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Anti-phospho-Akt (pThr308) antibody produced in rabbit

affinity isolated antibody


biological source


Quality Level



antibody form

affinity isolated antibody

antibody product type

primary antibodies




buffered aqueous solution

mol wt

antigen 55 kDa

species reactivity

mouse, rat, human


~1 mg/mL


ELISA: 1:10000
immunohistochemistry: 1:50-1:100
western blot: 1:500-1:1000

NCBI accession no.

UniProt accession no.

shipped in

wet ice

storage temp.


Gene Information

General description

The AKT/protein kinase B gene has three homologues, namely PKBα (Akt1), PKBβ (Akt2), and PKBγ (Akt3), which are localized to human chromosome 14q32, 19q13, and 1q44, respectively. The members of AKT family contain an amino-terminal pleckstrin homology (PH) domain, a short α-helical linker, and a carboxyl-terminal kinase domain. The AKT1 and AKT2 genes are expressed highly in insulin-responsive tissues, such as brown fat.


The antiserum was produced against synthesized peptide derived from human Akt around the phosphorylation site of Thr308.

Immunogen Range: 276-325


Anti-phospho-Akt (pThr308) antibody produced in rabbit has been used in immunoblotting.

Biochem/physiol Actions

AKT is activated in a multistep process that involves its translocation across the membrane and its phosphorylation. The 3′-phosphorylated phosphoinositides, 3,4,5-trisphosphate (PI-3,4,5-P3) and PI-3,4,-P2 produced by PI3K bind to the PH (pleckstrin homology) domain and this binding facilitates the localization of AKT kinases to the plasma membrane. Once localized, PDK1 (3-phosphoinositide-dependent kinase) phosphorylates Thr-308/309 residue on the AKT molecule, which is essential for its activation. Another residue, Ser- 473/474 on AKT, is also phosphorylated by PDK2. This phosphorylation, although not necessary, increases the activity of AKT. It plays a role in cell survival by regulating the effect of growth factors. AKT may facilitate phosphorylation and inactivation of glycogen synthase kinase-3 by insulin. In adipocytes, it may be involved in the activation of glucose transporter translocation. It is involved in the regulation of several proteins that are involved in cellular processes, such as metabolism, apoptosis, and proliferation. Variations in PI3K-AKT signaling have been observed in several types of cancer, such as human gastric cancer, prostate and breast cancers.

Features and Benefits

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Physical form

Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.


Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Storage Class Code

12 - Non Combustible Liquids



Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Certificate of Origin

PS48 can replace bovine serum albumin in pig embryo culture medium, and improve in vitro embryo development by phosphorylating AKT
Spate LD
Molecular Reproduction and Development, 82, 315?320-315?320 (2015)
Lee D Spate et al.
Molecular reproduction and development, 82(4), 315-320 (2015-03-18)
The application of embryo-related technology is dependent on in vitro culture systems. Unfortunately, most culture media are suboptimal and result in developmentally compromised embryos. Since embryo development is partially dependent upon Warburg Effect-like metabolism, our goal was to test the
PI3K-Akt pathway: Its functions and alterations in human cancer
Osaki, M
Apoptosis, 9, 667-676 (2004)
Protein kinase B/Akt mediates effects of insulin on hepatic insulin-like growth factor-binding protein-1 gene expression through a conserved insulin response sequence.
Cichy, S
The Journal of Biological Chemistry, 273, 6482-6487 (1998)
J Matthew Kuczmarski et al.
Experimental physiology, 103(4), 545-558 (2018-01-10)
What is the central question of this study? Translocation of nNOSμ initiates catabolic signalling via FoxO3a and skeletal muscle atrophy during mechanical unloading. Recent evidence suggests that unloading-induced muscle atrophy and FoxO3a activation are redox sensitive. Will a mimetic of

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