Anti-phospho-CDK2/CDK1 (Thr160/Thr161), clone 31C95

Rabbit IgG in phosphate buffered saline, pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol, 0.4-0.5mg/ml BSA. Phospho-CDK2/CDK1 (Thr160/Thr161) antibody detects cyclin dependent kinase 2 and cyclin dependent kinase 1 when phosphorylated at their critical threonine residues required for activation. CDK2, encoded by the CDK2 gene, and CDK1, encoded by the CDK1 gene, are central regulators of the eukaryotic cell cycle. Both kinases belong to the cyclin dependent kinase family and function by binding specific cyclins that direct their activity at distinct phases of the cycle. Phosphorylation of CDK2 at threonine 160 and CDK1 at threonine 161 is essential for full catalytic activity and progression through S phase and mitosis.Phospho-CDK2/CDK1 (Thr160/Thr161) antibody is widely applied in cancer biology, cell cycle research, and molecular pharmacology. Detection of phosphorylation at these residues provides a direct measure of CDK activation status. In proliferating cells, CDK2 in complex with cyclin E or cyclin A promotes DNA replication, while CDK1 in complex with cyclin B drives mitotic entry. By monitoring phosphorylation at Thr160 and Thr161, researchers can assess how CDK activation is controlled during the cell cycle and disrupted in disease. In western blot assays, Phospho-CDK2/CDK1 (Thr160/Thr161) antibody detects phosphorylated isoforms distinct from inactive CDK2 and CDK1. Immunohistochemistry highlights nuclear staining in actively cycling cells within tissues, while immunofluorescence reveals subcellular localization of active kinase complexes at replication foci and mitotic structures. These methods provide powerful tools for visualizing CDK activity in situ.CDK2 and CDK1 phosphorylation is regulated by cyclin binding and CDK activating kinase (CAK). In addition to activating phosphorylation, inhibitory phosphorylation at other residues fine tunes kinase activity, ensuring proper timing of cell cycle transitions. Aberrant phosphorylation results in unscheduled proliferation, genomic instability, and oncogenesis. By applying Phospho-CDK2/CDK1 (Thr160/Thr161) antibody, scientists can study how signaling pathways converge on CDK regulation and explore therapeutic strategies that target cell cycle kinases.In oncology, dysregulated CDK2 and CDK1 activity is a hallmark of many tumors. Overexpression of cyclins, loss of CDK inhibitors such as p21 or p27, and altered phosphorylation lead to unchecked proliferation. Small molecule inhibitors of CDKs are under clinical development, and monitoring phosphorylation status provides a biomarker for therapeutic efficacy. This antibody therefore supports translational research linking kinase signaling to cancer therapy.Beyond cancer, CDK2 and CDK1 phosphorylation contributes to developmental biology, stem cell regulation, and tissue regeneration. Phosphorylation at Thr160 and Thr161 ensures fidelity of DNA replication, chromosome segregation, and genome stability. Dysregulation is implicated in infertility, developmental syndromes, and age related decline. The phospho-specific antibody provides a means to evaluate CDK function across diverse biological systems.Phosphorylation dynamics also link CDKs to DNA damage response and stress signaling. Upon genotoxic stress, inhibitory pathways suppress CDK activity to allow repair before replication or division. Conversely, inappropriate activation leads to replication stress and apoptosis. By using Phospho-CDK2/CDK1 (Thr160/Thr161) antibody, researchers can examine how stress signals intersect with cell cycle progression and contribute to disease mechanisms.Phospho-CDK2/CDK1 (Thr160/Thr161) antibody from NSJ Bioreagents delivers dependable specificity for studying these key regulatory phosphorylation events. Its performance across multiple applications supports both mechanistic studies of kinase regulation and translational work in oncology and regenerative medicine. By enabling detection of CDK phosphorylation, the antibody provides insight into the molecular switches that drive cell division and maintain genomic stability.