TOLLIP Human
Toll-interacting protein, TOLLIP, IL-1RAcPIP.
Description
TOLLIP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 294 amino acids (1-274 a.a) and having a molecular mass of 32.4kDa.
TOLLIP is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Toll-interacting protein (TOLLIP) is an important regulatory protein in the innate immune system. It acts as a brake on the Toll-like receptor (TLR) pathway, which is responsible for detecting and responding to pathogens. By dampening TLR signaling, TOLLIP helps to prevent excessive inflammation and immune responses. In addition to its role in immunity, TOLLIP also interacts with a protein called Tom1 to control the transport of proteins within cells.
This product consists of the human TOLLIP protein, manufactured in a laboratory setting using E. coli bacteria. It is a single chain of 294 amino acids, with a molecular weight of 32.4kDa. For purification and detection purposes, a 20 amino acid His-tag is attached to the protein's N-terminus. The protein is purified to a high degree using specialized chromatographic methods.
The TOLLIP protein is provided in a solution at a concentration of 0.25mg/ml. The solution also contains 20mM Tris-HCl buffer (pH 8.0), 40% glycerol, 0.2M NaCl, and 2mM DTT.
For short-term storage (up to 1 week), the TOLLIP protein can be kept at 4°C. For longer storage, it is recommended to store the protein below -18°C. Repeated freezing and thawing of the protein should be avoided.
Toll-interacting protein, TOLLIP, IL-1RAcPIP.
MGSSHHHHHH SSGLVPRGSH MATTVSTQRG PVYIGELPQD FLRITPTQQQ RQVQLDAQAA QQLQYGGAVG TVGRLNITVV QAKLAKNYGM TRMDPYCRLR LGYAVYETPT AHNGAKNPRW NKVIHCTVPP GVDSFYLEIF DERAFSMDDR IAWTHITIPE SLRQGKVEDK WYSLSGRQGD DKEGMINLVM SYALLPAAMV MPPQPVVLMP TVYQQGVGYV PITGMPAVCS PGMVPVALPP AAVNAQPRCS EEDLKAIQDM FPNMDQEVIR SVLEAQRGNK DAAINSLLQM GEEP.
Product Science Overview
Toll-Interacting Protein 1 (TOLLIP) is a ubiquitously expressed intracellular adaptor protein that plays a crucial role in various intracellular signaling pathways. It is involved in mediating inflammatory responses, promoting autophagy, and enabling vacuole transport within cells . TOLLIP is increasingly recognized for its role in the pathophysiology of several diseases, including neurodegenerative diseases, pulmonary diseases, cardiovascular diseases, inflammatory bowel disease, and malignancies .
TOLLIP was first identified in 2000 through two-hybrid screening using the IL-1 receptor accessory protein as bait . It forms a constitutive complex with the interleukin-1 receptor-associated kinase 1 (IRAK1), which is essential for its function in the IL-1R/TLR-NF-κB signaling pathways . TOLLIP is expressed in various cell types, including epithelial cells, macrophages, alveolar type II cells, and basal cells .
TOLLIP is a key regulator of the acute inflammatory response. It modulates the IL-1R/TLR-NF-κB signaling pathways, which are critical for the body’s immune response to infections and injuries . In the central nervous system, TOLLIP has been shown to play a role in neuroinflammation, particularly in the substantia nigra pars compacta, a structure affected in Parkinson’s disease . Studies have demonstrated that TOLLIP knockout mice exhibit increased susceptibility to neuroinflammation, highlighting its importance in regulating inflammatory responses in the brain .
TOLLIP is also involved in autophagy, a cellular process that degrades and recycles cellular components . It plays a role in vacuole trafficking, which is essential for maintaining cellular homeostasis and responding to stress conditions . Dysregulation of these processes can lead to various diseases, including neurodegenerative diseases and malignancies .
Given its involvement in multiple intracellular processes, TOLLIP is a potential target for therapeutic interventions in various diseases. Research has shown that TOLLIP plays a role in the pathogenesis of neurodegenerative diseases, pulmonary diseases, cardiovascular diseases, inflammatory bowel disease, and malignancies . Understanding the mechanisms by which TOLLIP regulates these processes can inform the development of novel therapeutic strategies.
