GrpEL1 Activators
GrpE-like 1 (GrpEL1) activators represent a niche class of chemical compounds that interact with the GrpE protein family, specifically the GrpEL1 variant. GrpE proteins are a part of heat shock protein (Hsp) 70 complexes, which play a pivotal role in cellular stress responses. These proteins function as co-chaperones and are involved in the regulation and stabilization of Hsp70 activities. The GrpEL1 activators specifically target the GrpEL1 variant, influencing its interaction with Hsp70 proteins. The precise mechanism by which these activators function involves modulating the intrinsic ATPase activity of the Hsp70 proteins, thereby affecting their ability to bind and release substrate proteins. This modulation is crucial because it is intimately connected to the protein folding processes within the cell, ensuring proteins achieve and maintain their correct three-dimensional conformation, a state essential for proper cellular function.
Chemically, GrpEL1 activators can be diverse, encompassing small molecules, peptides, or other biologically active compounds that have been identified or designed to interact with the GrpEL1 protein. These activators are recognized for their ability to bind to specific regions on the GrpEL1 protein, which may induce conformational changes that enhance the activity of GrpEL1. The binding event often occurs at sites distinct from the nucleotide-binding domain of the Hsp70, suggesting a non-competitive mechanism of action. By engaging with GrpEL1, these activators can potentially influence the dynamics of the protein complex, affecting the cycle of binding and release events that are fundamental to the Hsp70 protein's operational cycle. Understanding and manipulating these interactions at the molecular level can lead to insights into the fundamental cellular processes of protein folding and maintenance, which are central to the functioning of all living cells.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Cyclosporin A | 59865-13-3 | sc-3503 sc-3503-CW sc-3503A sc-3503B sc-3503C sc-3503D | 100 mg 100 mg 500 mg 10 g 25 g 100 g | $62.00 $90.00 $299.00 $475.00 $1015.00 $2099.00 | 69 | |
Cyclosporin A is an immunosuppressant that binds to the cyclophilins and inhibits calcineurin. By inhibiting calcineurin, Cyclosporin A prevents the dephosphorylation and activation of NFAT, a transcription factor. Since NFAT regulates the expression of stress response genes, its inhibition could increase the need for GrpEL1's protein folding chaperone activity as a compensatory mechanism to manage cellular stress. | ||||||
Forskolin | 66575-29-9 | sc-3562 sc-3562A sc-3562B sc-3562C sc-3562D | 5 mg 50 mg 1 g 2 g 5 g | $76.00 $150.00 $725.00 $1385.00 $2050.00 | 73 | |
Forskolin is an activator of adenylate cyclase, leading to increased levels of cAMP in the cell. High cAMP levels activate PKA, which can phosphorylate and activate numerous proteins, including those involved in the unfolded protein response (UPR). Activation of the UPR would likely increase the demand for GrpEL1's chaperone activity to handle misfolded proteins. | ||||||
17-AAG | 75747-14-7 | sc-200641 sc-200641A | 1 mg 5 mg | $66.00 $153.00 | 16 | |
17-AAG is an Hsp90 inhibitor that disrupts its chaperone function, leading to the accumulation of unfolded proteins. This increase in unfolded proteins can activate the UPR, indirectly increasing the requirement for GrpEL1's chaperoning function in repairing or degrading misfolded proteins. | ||||||
MG-132 [Z-Leu- Leu-Leu-CHO] | 133407-82-6 | sc-201270 sc-201270A sc-201270B | 5 mg 25 mg 100 mg | $56.00 $260.00 $980.00 | 163 | |
MG132 is a proteasome inhibitor that prevents the degradation of ubiquitinated proteins, leading to their accumulation. The buildup of damaged or misfolded proteins can trigger the UPR and consequently enhance the cellular demand for GrpEL1's chaperone activity. | ||||||
Brefeldin A | 20350-15-6 | sc-200861C sc-200861 sc-200861A sc-200861B | 1 mg 5 mg 25 mg 100 mg | $30.00 $52.00 $122.00 $367.00 | 25 | |
Brefeldin A disrupts the function of the Golgi apparatus, impeding protein trafficking and potentially leading to protein misfolding. This disruption can activate the UPR, thereby increasing the need for GrpEL1 to assist in protein folding and maintain cellular homeostasis. | ||||||
Thapsigargin | 67526-95-8 | sc-24017 sc-24017A | 1 mg 5 mg | $94.00 $349.00 | 114 | |
Thapsigargin is a SERCA pump inhibitor that leads to the depletion of calcium stores from the endoplasmic reticulum, inducing ER stress. This stress activates the UPR, which could then enhance the demand for GrpEL1's function in mitigating unfolded protein accumulation. | ||||||
Tunicamycin | 11089-65-9 | sc-3506A sc-3506 | 5 mg 10 mg | $169.00 $299.00 | 66 | |
Tunicamycin inhibits N-linked glycosylation, causing protein misfolding and triggering the UPR. The induction of the UPR likely enhances the requirement for GrpEL1's role in managing misfolded or unassembled proteins. | ||||||
2-Deoxy-D-glucose | 154-17-6 | sc-202010 sc-202010A | 1 g 5 g | $65.00 $210.00 | 26 | |
2-Deoxy-D-glucose is a glycolysis inhibitor that leads to energy depletion and ER stress, further activating the UPR. This activation increases the need for the chaperone function of GrpEL1 in coping with the stress. | ||||||
Salubrinal | 405060-95-9 | sc-202332 sc-202332A | 1 mg 5 mg | $33.00 $102.00 | 87 | |
Salubrinal is a selective inhibitor of eIF2α dephosphorylation. Phosphorylation of eIF2α is a key part of the UPR, leading to reduced global protein synthesis and upregulation of chaperones like GrpEL1 to alleviate ER stress. | ||||||
Celastrol, Celastrus scandens | 34157-83-0 | sc-202534 | 10 mg | $155.00 | 6 | |
Celastrol is a proteasome inhibitor and induces heat shock response, leading to an increase in molecular chaperones including GrpEL1 to manage the misfolded proteins. | ||||||