Recombinant Proteins
Product List
PIM1 Human
PIM1 Human Recombinant
PIM2 Human
PIM2 Human Recombinant
PIM2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Introduction
The Pim oncogene family consists of serine/threonine kinases, which are enzymes that phosphorylate target proteins on serine or threonine residues. The family includes three members: Pim-1, Pim-2, and Pim-3. These kinases are classified as proto-oncogenes, meaning they have the potential to cause cancer when mutated or overexpressed.
Key Biological Properties: Pim kinases are characterized by their ability to promote cell survival, proliferation, and differentiation. They are constitutively active, meaning they do not require activation by upstream signals.
Expression Patterns: Pim kinases are expressed in various tissues, with Pim-1 being predominantly found in hematopoietic tissues, Pim-2 in the liver and spleen, and Pim-3 in the pancreas and brain.
Tissue Distribution: Pim-1 is highly expressed in the bone marrow, spleen, and thymus. Pim-2 is found in the liver, spleen, and lymph nodes, while Pim-3 is present in the brain, pancreas, and gastrointestinal tract.
Primary Biological Functions: Pim kinases play crucial roles in cell cycle progression, apoptosis inhibition, and metabolic regulation. They are involved in the regulation of various cellular processes, including protein synthesis, cell growth, and survival.
Role in Immune Responses: Pim kinases are important for the development and function of immune cells. They regulate the survival and proliferation of T cells, B cells, and natural killer (NK) cells, contributing to the immune response.
Pathogen Recognition: Pim kinases are involved in the recognition and response to pathogens. They modulate the activity of immune cells, enhancing their ability to detect and eliminate infectious agents.
Mechanisms with Other Molecules and Cells: Pim kinases interact with various signaling molecules and cellular components. They phosphorylate target proteins, altering their activity and function.
Binding Partners: Pim kinases have several binding partners, including transcription factors, cell cycle regulators, and apoptotic proteins. These interactions modulate the activity of target proteins, influencing cellular processes.
Downstream Signaling Cascades: Pim kinases activate multiple downstream signaling pathways, including the PI3K/Akt and mTOR pathways. These cascades regulate cell growth, survival, and metabolism.
Regulatory Mechanisms: The expression and activity of Pim kinases are tightly regulated at multiple levels.
Transcriptional Regulation: Pim gene expression is controlled by various transcription factors, including STAT3, NF-κB, and Myc. These factors bind to the promoter regions of Pim genes, modulating their transcription.
Post-Translational Modifications: Pim kinases undergo several post-translational modifications, including phosphorylation, ubiquitination, and sumoylation. These modifications influence their stability, localization, and activity.
Biomedical Research: Pim kinases are studied extensively in cancer research due to their role in tumorigenesis. They are potential targets for developing novel cancer therapies.
Diagnostic Tools: Elevated levels of Pim kinases can serve as biomarkers for certain cancers, aiding in diagnosis and prognosis.
Therapeutic Strategies: Inhibitors of Pim kinases are being developed as potential cancer treatments. These inhibitors aim to block the activity of Pim kinases, reducing tumor growth and survival.
Development: Pim kinases are essential for normal development, particularly in the hematopoietic system. They regulate the proliferation and differentiation of stem cells and progenitor cells.
Aging: The activity of Pim kinases declines with age, contributing to age-related changes in cellular function and immune response.
Disease: Dysregulation of Pim kinases is associated with various diseases, including cancer, cardiovascular diseases, and metabolic disorders. Understanding their role in these conditions can lead to new therapeutic approaches.
