KDEL receptor 3 Inhibitors
Chemical inhibitors of KDEL receptor 3 target various aspects of cellular function to disrupt the protein's role in recycling endoplasmic reticulum (ER) resident proteins from the Golgi apparatus back to the ER. Brefeldin A and Monensin interfere with vesicle formation and cation gradients, respectively, which are essential for the proper functioning of the Golgi apparatus. The disruption caused by these chemicals leads to a compromise in KDEL receptor 3's ability to cycle between the Golgi and the ER, thus inhibiting its protein recycling capability. Tunicamycin and Castanospermine target glycosylation processes and glucosidase enzymes, critical for the folding and trafficking of glycoproteins. As KDEL receptor 3 is a transmembrane protein reliant on proper glycosylation for its function, these inhibitors can impair the receptor's ability to bind to and recycle proteins. Similarly, Swainsonine and Deoxynojirimycin inhibit enzymes involved in glycan processing, which can lead to misfolding and mislocalization of glycoproteins, including KDEL receptor 3, obstructing its normal recycling function.
Additional inhibitors such as Thapsigargin, which disrupts calcium homeostasis in the ER, can affect KDEL receptor 3's binding affinity and recycling due to altered calcium levels. Microtubule-disrupting agents like Colchicine and Nocodazole directly inhibit KDEL receptor 3 by preventing its trafficking along the microtubule network, essential for its intracellular movement and function. Bafilomycin A1 and Chloroquine raise the pH within intracellular compartments, affecting the pH-dependent ligand binding and release that is crucial for KDEL receptor 3's recycling process. Lastly, EerI induces ER stress and the unfolded protein response, leading to an accumulation of misfolded proteins in the ER. This stress can effectively inhibit KDEL receptor 3's function by overwhelming the receptor with an excess of proteins to recycle, thereby impeding its role in maintaining ER homeostasis.
SEE ALSO...
Items 1 to 10 of 12 total
Display:
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
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 is known to disrupt the Golgi apparatus by inhibiting the ADP-ribosylation factor, which is crucial for vesicle formation and protein trafficking. This disruption can lead to the inhibition of KDEL receptor 3 by impairing its ability to recycle proteins from the Golgi to the endoplasmic reticulum, its primary function. | ||||||
Monensin A | 17090-79-8 | sc-362032 sc-362032A | 5 mg 25 mg | $152.00 $515.00 | ||
Monensin is an ionophore that disrupts Golgi function by altering pH and cation gradients. This alteration inhibits the normal functioning of KDEL receptor 3 by preventing its proper cycling between the Golgi and the endoplasmic reticulum, thereby inhibiting the receptor's protein recycling capability. | ||||||
Tunicamycin | 11089-65-9 | sc-3506A sc-3506 | 5 mg 10 mg | $169.00 $299.00 | 66 | |
Tunicamycin inhibits N-linked glycosylation in the endoplasmic reticulum. As glycosylation can be crucial for the proper functioning and localization of transmembrane proteins like KDEL receptor 3, its inhibition would disrupt the receptor's cycling and binding to ligands. | ||||||
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 depletion of calcium stores in the endoplasmic reticulum. This depletion can indirectly inhibit KDEL receptor 3 function by affecting its binding affinity and recycling due to altered calcium homeostasis. | ||||||
Castanospermine | 79831-76-8 | sc-201358 sc-201358A | 100 mg 500 mg | $180.00 $620.00 | 10 | |
Castanospermine is an inhibitor of glucosidase I and II, enzymes involved in the trimming of N-linked glycoproteins in the ER. This inhibition can impair the folding and trafficking of glycoproteins, potentially inhibiting the function of KDEL receptor 3 by disrupting its glycoprotein binding and recycling. | ||||||
Swainsonine | 72741-87-8 | sc-201362 sc-201362C sc-201362A sc-201362D sc-201362B | 1 mg 2 mg 5 mg 10 mg 25 mg | $135.00 $246.00 $619.00 $799.00 $1796.00 | 6 | |
Swainsonine is an inhibitor of Golgi alpha-mannosidase II. By inhibiting this enzyme, the glycan processing is halted, which can lead to a mislocalization and dysfunction of glycoproteins like KDEL receptor 3, inhibiting its recycling ability. | ||||||
Deoxynojirimycin | 19130-96-2 | sc-201369 sc-201369A | 1 mg 5 mg | $72.00 $142.00 | ||
Deoxynojirimycin is an inhibitor of alpha-glucosidase enzymes involved in the processing of N-linked glycans in the ER. This inhibition can affect the proper folding and function of KDEL receptor 3, impeding its protein trafficking role. | ||||||
Colchicine | 64-86-8 | sc-203005 sc-203005A sc-203005B sc-203005C sc-203005D sc-203005E | 1 g 5 g 50 g 100 g 500 g 1 kg | $98.00 $315.00 $2244.00 $4396.00 $17850.00 $34068.00 | 3 | |
Colchicine disrupts microtubule polymerization, affecting cellular transport mechanisms. The disruption of microtubules can inhibit the trafficking of KDEL receptor 3, as its movement within the cell is dependent on the microtubule network. | ||||||
Nocodazole | 31430-18-9 | sc-3518B sc-3518 sc-3518C sc-3518A | 5 mg 10 mg 25 mg 50 mg | $58.00 $83.00 $140.00 $242.00 | 38 | |
Similar to colchicine, nocodazole disrupts microtubules. This disruption can lead to the inhibition of the trafficking and function of KDEL receptor 3 by impairing its movement along the microtubule network within the cell. | ||||||
Bafilomycin A1 | 88899-55-2 | sc-201550 sc-201550A sc-201550B sc-201550C | 100 µg 1 mg 5 mg 10 mg | $96.00 $250.00 $750.00 $1428.00 | 280 | |
Bafilomycin A1 is a V-ATPase inhibitor that prevents acidification of organelles like lysosomes and endosomes. By preventing this acidification, the function of KDEL receptor 3 can be inhibited as it relies on proper organelle pH for its recycling and ligand release. | ||||||