Recombinant Human TRC40 protein is a Human Full Length protein, in the 1 to 348 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.
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Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application MS | Reactivity Reacts | Dilution info - | Notes - |
ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors GET1/WRB and CAMLG/GET2, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the GET1-CAMLG receptor, and returning it to the cytosol to initiate a new round of targeting. May be involved in insulin signaling.
ARSA, ASNA1, TRC40, GET3, ATPase GET3, Arsenical pump-driving ATPase, Arsenite-stimulated ATPase, Transmembrane domain recognition complex 40 kDa ATPase subunit, hARSA-I, hASNA-I
Recombinant Human TRC40 protein is a Human Full Length protein, in the 1 to 348 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.32% Tris HCl
ab134590 is purified using conventional chromatography techniques.
ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors GET1/WRB and CAMLG/GET2, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the GET1-CAMLG receptor, and returning it to the cytosol to initiate a new round of targeting. May be involved in insulin signaling.
Belongs to the arsA ATPase family.
TRC40 also known as the transmembrane domain recognition complex subunit is a 41 kDa protein important for targeting and insertion of tail-anchored proteins into the endoplasmic reticulum membrane. It is well-expressed in human tissue especially those with high secretory or membrane protein activity. The protein interacts closely with the cytosolic components and serves as an important part of the guiding mechanism for specific proteins important for cellular function.
The targeting process involves TRC40 interacting with several tail-anchored proteins. It forms part of a delivery complex required for efficient insertion of these proteins into the correct cellular locations. TRC40 ensures accurate membrane localization firmly supporting cellular physiology and protein homeostasis. This activity is essential for maintaining the protein synthesis balance within the endoplasmic reticulum influencing many cellular metabolic processes.
TRC40 operates in the endoplasmic reticulum-associated degradation (ERAD) and secretory pathways. It cooperates with proteins like BAG6 and the Get3 complex acting as routing machinery for tail-anchored protein targeting. These pathways play a critical role in maintaining cellular protein composition by sorting membrane proteins essential for cellular health and stress responses.
TRC40 shows a significant role in neurodegenerative diseases and metabolic syndromes. Misregulation or dysfunction of its targeting process can disrupt protein homeostasis linking it to disorders such as Alzheimer's disease. The ERAD pathway involving TRC40 interacts with proteins like APP and presenilin contributing to the progression of these neurodegenerative conditions. Insights into TRC40's function reveal potential therapeutic targets in tackling related diseases.
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15% SDS-PAGE analysis of 3 µg ab134590
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