The HCK Knockout HAP1 Polyclonal Cells are a CRISPR/Cas9-edited polyclonal cell population targeting the human HCK gene in the HAP1 near-haploid cell line. This product provides a heterogeneous population of knockout cells for loss-of-function studies of HCK, a Src family tyrosine kinase. The polyclonal format is suited for population-level functional assays, avoiding clonal selection bias while enabling robust characterization of HCK-dependent signaling.
HAP1 cells are derived from the chronic myeloid leukemia (CML) line KBM-7 and are BCR-ABL1-positive and male. Their near-haploid karyotype makes them a valuable tool for functional genomics, as gene disruption frequently yields complete loss of function from a single allele. Although not fully mature myeloid cells, HAP1 cells retain expression of key signaling components relevant to myeloid biology and leukemia, providing a suitable background for studying HCK in a CML-related context.
HCK encodes a Src family kinase predominantly expressed in myeloid cells, where it regulates innate immune processes such as phagocytosis, adhesion, and migration. HCK is activated downstream of receptors including Fc gamma receptors, integrins, GM-CSF receptor, and cytokine receptors, and is inhibited by Csk. Upon activation, HCK phosphorylates ITAM motifs on Fc receptor gamma chains, recruiting Syk and initiating a cascade involving Vav, Rac1, and paxillin that drives actin reorganization and respiratory burst. HCK also signals through the PI3K/Akt and MAPK pathways and influences NF-kappaB. Among its interacting partners are BCR-ABL, CrkL, CD14, and the IL-6 receptor beta chain, situating HCK at the intersection of immune signaling and leukemogenesis.
In the HAP1 background, HCK disruption offers a simplified model to study Src kinase functions in myeloid-like cells. The presence of BCR-ABL and expression of Fc receptor pathway components allow investigation of HCK??s role downstream of oncogenic signaling and in phagocytic regulation. This knockout population is particularly useful for dissecting HCK interactions with BCR-ABL and CrkL, and for examining integrin-dependent adhesion and migration in a leukemia-derived line. The near-haploid nature further enhances the clarity of phenotypic readouts.
This HCK knockout population enables detailed investigation of Fc receptor-mediated phagocytosis using IgG-coated beads, migration assays toward chemokine gradients, and adhesion assays on integrin substrates. It is suitable for drug screening of Src kinase inhibitors and for mechanistic studies using phospho-specific western blotting (e.g., phospho-HCK, phospho-Syk, phospho-Vav), flow cytometry for Fc receptors, and co-immunoprecipitation of HCK with its binding partners. Cytokine production assays can assess functional consequences. For additional product information or technical support, please contact Ascent Research.
