Phospho-Akt1 (Ser129) Antibody [K23C4]

Application: Reactivity: Human

Lane 1: MCF-7, Lane 2: MCF-7 (Alkaline Phosphatase treated)

Usage Information

Dilution
WB1:1000 - 1:10000

Application
WB

Reactivity
Human

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
55 kDa

Positive Control	MCF-7 cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
Phospho-Akt1 (Ser129) Antibody [K23C4] detects endogenous levels of total Akt1 protein only when it is phosphorylated at Ser129.

Clone
K23C4

Synonym(s)
PKB; RAC; AKT1; RAC-alpha serine/threonine-protein kinase; Protein kinase B; Protein kinase B alpha; Proto-oncogene c-Akt; RAC-PK-alpha; PKB alpha

Background
Phospho-Akt1 (Ser129) is a specific post-translational modification of Akt1 (RAC-alpha serine/threonine-protein kinase, PKBα), occurring within the flexible linker region between the pleckstrin homology (PH) domain and the kinase domain of this 480-amino-acid protein. Akt1 comprises an N-terminal PH domain for PIP3-mediated membrane recruitment, a catalytic kinase domain with key regulatory phosphorylation sites at Thr308 (activation loop) and Ser473 (hydrophobic motif), and a C-terminal regulatory tail. Phosphorylation of Ser129 by protein kinase CK2 generates a consensus S-x-x-D/E motif that primes subsequent modification at Ser126 and stabilizes the overall conformation of Akt1. This modification hyperactivates Akt1 beyond the effects of canonical PDK1/mTORC2 phosphorylation by strengthening its association with the HSP90 chaperone complex, which protects Thr308 from PP2A-mediated dephosphorylation, thereby sustaining Akt1 kinase activity. Additionally, phospho-Ser129 enhances β-catenin/TCF transcriptional activity, either directly or by stabilizing Wnt signaling components, and locks Akt1 in an extended active conformation that allows for isoform-specific substrate selection, such as preferential phosphorylation of palladin, a process not mirrored in Akt2 due to the absence of the equivalent Ser131 site. This modification drives cytoskeletal remodeling, cell survival through inhibition of Bad and FoxO, proliferation by promoting cyclin D1 stability and p27/p21 sequestration, and mTORC1 activation via TSC2 phosphorylation, with hierarchical phosphorylation ensuring robust signal amplification upon growth factor stimulation. In disease, elevated phospho-Ser129 levels enhance cancer cell survival and metastasis by amplifying PI3K/Akt oncogenic signaling (notably in breast and prostate cancers), contribute to chemoresistance via sustained HSP90 protection, and are implicated in metabolic disorders through disruption of glucose homeostasis by hyperactiving Akt1.

Background

Phospho-Akt1 (Ser129) is a specific post-translational modification of Akt1 (RAC-alpha serine/threonine-protein kinase, PKBα), occurring within the flexible linker region between the pleckstrin homology (PH) domain and the kinase domain of this 480-amino-acid protein. Akt1 comprises an N-terminal PH domain for PIP3-mediated membrane recruitment, a catalytic kinase domain with key regulatory phosphorylation sites at Thr308 (activation loop) and Ser473 (hydrophobic motif), and a C-terminal regulatory tail. Phosphorylation of Ser129 by protein kinase CK2 generates a consensus S-x-x-D/E motif that primes subsequent modification at Ser126 and stabilizes the overall conformation of Akt1. This modification hyperactivates Akt1 beyond the effects of canonical PDK1/mTORC2 phosphorylation by strengthening its association with the HSP90 chaperone complex, which protects Thr308 from PP2A-mediated dephosphorylation, thereby sustaining Akt1 kinase activity. Additionally, phospho-Ser129 enhances β-catenin/TCF transcriptional activity, either directly or by stabilizing Wnt signaling components, and locks Akt1 in an extended active conformation that allows for isoform-specific substrate selection, such as preferential phosphorylation of palladin, a process not mirrored in Akt2 due to the absence of the equivalent Ser131 site. This modification drives cytoskeletal remodeling, cell survival through inhibition of Bad and FoxO, proliferation by promoting cyclin D1 stability and p27/p21 sequestration, and mTORC1 activation via TSC2 phosphorylation, with hierarchical phosphorylation ensuring robust signal amplification upon growth factor stimulation. In disease, elevated phospho-Ser129 levels enhance cancer cell survival and metastasis by amplifying PI3K/Akt oncogenic signaling (notably in breast and prostate cancers), contribute to chemoresistance via sustained HSP90 protection, and are implicated in metabolic disorders through disruption of glucose homeostasis by hyperactiving Akt1.

References
https://pubmed.ncbi.nlm.nih.gov/24769357/ https://pubmed.ncbi.nlm.nih.gov/15818404/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%