custom model requests, contact Ascent Research.
