Recombinant Human TR-1 protein (Tagged) is a Human Fragment protein, in the 40 to 330 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE.
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Neuron-specific restriction factor that prevents herpes simplex virus 1 (HHV-1) infection in the brain by blocking viral entry (PubMed:39048823, PubMed:39048830). Also able to restrict herpes simplex virus 2 (HHV-2) infection, although to a lesser extent (PubMed:39048823). Acts by preventing the association between the viral glycoprotein D (gD) and its cell surface receptor NECTIN1, thereby inhibiting fusion of the virus and the cell membrane (PubMed:39048823, PubMed:39048830). Also able to prevent the association between the viral glycoprotein B (gB) and MYH9/NMMHC-IIA and MYH10/NMMHC-IIB receptors (PubMed:39048823). May be a tumor suppressor in brain cancers (PubMed:12743596).
C9orf2, TMEFF1, Tomoregulin-1, TR-1, H7365, Transmembrane protein with EGF-like and one follistatin-like domain
Recombinant Human TR-1 protein (Tagged) is a Human Fragment protein, in the 40 to 330 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE.
pH: 7.2 - 7.4
Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)
Neuron-specific restriction factor that prevents herpes simplex virus 1 (HHV-1) infection in the brain by blocking viral entry (PubMed:39048823, PubMed:39048830). Also able to restrict herpes simplex virus 2 (HHV-2) infection, although to a lesser extent (PubMed:39048823). Acts by preventing the association between the viral glycoprotein D (gD) and its cell surface receptor NECTIN1, thereby inhibiting fusion of the virus and the cell membrane (PubMed:39048823, PubMed:39048830). Also able to prevent the association between the viral glycoprotein B (gB) and MYH9/NMMHC-IIA and MYH10/NMMHC-IIB receptors (PubMed:39048823). May be a tumor suppressor in brain cancers (PubMed:12743596).
Belongs to the tomoregulin family.
The TR-1 protein also known by the alternative name 'TR' is a thioredoxin reductase enzyme with a molecular mass of approximately 55 kDa. This protein is expressed in various tissues including the liver and heart and is part of the broader family of selenoproteins. TR-1 is responsible for catalyzing the reduction of thioredoxin using the electrons from NADPH to maintain a reducing environment in the cell. This activity is essential for various cellular processes ensuring the proper function and stability of cellular components.
TR-1 plays an important role in the regulation of oxidative stress by maintaining the redox balance within the cell. It is an important component of a cellular complex involved in the detoxification of reactive oxygen species (ROS). Through its enzymatic activity TR-1 helps protect cells from oxidative damage and supports the regulation of cellular growth and apoptosis. Furthermore TR-1 influences DNA synthesis by facilitating ribonucleotide reductase activity highlighting its significance in cellular proliferation.
TR-1 is involved in the antioxidant defense system and the regulation of apoptosis pathways. It interacts with proteins like thioredoxin and glutathione peroxidase in the ROS detoxification pathway highlighting its role in cellular defense mechanisms. Moreover the interaction of TR-1 with other redox-related proteins ensures the modulation of apoptotic signaling pathways therefore balancing cell survival and programmed cell death.
TR-1 shows a connection to cancer and neurodegenerative diseases. Altered TR-1 activity has been linked to cancer where it affects tumor growth due to its role in cell proliferation and survival. Dysregulated redox balance from TR-1 malfunction contributes to cancer cell resistance to therapy. Additionally in neurodegenerative diseases TR-1's involvement with proteins like glutathione peroxidase plays a part in mitigating cellular damage from oxidative stress thereby affecting the progression of neurodegenerative conditions.
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ab238288 analyzed by (Tris-Glycine gel) discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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