Code | CSB-EP001553HU |
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Size | $224 |
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To produce recombinant human AKT1 in E. coli, the gene of interest is co-cloned into a vector with an N-terminal GST-tag gene and transformed into E. coli cells. The gene of interest encodes the full-length human AKT1 (1-480aa). The cells are cultured to express the AKT1 protein and then lysed to extract it. The harvested protein is purified using affinity chromatography. Its purity is checked with SDS-PAGE, reaching over 90%.
The Human AKT1 protein is a serine/threonine-protein kinase that belongs to the protein kinase B (PKB) family. AKT1 phosphorylates various substrates, indicating its role in diverse cellular processes [1]. It plays a crucial role in various cellular processes such as cell growth, survival, glucose metabolism, genome stability, and neovascularization [2][3]. The phosphorylation-dependent substrate selectivity of AKT1 underscores its specificity in signaling cascades [4]. AKT1 is a key mediator of the PI3K/AKT/mTOR signaling pathway, which is essential for regulating cell proliferation and inhibiting apoptosis, particularly in cancer [5]. Human AKT1 has been identified to have 215 unique human proteins as its experimentally verified substrates, highlighting its significance in cellular signaling networks [6]. The activation of AKT1 is initiated by binding its pleckstrin homology (PH) domain to phosphoinositides, followed by phosphorylation at specific regulatory amino acids, serine 473 and threonine 308 [7].
References:
[1] M. McKenna, N. Balasuriya, S. Zhong, S. Li, & P. O’Donoghue, Phospho-form specific substrates of protein kinase b (akt1), Frontiers in Bioengineering and Biotechnology, vol. 8, 2021. https://doi.org/10.3389/fbioe.2020.619252
[2] Y. Yoshioka, T. Suzuki, Y. Matsuo, M. Nakakido, G. Tsurita, C. Simoneet al., Smyd3-mediated lysine methylation in the ph domain is critical for activation of akt1, Oncotarget, vol. 7, no. 46, p. 75023-75037, 2016. https://doi.org/10.18632/oncotarget.11898
[3] J. Testa and A. Bellacosa, Akt plays a central role in tumorigenesis, Proceedings of the National Academy of Sciences, vol. 98, no. 20, p. 10983-10985, 2001. https://doi.org/10.1073/pnas.211430998
[4] N. Balasuriya, N. Davey, J. Johnson, H. Liu, K. Biggar, L. Cantleyet al., Phosphorylation-dependent substrate selectivity of protein kinase b (akt1), Journal of Biological Chemistry, vol. 295, no. 24, p. 8120-8134, 2020. https://doi.org/10.1074/jbc.ra119.012425
[5] H. Zhao, B. Martin, M. Bisoffi, & D. Dunaway-Mariano, The akt c-terminal modulator protein is an acyl-coa thioesterase of the hotdog-fold family, Biochemistry, vol. 48, no. 24, p. 5507-5509, 2009. https://doi.org/10.1021/bi900710w
[6] F. Chen, Q. Liu, T. Hilliard, T. Wang, H. Liang, W. Gaoet al., A chemical-genetics and nanoparticle enabled approach for in vivo protein kinase analysis,, 2020. https://doi.org/10.1101/2020.05.13.094573
[7] A. Kumar, V. Rajendran, R. Sethumadhavan, & R. Purohit, Akt kinase pathway: a leading target in cancer research, The Scientific World Journal, vol. 2013, p. 1-6, 2013. https://doi.org/10.1155/2013/756134
Applications : Glutathione S transferase (GST) pull-down assay
Review: GST pull-down analysis showed direct binding between recombinant UPP1 and recombinant AKT in vitro (Fig. 6C).
By Anonymous
I am interested in several of your recombinant proteins. Can you please provide some informations:
For CSB-EP001553HU (all expression systems):
a.Sequence
b.Tag type
c.Tag position
d.Sizes and formats
e.Is the protein provided soluble in solution?
f.Is the protein purified from bacterial inclusion bodies are you supplied refolded or still in urea?
g.I want to use this protein for conjugation purposes and need it supplied in an amine free buffer (so not Tris). Can you supply this protein in one of the buffers at my request: phosphate, carbonate, or borate? Would there be an extra charge?