- Tel: 858.663.9055
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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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AKT, also known as Protein kinase B (AKT), is a central serine-threonine kinase that regulates cell survival, metabolism, proliferation, and growth through the PI3K-AKT signaling pathway. Activation of AKT normally requires phosphoinositide 3-kinase-mediated generation of phosphatidylinositol 3,4,5-trisphosphate (PIP3), which recruits AKT to the plasma membrane via its pleckstrin homology (PH) domain. This membrane recruitment enables phosphorylation at key regulatory residues, leading to full kinase activation and downstream signaling. AKT proteins are broadly expressed across tissues and are essential for maintaining cellular homeostasis.
AKT antibody, also referred to as Protein kinase B antibody and PKB antibody in the literature, can be used to study both total and mutant forms of the protein involved in signaling regulation. The E17K mutation is a well-characterized substitution within the PH domain of AKT that alters lipid binding specificity and enhances membrane association. This mutation enables AKT to localize to the plasma membrane independently of normal PI3K signaling, resulting in constitutive kinase activation. As a result, the E17K variant represents a gain-of-function mutation that disrupts normal regulatory control of AKT signaling.
This AKT E17K Mutant Antibody / Oncogenic Activation and Membrane Localization Marker Antibody (clone RM336) is uniquely positioned for research focused on mutation-driven signaling and cancer biology. The AKT E17K mutation has been identified in multiple tumor types, including breast, colorectal, and endometrial cancers, where it contributes to persistent activation of survival and growth pathways. Constitutive activation of AKT through this mutation promotes resistance to apoptosis, enhances proliferative signaling, and supports tumor progression. Detection of the E17K mutant form of AKT therefore provides important insight into oncogenic signaling mechanisms and mutation-specific pathway dysregulation.
In cellular and tissue-based studies, the E17K mutant form of AKT is often associated with increased membrane localization and altered subcellular distribution compared to wild-type protein. This shift reflects the mutationâs impact on PH domain-mediated lipid interactions and highlights the importance of spatial regulation in AKT signaling. In tumor tissues, detection of AKT E17K can reveal aberrant activation patterns and support studies of targeted therapeutic strategies aimed at inhibiting PI3K-AKT pathway components.
Clone RM336 is a recombinant rabbit monoclonal antibody designed to recognize the AKT E17K mutant protein, enabling selective detection of this oncogenic variant in research applications. An AKT E17K antibody is suitable for detecting mutant AKT expression in studies of cancer signaling, pathway activation, and mutation-specific cellular responses.
For a microarray-validated AKT1 antibody supporting high-specificity detection, see our AKT1 antibody (clone AKT1/2552).
The stated application concentrations are suggested starting points. Titration of the AKT E17K Mutant Antibody / Oncogenic Activation and Membrane Localization Marker Antibody may be required due to differences in protocols and secondary/substrate sensitivity.
A peptide corresponding to the Akt E17K Mutant was used as the immunogen for the recombinant AKT E17K Mutant antibody.
Store the AKT E17K Mutant antibody at -20oC.
AKT E17K antibody, AKT1 E17K mutant antibody, Protein kinase B E17K antibody, PKB E17K antibody, AKT oncogenic mutant antibody
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