Date published: 2026-5-16

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TSR3 Activators

The chemical class of TSR3 activators encompasses a diverse array of molecules that modulate TSR3 activity by targeting cellular pathways involved in protein folding and ER stress response. These activators exert their effects by promoting protein folding, reducing ER stress, and enhancing cellular protein quality control mechanisms. Thapsigargin and tunicamycin, for example, activate TSR3 indirectly by inducing ER stress through the inhibition of calcium pumps and glycosylation, respectively. This ER stress triggers the unfolded protein response (UPR), leading to the upregulation of TSR3 expression and its involvement in protein folding within the ER.

Additionally, chemical chaperones such as 4-phenylbutyric acid (4-PBA) and sodium 4-phenylbutyrate activate TSR3 by assisting in protein folding and trafficking within the ER, thereby reducing ER stress and allowing TSR3 to function optimally. Other activators like geldanamycin and MG-132 activate TSR3 by targeting protein quality control mechanisms, such as the inhibition of heat shock protein 90 (HSP90) and the proteasome, respectively, leading to the upregulation of TSR3 expression and its involvement in protein folding and degradation processes. Overall, TSR3 activators play crucial roles in maintaining protein homeostasis and cellular function by regulating protein folding and ER stress response pathways.

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Items 11 to 12 of 12 total

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Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

2-Deoxy-D-glucose

154-17-6sc-202010
sc-202010A
1 g
5 g
$70.00
$215.00
26
(2)

2-Deoxy-D-glucose (2-DG) activates TSR3 by inhibiting glycolysis, leading to ATP depletion and the activation of the AMP-activated protein kinase (AMPK) pathway. AMPK activation triggers the unfolded protein response (UPR) and upregulates TSR3 expression to enhance protein folding capacity and alleviate endoplasmic reticulum (ER) stress.

Guanabenz HCl

23113-43-1sc-507500
100 mg
$246.00
(0)

Guanabenz activates TSR3 by inhibiting eukaryotic translation initiation factor 2 alpha (eIF2α) phosphatase, leading to sustained phosphorylation of eIF2α and attenuation of protein synthesis. Reduced protein synthesis lowers the influx of nascent proteins into the endoplasmic reticulum (ER), alleviating ER stress and promoting TSR3-mediated protein folding.