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anti-Human PIM1 Antikörper:
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Human Polyclonal PIM1 Primary Antibody für IHC (p), WB - ABIN392440
Wallentine, Kim, Seiler, Vaughn, Crockett, Tripp, Elenitoba-Johnson, Lim: Comprehensive identification of proteins in Hodgkin lymphoma-derived Reed-Sternberg cells by LC-MS/MS. in Laboratory investigation; a journal of technical methods and pathology 2007
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Human Polyclonal PIM1 Primary Antibody für IP, PLA - ABIN250694
Shankar, Li, Tapang, Owen McCall, Pease, Dai, Wei, Albert, Bouska, Osterling, Guo, Marcotte, Johnson, Soni, Hartandi, Michaelides, Davidsen, Priceman, Chang, Rhodes, Shah, Moore, Sakamoto, Glaser: ABT-869, a multitargeted receptor tyrosine kinase inhibitor: inhibition of FLT3 phosphorylation and signaling in acute myeloid leukemia. in Blood 2007
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Human Monoclonal PIM1 Primary Antibody für ELISA - ABIN948263
Menter, Ernst, Drachneris, Dirnhofer, Barghorn, Went, Tzankov: Phenotype profiling of primary testicular diffuse large B-cell lymphomas. in Hematological oncology 2014
Human Polyclonal PIM1 Primary Antibody für IHC (p), WB - ABIN392441
Baron, Anastasi, Hyjek, Bies, Reddy, Dong, Joseph, Thirman, Wroblewski, Wolff, Baron: PIM1 gene cooperates with human BCL6 gene to promote the development of lymphomas. in Proceedings of the National Academy of Sciences of the United States of America 2012
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.
Results show that PIM-1 is upregulated in pancreatic cancer tissues and plasma. Its knockdown in pancreatic cancer cells suppressed proliferation, induced cell cycle arrest, enhanced apoptosis, resensitized cells to gemcitabine and erlotinib treatment, and inhibited ABCG2 (zeige ABCG2 Antikörper) and EZH2 (zeige EZH2 Antikörper) mRNA expression.
Results show that PIM1 is overexpressed in breast cancer tumors and provide evidence for its role in tumor resistance to PI3K (zeige PIK3CA Antikörper) inhibitors.
These results demonstrate the involvement of PIM kinases in LIF (zeige LIF Antikörper)-induced regulation in different trophoblastic cell lines which may indicate similar functions in primary cells.
Down-regulation of UHRF1 (zeige UHRF1 Antikörper) is an important mechanism of PIM1-mediated cellular senescence.
PIM kinases in classical Hodgkin lymphoma exhibit pleiotropic effects, orchestrating tumor immune escape and supporting Reed-Sternberg cell survival.
Triple negative breast cancer cells, but not nonmalignant mammary epithelial cells, were dependent on PIM1 for proliferation and protection from apoptosis.
PIM1 expression was higher in triple negative breast tumors than in estrogen and progesterone receptor (zeige PGR Antikörper) positive tumors.
High PIM1 expression is associated with osteosarcoma.
downregulation of PIM1 led to suppression of cell proliferation by cell cycle arrest at G1 phase and suppression of cell invasion and migration.
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 (zeige MLXIP Antikörper)-15b as an early response to Dicer (zeige DICER1 Antikörper) depletion silenced Pim-1 kinase resulting in mitochondrial dysfunction. Rescue experiments demonstrated that suppression of miRNA-15b induction in Dicer (zeige DICER1 Antikörper)-deleted adult hearts result in marked amelioration of cardiac dysfunction.
Pim-1L protects hepatic ABCA1 (zeige ABCA1 Antikörper) from lysosomal degradation by facilitating the physical interaction between ABCA1 (zeige ABCA1 Antikörper) and liver X receptor beta (zeige NR1H2 Antikörper) and subsequent stabilization of the ABCA1 (zeige ABCA1 Antikörper)-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 (zeige HGF Antikörper)-induced tumor cell migration, invasion, and cell scattering.
these results identify Pim1 as a novel effector molecule sufficient to drive CD4 (zeige CD4 Antikörper)( ) alphabeta T-cell development and survival in the absence of gammac cytokine receptor (zeige LEPR Antikörper) 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.
Pim-1 activity prevents Drp1 (zeige CRMP1 Antikörper) compartmentalization to the mitochondria and preserves reticular mitochondrial morphology in response to sI
Inhibition of the Pim1 oncogene (zeige RAB1A Antikörper) 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