Our Anti-AKT (Thr342) rabbit polyclonal phosphospecific primary antibody from PhosphoSolutions is produced in-house. It detects drosophila AKT (Thr342) and is antigen affinity purified from pooled serum. It is great for use in WB.
Western blot of Drosophila lysate showing specific labeling of the ~68 kDa AKT protein phosphorylated at Thr342 in the first lane (-). Phosphospecificity is shown in the second lane (+) where the immunolabeling is completely eliminated by blot treatment with lambda phosphatase (λ-Ptase, 1200 units for 30 minutes).
The serine/threonine kinase Akt also known as protein kinase B (PKB) or Rac, plays a crucial role in controlling many diverse and important cellular functions such as cell survival and glycogen metabolism (Hajduch et al., 2001 and Nicholson & Anderson, 2002). Three isoforms (α, β, and γ) have been identified that can be activated rapidly in response to insulin and growth factors in a phosphoinositide 3-kinase (PI3K)-dependent fashion (Hajduch et al., 2003). Phosphorylation of Aktα occurs at two specific regulatory sites in Drosophila, one localized in the kinase domain, Thr342, and the other in the C-terminal regulatory domain, Ser505: these two activation sites are homologous to mammalian Ser473 and Thr308 respectively (Powell et al., 2004).
Antigen Affinity Purified from Pooled Serum
Polyclonal
IgG
WB
Rabbit
AKT1
68 kDa
Synthetic phospho-peptide corresponding to amino acid residues surrounding Thr342 of Drosophila AKT, conjugated to keyhole limpet hemocyanin (KLH)
Drosophila
AB_2492036
Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.
Liquid
Prepared from pooled rabbit serum by affinity purification via sequential chromatography on phospho and non-phosphopeptide affinity columns.
10 mM HEPES (pH 7.5), 150 mM NaCl, 100 µg per ml BSA and 50% glycerol.
WB: 1:500
Unconjugated
Specific for endogenous levels of the ~68 kDa AKT protein phosphorylated at Thr342. Immunolabeling is completely eliminated with λ-phosphatase treatment. It has been reported that this antibody may also recognize some level of phosphorylated S6K as there is 67% homology with the sequence used as antigen.
Phosphorylated
Thr342
Western blots performed on each lot.
For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.
After date of receipt, stable for at least 1 year at -20°C.
Xu, Y., et al. 2019. Chronic dysfunction of Stromal interaction molecule by pulsed RNAi induction in fat tissue impairs organismal energy homeostasis in Drosophila. Scientific Reports, 9(1), p.6989.
Post, S., et al. 2018. Drosophila insulin-like peptides DILP2 and DILP5 differentially stimulate cell signaling and glycogen phosphorylase to regulate longevity. Frontiers in Endocrinology, May 28; 9:245.
Lin, F., et al. 2017. Total solid-phase synthesis of biologically active drosophila insulin-like peptide 2 (DILP2). Australian Journal of Chemistry, 70(2), pp.208-212.
Schleich, S., et al. 2014. DENR-MCT-1 promotes translation re-initiation downstream of uORFs to control tissue growth. Nature. Aug 14; 512(7513):208-12.
Martinson, E., et al. 2022. Insulin-like peptide 3 stimulates hemocytes to proliferate in anautogenous and facultatively autogenous mosquitoes. The Journal of Experimental Biology, 225(5).