Akt1 Antibody [B17F18] | Primary Antibodies

Application: Reactivity: Human, Mouse, Rat, Monkey

Usage Information

Dilution
WB1:1000 IHC1:150 - 1:600

Application
WB, IHC

Reactivity
Human, Mouse, Rat, Monkey

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
55 kDa 60 kDa
^*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
Akt1 Antibody [B17F18] detects endogenous levels of total Akt1 protein.

Clone
B17F18

Synonym(s)
AKT; AKT serine/threonine kinase 1; AKT1; AKT1 kinase; AKT1m; MGC99656; PKB; PKB alpha; PKB-ALPHA; PRKBA; Protein kinase B; Protein kinase B alpha; RAC-PK-alpha

Background
Akt1 (also termed protein kinase B alpha) is a serine/threonine kinase of the AGC family that functions as a central signaling hub downstream of phosphoinositide 3-kinase, integrating growth factor, cytokine, and nutrient inputs into coordinated control of cell survival, proliferation, metabolism, and growth. The protein contains an N‑terminal pleckstrin homology domain that binds phosphatidylinositol 3,4,5‑trisphosphate at the plasma membrane, a central catalytic kinase domain with the conserved activation loop threonine, and a C‑terminal regulatory tail harboring a hydrophobic motif serine and other residues that tune activity and interactions with upstream kinases and phosphatases. Activation begins when receptor tyrosine kinases, G protein–coupled receptors, or other receptors stimulate class I PI3K to generate phosphatidylinositol 3,4,5‑trisphosphate, which recruits Akt1 and its upstream kinase PDK1 to the membrane via their pleckstrin homology domains; PDK1 phosphorylates the activation loop threonine and mTOR complex 2 phosphorylates the C‑terminal hydrophobic motif serine, together producing full Akt1 catalytic activity. Protein phosphatases such as PP2A and PHLPP reverse these phosphorylations, while PTEN and related lipid phosphatases suppress Akt1 indirectly by dephosphorylating phosphatidylinositol 3,4,5‑trisphosphate, establishing a balance between kinase and phosphatase activities that defines Akt1 signaling amplitude and duration. Once active, Akt1 phosphorylates substrates containing an RxRxxS/T motif across multiple compartments, including the pro-apoptotic Bcl‑2 family member Bad, FoxO transcription factors, and components of the intrinsic caspase machinery, which shifts signaling toward survival and resistance to apoptotic triggers. Akt1 also modulates metabolism and nutrient handling through targets such as AS160 and glycolytic regulators, couples insulin and growth factor signaling to glucose transport and glycogen synthesis via inhibition of GSK‑3 isoforms, and regulates cell-cycle progression by phosphorylating p21 and p27 to influence their stability and localization. Direct phosphorylation of TSC2 and other elements of the TSC1–TSC2–mTOR axis links Akt1 to mTOR complex 1 activation, eIF4F assembly, and protein synthesis, placing this kinase at the core of growth and anabolic signaling networks.

Background

Akt1 (also termed protein kinase B alpha) is a serine/threonine kinase of the AGC family that functions as a central signaling hub downstream of phosphoinositide 3-kinase, integrating growth factor, cytokine, and nutrient inputs into coordinated control of cell survival, proliferation, metabolism, and growth. The protein contains an N‑terminal pleckstrin homology domain that binds phosphatidylinositol 3,4,5‑trisphosphate at the plasma membrane, a central catalytic kinase domain with the conserved activation loop threonine, and a C‑terminal regulatory tail harboring a hydrophobic motif serine and other residues that tune activity and interactions with upstream kinases and phosphatases. Activation begins when receptor tyrosine kinases, G protein–coupled receptors, or other receptors stimulate class I PI3K to generate phosphatidylinositol 3,4,5‑trisphosphate, which recruits Akt1 and its upstream kinase PDK1 to the membrane via their pleckstrin homology domains; PDK1 phosphorylates the activation loop threonine and mTOR complex 2 phosphorylates the C‑terminal hydrophobic motif serine, together producing full Akt1 catalytic activity. Protein phosphatases such as PP2A and PHLPP reverse these phosphorylations, while PTEN and related lipid phosphatases suppress Akt1 indirectly by dephosphorylating phosphatidylinositol 3,4,5‑trisphosphate, establishing a balance between kinase and phosphatase activities that defines Akt1 signaling amplitude and duration. Once active, Akt1 phosphorylates substrates containing an RxRxxS/T motif across multiple compartments, including the pro-apoptotic Bcl‑2 family member Bad, FoxO transcription factors, and components of the intrinsic caspase machinery, which shifts signaling toward survival and resistance to apoptotic triggers. Akt1 also modulates metabolism and nutrient handling through targets such as AS160 and glycolytic regulators, couples insulin and growth factor signaling to glucose transport and glycogen synthesis via inhibition of GSK‑3 isoforms, and regulates cell-cycle progression by phosphorylating p21 and p27 to influence their stability and localization. Direct phosphorylation of TSC2 and other elements of the TSC1–TSC2–mTOR axis links Akt1 to mTOR complex 1 activation, eIF4F assembly, and protein synthesis, placing this kinase at the core of growth and anabolic signaling networks.

References
https://pubmed.ncbi.nlm.nih.gov/30901610/

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%