SAB4504332
Anti-phospho-Akt (pThr308) antibody produced in rabbit
affinity isolated antibody
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.41
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biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen 55 kDa
species reactivity
mouse, rat, human
concentration
~1 mg/mL
technique(s)
ELISA: 1:10000
immunohistochemistry: 1:50-1:100
western blot: 1:500-1:1000
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
phosphorylation (pThr308)
Related Categories
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.
Immunogen
The antiserum was produced against synthesized peptide derived from human Akt around the phosphorylation site of Thr308.
Immunogen Range: 276-325
Immunogen Range: 276-325
Application
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.
Disclaimer
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.
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Storage Class Code
12 - Non Combustible Liquids
WGK
nwg
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Find documentation for the products that you have recently purchased in the Document Library.
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)
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)
PI3K-Akt pathway: Its functions and alterations in human cancer
Osaki, M
Apoptosis, 9, 667-676 (2004)
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
AKT plays a central role in tumorigenesis.
Testa JR
Proceedings of the National Academy of Sciences of the USA, 98, 10983-10985 (2001)
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