Prothymosin Alpha Human Recombinant
Prothymosin Human Recombinant
Prothymosin α (PTMA) is an unstructured, highly acidic protein with an isoelectric point of 3.5 . It belongs to the thymosin family, which includes various peptides initially isolated from the thymus gland. Prothymosin α is ubiquitously expressed in a wide range of cell types and has been implicated in numerous physiological and pathological processes .
Key Biological Properties: Prothymosin α is characterized by its unstructured nature and high acidity. It is predominantly a nuclear protein but can also function in the cytoplasm and extracellularly .
Expression Patterns: Prothymosin α is expressed in a variety of cell types, including those in the brain, stomach, and thymus . Its expression is particularly prominent in proliferating cells and tissues undergoing rapid growth or repair .
Tissue Distribution: The protein is widely distributed across different tissues, with notable presence in the thymus, brain, and stomach . In the brain, it is prominently stained in the nucleus, whereas in the stomach, it is observed in the cytoplasm .
Primary Biological Functions: Prothymosin α plays a crucial role in cell proliferation, apoptosis, and immune responses . It is involved in protecting cells from oxidative stress and regulating the expression of genes associated with oxidative stress defense .
Role in Immune Responses: Prothymosin α acts as an immunomodulator, stimulating the proliferation and differentiation of lymphocytes . It also enhances the production of interleukin-2 and the expression of interleukin-2 receptors in T lymphocytes .
Pathogen Recognition: The protein is involved in the recognition and response to pathogens, contributing to the body’s defense mechanisms .
Mechanisms with Other Molecules and Cells: Prothymosin α interacts with various cellular components, including histone H1 and transcription factors . It modulates the interaction of histone H1 with chromatin, affecting the regulation of gene expression .
Binding Partners: The protein binds to linker histone H1, influencing the stoichiometry and mode of interaction of H1 with chromatin . It also interacts with tripartite motif-containing protein 21 (TRIM21), regulating the ubiquitination and stability of PTMA .
Downstream Signaling Cascades: Prothymosin α is involved in the regulation of the nuclear factor erythroid 2-related factor 2 (Nrf2) signaling pathway, which plays a key role in cellular defense against oxidative stress .
Transcriptional Regulation: The expression of prothymosin α is regulated by various transcription factors, including c-myc and E2F . Its mRNA levels increase during the S/G2 phase of the cell cycle .
Post-Translational Modifications: Prothymosin α undergoes proteolytic modifications that influence its interactions with other molecules and its functional roles . These modifications include the binding to TRIM21, which regulates its ubiquitination and stability .
Biomedical Research: Prothymosin α is extensively studied for its role in cell proliferation, apoptosis, and immune responses. It serves as a model protein for understanding the mechanisms of unstructured proteins .
Diagnostic Tools: The protein’s expression levels and modifications can serve as biomarkers for various diseases, including cancer and immune disorders .
Therapeutic Strategies: Prothymosin α has potential therapeutic applications in cancer immunotherapy and the treatment of immunodeficiencies and autoimmune diseases . It is also being explored for its role in enhancing immune responses in viral infections .
Development: Prothymosin α is involved in the proliferation and differentiation of cells during development . Its expression is crucial for the growth and repair of tissues .
Aging: The protein’s levels and activity may decline with age, contributing to decreased immune function and increased susceptibility to diseases .
Disease: Prothymosin α is implicated in various diseases, including cancer, where it is associated with cell proliferation and survival . It also plays a role in protecting cells from apoptosis and oxidative stress .