The PIM-1 (proto-oncogene serine/threonine-protein kinase) protein is an epithelial-derived, integral membrane serine protease. This protease forms a complex with the Kunitz-type serine protease inhibitor, HAI-1, and is activated by sphingosine 1-phosphate. PIM-1 cleaves and activates hepatocyte growth factor/scattering factor (HGF) as well as urokinase plasminogen activator (uPA). Such downstream targets implicate this serine protease as an epithelial membrane trigger for a sequential protease cascade. PIM-1 expression is associated with many tumors including breast, colon, prostate, and ovarian. Hematologists at UCLA used the PIM-1 antibody to characterize the physiological effects of ABT-869, a multi-targeted receptor tyrosine kinase inhibitor1. This group found that ABT-869 blocked FMS-like tyrosine kinase 3-internal tandem duplication (FLT3) phosphorylation, induced apoptosis, decreased proliferation, reduced tumor formation, and increased survival in their acute myeloid leukemia (AML) models.
Immunohistochemistry-Paraffin: PIM1 Antibody
Prendergast’s group also employed the PIM-1 antibody to study centromere chromatin with respect to pre-mitosis assembly and inheritance of a histone fold complex2. Their data led them to propose that the different centromere CENP proteins are specifically utilized for centromere and kinetochore functions. Studies on innate immunity relied upon ELISA assays with the PIM-1 antibody identified five novel autoantibodies that could contribute to type I interferon production in plasmacytoid dendritic cells in a nucleic acid-independent fashion3. These newly found antibodies appear to function in a variety of cell processes and should be further studied.
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