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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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Protein kinase B alpha (AKT1) is a serine-threonine kinase that functions as a central regulator of the PI3K-AKT signaling pathway, controlling cellular processes including metabolism, proliferation, survival, and growth. AKT1 activation is a multi-step process that involves membrane recruitment via its pleckstrin homology domain followed by phosphorylation at key regulatory residues. Among these sites, threonine 450 (T450) is located within the turn motif and plays an important role in stabilizing the kinase and supporting proper folding and maturation. This phosphorylation event contributes to the structural integrity and sustained signaling capacity of AKT1.
Phospho-AKT1 (pT450) antibody, also referred to as AKT1 pT450 antibody and phosphorylated AKT1 antibody in the literature, recognizes AKT1 specifically when phosphorylated at threonine 450. Detection of this modification provides insight into AKT1 activation status and kinase regulation, particularly in response to upstream PI3K signaling. Unlike phosphorylation at other regulatory residues that directly control catalytic activity, T450 phosphorylation is associated with protein stability and proper conformational maintenance, making it an important indicator of functional AKT1 protein within cells.
This Phospho-AKT1 (pT450) Antibody / Activation and PI3K-AKT Signaling Marker Antibody (clone HEA-1) is uniquely positioned for studies of signaling dynamics and pathway regulation. AKT1 phosphorylation is frequently altered in cancer and other disease states, where dysregulation of PI3K-AKT signaling leads to enhanced cell survival, resistance to apoptosis, and increased proliferation. Monitoring phosphorylation at T450 provides valuable information about the presence of properly folded and signaling-competent AKT1, complementing analysis of other phosphorylation sites involved in acute activation.
In western blot analysis, phosphorylated AKT1 may exhibit an apparent molecular weight higher than the predicted size due to phosphorylation-dependent changes in electrophoretic mobility. This shift is commonly observed in activated or treatment-responsive samples, where increased phosphorylation correlates with altered migration patterns. Treatment-dependent variation in phospho-AKT1 signal intensity can reflect modulation of upstream signaling pathways and cellular response to pharmacological agents.
Clone HEA-1 is a recombinant rabbit monoclonal antibody designed to detect AKT1 phosphorylated at threonine 450 with specificity for the modified form of the protein. A phospho-AKT1 antibody is suitable for detecting phosphorylation-dependent changes in AKT1 signaling in studies of PI3K-AKT pathway activation, cancer biology, and cellular signaling regulation.
For a microarray-validated AKT1 antibody supporting high-specificity detection, see our AKT1 antibody (clone AKT1/2552).
Optimal dilution of the Phospho-AKT1 (pT450) Antibody / Activation and PI3K-AKT Signaling Marker Antibody should be determined by the researcher.
A synthetic peptide specific to the region of human AKT1 protein surrounding phosphorylated threonine 450 was used as the immunogen for the Phospho-AKT1 (pT450) Antibody.
Store the Phospho-AKT1 (pT450) Antibody at -20oC.
Phospho AKT1 T450 antibody, AKT1 pT450 antibody, Phosphorylated AKT1 antibody, Protein kinase B alpha phospho T450 antibody, AKT1 activation marker antibody
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