Recombinant Proteins
Product List
STIP1 Human
Stress-Induced-Phosphoprotein 1 Human Recombinant
STIP1 Human, His
Stress-Induced-Phosphoprotein 1 Human Recombinant, His Tag
STIP1 Mouse
Stress-Induced-Phosphoprotein 1 Mouse Recombinant
Introduction
STIP, or Stress-Induced Phosphoprotein 1 (STIP1), is a protein-coding gene that plays a crucial role in cellular stress responses. It is also known by other names such as HOP (Hsp70-Hsp90 Organizing Protein) and STI1. STIP1 is classified as an adaptor protein that coordinates the functions of heat shock proteins HSP70 and HSP90, which are essential for protein folding and stabilization .
Key Biological Properties: STIP1 is involved in the regulation of protein folding by mediating the interaction between HSP70 and HSP90. It stimulates the ATPase activity of HSP70 and inhibits the ATPase activity of HSP90, thus regulating their conformations and ATPase cycles .
Expression Patterns: STIP1 is ubiquitously expressed in various tissues, with higher expression levels observed in the brain, testis, and skeletal muscle .
Tissue Distribution: The protein is found in multiple tissues, including lymphoid tissue, bone marrow, testis, skeletal muscle, and various immune cells such as NK-cells and T-cells .
Primary Biological Functions: STIP1 acts as a co-chaperone for HSP90, facilitating the transfer of client proteins from HSP70 to HSP90. It plays a critical role in protein folding, stabilization, and degradation .
Role in Immune Responses: STIP1 is involved in the innate immune response, particularly in lymphoid tissues and bone marrow .
Pathogen Recognition: While specific details on pathogen recognition are limited, STIP1’s role in immune responses suggests it may be involved in recognizing and responding to pathogenic stress.
Mechanisms with Other Molecules and Cells: STIP1 interacts with HSP70 and HSP90, forming a complex that assists in protein folding. It also interacts with other proteins such as JAK2, influencing various signaling pathways .
Binding Partners: STIP1 binds to HSP70 and HSP90, facilitating the transfer of client proteins between these chaperones .
Downstream Signaling Cascades: STIP1 is involved in the JAK2/STAT3 signaling pathway, where it stabilizes JAK2 and promotes its phosphorylation, leading to enhanced cell viability and resistance to cell death .
Expression and Activity Control: The expression of STIP1 is regulated at the transcriptional level by various transcription factors. Post-translational modifications, such as phosphorylation by JAK2, also play a role in regulating its activity .
Transcriptional Regulation: Specific transcription factors that regulate STIP1 expression are not well-documented, but it is likely influenced by stress-responsive elements.
Post-Translational Modifications: Phosphorylation by JAK2 enhances STIP1’s stability and promotes its nuclear-cytoplasmic shuttling .
Biomedical Research: STIP1 is a valuable target in cancer research due to its role in stabilizing oncogenic proteins and promoting cell survival .
Diagnostic Tools: Elevated levels of STIP1 can serve as biomarkers for certain cancers, aiding in diagnosis and prognosis .
Therapeutic Strategies: Targeting STIP1 interactions with HSP70, HSP90, and JAK2 offers potential therapeutic strategies for cancer treatment .
Development to Aging and Disease: STIP1 plays a critical role throughout the life cycle, from development to aging. It is involved in protein homeostasis, which is essential for cellular function and longevity. Dysregulation of STIP1 is associated with various diseases, including cancer and neurodegenerative disorders .
