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<p>An essential modulator of cell growth and division is the evolutionarily conserved kinase (S6K1). It is triggered by certain stimulants, including amino acids, insulin, and other growth hormones. The Akt/phosphatidylinositol 3-kinase pathway's downstream effector, the serine/threonine kinase S6K1, is consistently activated in a variety of cancer types. Rho family guanosine triphosphate (GTPase) activation and actin filament cross-linking are two of S6K1's roles. The p70 (∆2-146/∆CT104) S6K is a truncated variant of p70S6 kinase, created by removing 146 amino acids from the N-terminal and 104 amino acids from the C-terminal end of the original protein, resulting in a total of 275 amino acids. The p70 (∆2-146/∆CT104) S6K was effectively expressed in the <i>E. coli</i> BL21 (DE3)pLysS strain after being cloned in <i>E. coli</i> DH5α. A rabbit polyclonal anti-GST antibody had been employed during Western blot analysis throughout the protein's production and purification process. Protein purification was achieved by affinity chromatography using glutathione resin-agarose beads, and chromatography onto a spin concentration column was performed. Rabbit polyclonal anti-(p70S6Kinase and GST) antibodies confirmed the presence of the purified protein.</p> Graphic Abstract <p></p>

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Expression and Purification of p70 (∆NH2-146/∆CT104) S6 K, a 57.3 kDa N- and C-Terminal Truncated p70S6 Kinase-GST Fusion Protein in Bacterial Expression System

  • 期刊论文

  • 发表日期：

    2025年12月8日

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  • Shafat A. Latoo

摘要

An essential modulator of cell growth and division is the evolutionarily conserved kinase (S6K1). It is triggered by certain stimulants, including amino acids, insulin, and other growth hormones. The Akt/phosphatidylinositol 3-kinase pathway's downstream effector, the serine/threonine kinase S6K1, is consistently activated in a variety of cancer types. Rho family guanosine triphosphate (GTPase) activation and actin filament cross-linking are two of S6K1's roles. The p70 (∆2-146/∆CT104) S6K is a truncated variant of p70S6 kinase, created by removing 146 amino acids from the N-terminal and 104 amino acids from the C-terminal end of the original protein, resulting in a total of 275 amino acids. The p70 (∆2-146/∆CT104) S6K was effectively expressed in the E. coli BL21 (DE3)pLysS strain after being cloned in E. coli DH5α. A rabbit polyclonal anti-GST antibody had been employed during Western blot analysis throughout the protein's production and purification process. Protein purification was achieved by affinity chromatography using glutathione resin-agarose beads, and chromatography onto a spin concentration column was performed. Rabbit polyclonal anti-(p70S6Kinase and GST) antibodies confirmed the presence of the purified protein.

Graphic Abstract