AKT3 + AKT1 Antibody [L21G14] | Primary Antibodies

Application: Reactivity: Human

Lane 1: 293T (transfected with Empty vector), Lane 2: 293T (transfected with GFP tagged AKT1), Lane 3: 293T (transfected with GFP tagged AKT2), Lane 4: 293T (transfected with GFP tagged AKT3)

Usage Information

Dilution
WB1:10000 IHC1:250-1:1000 IF1:500

Application
WB, IHC, IF

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 Observed MW
54 kDa 82kDa, 56kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
AKT3 + AKT1 Antibody [L21G14] detects endogenous levels of total AKT3 and AKT1 protein.

Clone
L21G14

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; PKBG; AKT3; Protein kinase B gamma; RAC‑PK‑gamma; STK‑2; PKB gamma

Background
AKT1 and AKT3 are closely related serine/threonine kinases of the protein kinase B (PKB) family that function as central nodes in the PI3K–AKT–mTOR signaling axis, integrating growth factor, insulin, and nutrient inputs to regulate cell survival, proliferation, metabolism, and neuronal development. Both isoforms adopt a conserved modular architecture that positions regulatory hydrophobic and pleckstrin homology domains upstream of the kinase domain, enabling membrane recruitment and allosteric activation through phosphorylation at key regulatory sites such as threonine 308 and serine 473, which together stabilize the active kinase conformation and promote interaction with downstream substrates. Upon PI3K dependent phosphoinositide generation at the plasma membrane, AKT1 and AKT3 are recruited and phosphorylated by PDK1 and mTORC2, initiating site specific phosphorylation of effectors such as mTORC1, GSK 3β, FOXO transcription factors, and BAD, thereby enhancing protein synthesis, cell cycle progression, and survival signaling while attenuating glycogen synthesis and autophagy linked catabolism. In most tissues, AKT1 driven signaling supports growth factor–dependent proliferation, glucose utilization, and suppression of apoptosis, whereas in the brain AKT3 rich activity modulates neuronal migration, axon guidance, and synaptic plasticity, contributing to cortical lamination and higher order connectivity during development. Dysregulation of AKT1 or AKT3 activity, arising from upstream lesions in PI3K, PTEN, or receptor tyrosine kinases or from gain of function mutations in AKT genes, is associated with malignant transformation in carcinomas and hematologic neoplasms as well as with neurodevelopmental and neuropsychiatric disorders.

Background

AKT1 and AKT3 are closely related serine/threonine kinases of the protein kinase B (PKB) family that function as central nodes in the PI3K–AKT–mTOR signaling axis, integrating growth factor, insulin, and nutrient inputs to regulate cell survival, proliferation, metabolism, and neuronal development. Both isoforms adopt a conserved modular architecture that positions regulatory hydrophobic and pleckstrin homology domains upstream of the kinase domain, enabling membrane recruitment and allosteric activation through phosphorylation at key regulatory sites such as threonine 308 and serine 473, which together stabilize the active kinase conformation and promote interaction with downstream substrates. Upon PI3K dependent phosphoinositide generation at the plasma membrane, AKT1 and AKT3 are recruited and phosphorylated by PDK1 and mTORC2, initiating site specific phosphorylation of effectors such as mTORC1, GSK 3β, FOXO transcription factors, and BAD, thereby enhancing protein synthesis, cell cycle progression, and survival signaling while attenuating glycogen synthesis and autophagy linked catabolism. In most tissues, AKT1 driven signaling supports growth factor–dependent proliferation, glucose utilization, and suppression of apoptosis, whereas in the brain AKT3 rich activity modulates neuronal migration, axon guidance, and synaptic plasticity, contributing to cortical lamination and higher order connectivity during development. Dysregulation of AKT1 or AKT3 activity, arising from upstream lesions in PI3K, PTEN, or receptor tyrosine kinases or from gain of function mutations in AKT genes, is associated with malignant transformation in carcinomas and hematologic neoplasms as well as with neurodevelopmental and neuropsychiatric disorders.

References
https://pubmed.ncbi.nlm.nih.gov/28431241/ https://pubmed.ncbi.nlm.nih.gov/29173281/

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%