BMPR1B Knockout HeLa Polyclonal Cells are a CRISPR/Cas9-edited polyclonal population of HeLa cells with targeted disruption of the BMPR1B gene. This polyclonal knockout model provides a heterogeneous loss-of-function system for investigating bone morphogenetic protein (BMP) signaling. The product is supplied as a mixed pool of edited cells, reflecting diverse genetic modifications within the BMPR1B locus, suitable for bulk assays and pathway analysis.
The HeLa cell line, derived from the cervical adenocarcinoma of Henrietta Lacks, is a widely utilized epithelial model in cancer biology, virology, and cell signaling studies. These cells exhibit robust growth characteristics and have been extensively characterized for gene expression and functional assays. Their human origin and epithelial nature make them an appropriate background for studying BMPR1B function in cellular processes such as proliferation, migration, and apoptosis.
BMPR1B encodes a type I serine/threonine kinase receptor for BMPs, transducing signals upon ligand binding. Ligands such as BMP2, BMP4, BMP7, and GDF5 bind BMPR1B, which then heterodimerizes with type II receptors (BMPR2, ACVR2A/B) leading to kinase activation. This results in phosphorylation of SMAD1/5/8, which complex with SMAD4 and translocate to the nucleus to regulate targets like ID1, ID2, ID3, RUNX2, and Osterix. Non-SMAD pathways, including p38 MAPK and ERK1/2, are also activated downstream of BMPR1B. Regulatory interactions with Endoglin and FKBP12 fine-tune receptor signaling.
In HeLa cells, BMPR1B mediates typical BMP responses affecting growth and survival. Knockout of BMPR1B in this polyclonal population disrupts SMAD1/5/8 phosphorylation and target gene transcription, impairing ligand-dependent signaling. Given HeLa??s cancer origin, the model allows dissection of BMPR1B??s role in tumor-relevant processes like proliferation, apoptosis, and migration.
This polyclonal knockout pool is suited for functional studies using Western blot for phospho-SMAD1/5/8, RT-qPCR for ID1/2, and immunofluorescence for SMAD localization. Assays for cell proliferation, migration, invasion, apoptosis, and BMP-responsive luciferase reporters are compatible. The model supports research in bone biology, cancer progression, and target validation. For further information, please contact Ascent Research.
