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Results provide evidence that glucose deprivation is one of the mechanisms that leads to elevated Pim1 expression in colorectal cancer (CRC (show CALR Proteins)), and Pim1 upregulation ensures CRC (show CALR Proteins) growth in response to glucose deprivation by facilitating the Warburg effect in a compensatory way.
data suggest that PIM1/2 kinase overexpression is a common feature of male reproductive organs tumors, which provoke tissue alterations and a large inflammatory response that may act synergistically during the process of tumorigenesis.
PIM-1 mRNA levels may be an independent prognostic factor in acute myeloid leukemia (show BCL11A Proteins).
PIM1 role in cell proliferation, migration and apoptosis in triple-negative breast cancer [review]
Inhibition of PIM1 kinase attenuates inflammation-induced pro-labor mediators in human fetal membranes in vitro.
PIM1 destabilization is associated with cancer.
The Ser/Thr-protein kinase-1 (PIM-1) was identified as a direct target of miR (show MLXIP Proteins)-328.
Data show that PIM1 contributes to melanoma cell proliferation and tumor growth in vivo; however, the presence of PIM2 (show PIM2 Proteins) and PIM3 (show PIM3 Proteins) could also influence the outcome.
High expression level of PIM is associated with neoplasms.
This review summarizes effects of PIM kinases and their substrates especially on cancer cell migration, invasion and metastatic growth, based on data from cell-based assays, animal experiments and patients.
Pim-1 is a novel kinase that phosphorylates cTnI primarily at Ser23/24 and Ser150 in cardiomyocytes, which in turn may modulate myofilament function under a variety of physiological and pathophysiological conditions.
this study shows that Pim-1 dysregulation has developmental-stage-specific effects on B lymphopoiesis and early myeloid, but not erythroid progenitors
Results show that elevated miR (show MLXIP Proteins)-15b as an early response to Dicer (show DICER1 Proteins) depletion silenced Pim-1 kinase resulting in mitochondrial dysfunction. Rescue experiments demonstrated that suppression of miRNA-15b induction in Dicer (show DICER1 Proteins)-deleted adult hearts result in marked amelioration of cardiac dysfunction.
Pim-1L protects hepatic ABCA1 (show ABCA1 Proteins) from lysosomal degradation by facilitating the physical interaction between ABCA1 (show ABCA1 Proteins) and liver X receptor beta (show NR1H2 Proteins) and subsequent stabilization of the ABCA1 (show ABCA1 Proteins)-Pim-1L complex and thereby regulates the circulating level of high-density lipoprotein.
Pim1 kinase activity maintains airway epithelial integrity and protects against house dust mite-induced proinflammatory activation of the airway epithelium.
Pim kinases prevent premature cardiac aging and maintain a healthy pool of functional mitochondria leading to efficient cellular energetics.
Pim-1 kinase activity regulates hepatocyte growth factor (show HGF Proteins)-induced tumor cell migration, invasion, and cell scattering.
these results identify Pim1 as a novel effector molecule sufficient to drive CD4 (show CD4 Proteins)( ) alphabeta T-cell development and survival in the absence of gammac cytokine receptor (show LEPR Proteins) signaling.
Our data suggest that Pim1 might contribute to progression rather than initiation in prostate neoplasia.
Loss of PIM1 is associated with abnormal hematopoietic phenotypes.
Inhibition of the Pim1 oncogene (show RAB1A Proteins) results in diminished visual function.
Pim1 overexpression enhanced the effect of intramyocardial delivery of CSCs to infarcted porcine hearts.
The protein encoded by this gene belongs to the Ser/Thr protein kinase family, and PIM subfamily. This gene is expressed primarily in B-lymphoid and myeloid cell lines, and is overexpressed in hematopoietic malignancies and in prostate cancer. It plays a role in signal transduction in blood cells, contributing to both cell proliferation and survival, and thus provides a selective advantage in tumorigenesis. Both the human and orthologous mouse genes have been reported to encode two isoforms (with preferential cellular localization) resulting from the use of alternative in-frame translation initiation codons, the upstream non-AUG (CUG) and downstream AUG codons (PMIDs:16186805, 1825810).
, pim-1 kinase 44 kDa isoform
, pim-1 oncogene (proviral integration site 1)
, proto-oncogene serine/threonine-protein kinase pim-1
, serine/threonine-protein kinase pim-1
, pim-1 oncogene
, non-specific serine/threonine protein kinase
, proto-oncogene serine/threonine-protein kinase Pim-1
, proviral integration site 1
, kinase pim-1
, proviral integration site 2
, serine/threonine-protein kinase Pim-1
, serine/threonine-protein kinase pim-2