PIM1 Human

PIM1 was first identified as a proviral integration site in Moloney murine leukemia virus-induced T-cell lymphomas. It is highly conserved across species, indicating its crucial role in cellular functions. PIM1 is predominantly expressed in hematopoietic and germ line cells, but its expression is also upregulated in various cancers, including prostate cancer and diffuse large B-cell lymphoma .

PIM1 kinase has a molecular weight of approximately 44 kDa and consists of a single catalytic domain. It phosphorylates a variety of substrates, including proteins involved in cell cycle regulation and apoptosis. One of its key functions is the phosphorylation of the pro-apoptotic protein BAD, which inhibits apoptosis and promotes cell survival. Additionally, PIM1 can phosphorylate and activate other kinases and transcription factors, further influencing cell proliferation and survival .

Recombinant PIM1 is produced using various expression systems, including insect cells and bacterial systems. The recombinant protein is often tagged with a His-tag to facilitate purification. It is used extensively in research to study its biochemical properties, substrate specificity, and potential as a therapeutic target. The recombinant form retains the kinase activity of the native protein, making it a valuable tool for in vitro studies .

The overexpression of PIM1 in cancers has made it a target for therapeutic intervention. Inhibitors of PIM1 kinase are being developed and tested for their efficacy in treating cancers with high PIM1 expression. Studies have shown that PIM1 inhibitors can reduce tumor growth and enhance the effectiveness of other chemotherapeutic agents. The role of PIM1 in cancer makes it a promising target for drug development .