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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
Checkpoint kinase 1 (CHEK1), also known as CHK1, is a critical regulator of the DNA damage response that coordinates cell cycle checkpoints and maintains genomic stability. Phospho-CHK1 (pSer280) Antibody, clone 31C46, is designed to detect CHK1 phosphorylated at serine 280, a regulatory site associated with modulation of CHK1 activity and signaling cross-talk with other cellular pathways. Unlike autophosphorylation sites that directly reflect kinase activation, Ser280 phosphorylation is linked to regulation of CHK1 function and integration of upstream signaling inputs.
Phosphorylation of CHK1 at Ser280 has been associated with signaling pathways beyond the canonical ATR-CHK1 axis, including potential regulation by kinases such as AKT. This modification is thought to influence CHK1 localization, stability, and interaction with other regulatory proteins. As a result, detection of Ser280 phosphorylation provides insight into how CHK1 activity is modulated in response to broader cellular signaling environments.
Unlike phosphorylation at Ser296, which reflects direct activation of CHK1 kinase activity during DNA damage response, Ser280 phosphorylation represents a regulatory modification that may fine-tune CHK1 function. This distinction makes Ser280 a useful marker for studying pathway cross-talk and regulatory mechanisms that influence checkpoint signaling rather than serving as a direct indicator of checkpoint activation.
Phosphorylation at Ser280 may occur under conditions of cellular stress, growth factor signaling, or metabolic regulation, reflecting integration of multiple signaling pathways. Detection of this site can therefore provide additional context for understanding how CHK1 activity is coordinated with other signaling networks within the cell.
Subcellularly, phosphorylated CHK1 is observed in both nuclear and cytoplasmic compartments depending on cellular conditions and regulatory state. Changes in localization may reflect shifts in CHK1 function or interaction with different signaling complexes. Immunodetection typically reveals variable staining patterns consistent with its role in dynamic regulation.
Dysregulation of CHK1 regulatory phosphorylation contributes to altered checkpoint control and may influence sensitivity to DNA damage or therapeutic agents. Understanding phosphorylation at sites such as Ser280 provides insight into how checkpoint signaling is modulated in cancer and other disease contexts.
Phospho-CHK1 (pSer280) Antibody, clone 31C46, enables detection of this regulatory phosphorylation event, supporting studies of CHK1 modulation, signaling cross-talk, and pathway integration. For analysis of DNA damage checkpoint activation, see our Phospho-CHK1 (Ser296) Antibody page.
Optimal dilution of the Phospho-CHK1 (pSer280) Antibody / CHK1 Regulation and Signaling Cross-Talk Marker should be determined by the researcher.
A synthesized peptide derived from human Phospho-Chk1 (S280) was used as the immunogen for the Phospho-CHK1 (pSer280) Antibody.
Store the Phospho-CHK1 (pSer280) Antibody at -20oC.
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