Date published: 2026-5-17

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HDEL Activators

Regarding the chemical class called KDELR1 Activators, it encompasses compounds that indirectly influence the activity of KDELR1, mainly through modulation of ER stress, protein folding, and trafficking processes. These compounds do not directly bind to or activate KDELR1 but can create cellular conditions that necessitate enhanced KDELR1 activity. For instance, agents that induce ER stress, such as Tunicamycin or Thapsigargin, can increase the demand for KDELR1-mediated retrieval of misfolded proteins from the Golgi to the ER. Similarly, compounds affecting protein folding efficiency, like Dithiothreitol or 4-Phenylbutyric acid, might indirectly increase KDELR1 activity by altering the load of proteins requiring ER retrieval.

Furthermore, compounds influencing proteasomal degradation or lysosomal function, like MG132 or Chloroquine, can indirectly affect the dynamics of protein trafficking between the ER and Golgi, modifying the functional demand on KDELR1. The efficacy and specificity of these compounds in modulating KDELR1 activity depend on the context of their application and the interplay with other cellular processes

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Tunicamycin

11089-65-9sc-3506A
sc-3506
5 mg
10 mg
$172.00
$305.00
66
(3)

Tunicamycin causes ER stress by inhibiting N-linked glycosylation, potentially affecting KDELR1 activity by increasing the demand for protein retrieval to the ER.

Thapsigargin

67526-95-8sc-24017
sc-24017A
1 mg
5 mg
$136.00
$446.00
114
(2)

Thapsigargin disrupts ER calcium homeostasis, leading to ER stress. This stress could enhance the role of KDELR1 in protein retrieval as part of the unfolded protein response.

Brefeldin A

20350-15-6sc-200861C
sc-200861
sc-200861A
sc-200861B
1 mg
5 mg
25 mg
100 mg
$31.00
$53.00
$124.00
$374.00
25
(3)

Brefeldin A disrupts Golgi apparatus structure, which might influence KDELR1's role in retrieving proteins from the Golgi to the ER.

4-Phenylbutyric acid

1821-12-1sc-232961
sc-232961A
sc-232961B
25 g
100 g
500 g
$53.00
$136.00
$418.00
10
(1)

4-Phenylbutyric acid acts as a chemical chaperone, potentially modulating the load on KDELR1 by influencing protein folding efficiency in the ER.

MG-132 [Z-Leu- Leu-Leu-CHO]

133407-82-6sc-201270
sc-201270A
sc-201270B
5 mg
25 mg
100 mg
$60.00
$265.00
$1000.00
163
(3)

MG132 inhibits proteasomal degradation, potentially leading to increased ER stress and altered KDELR1 activity in response to altered protein trafficking dynamics.

Cyclopiazonic Acid

18172-33-3sc-201510
sc-201510A
10 mg
50 mg
$176.00
$624.00
3
(1)

Cyclopiazonic acid inhibits the SERCA pump, leading to ER calcium depletion and potential changes in KDELR1 function due to ER stress.

Glyburide (Glibenclamide)

10238-21-8sc-200982
sc-200982A
sc-200982D
sc-200982B
sc-200982C
1 g
5 g
25 g
100 g
500 g
$46.00
$61.00
$117.00
$173.00
$530.00
36
(1)

Glibenclamide affects ER stress and may indirectly influence KDELR1 activity through its impact on ER homeostasis.

Ionomycin

56092-82-1sc-3592
sc-3592A
1 mg
5 mg
$78.00
$270.00
80
(4)

Ionomycin increases intracellular calcium levels, which could affect KDELR1 activity by altering ER stress and protein folding pathways.

Curcumin

458-37-7sc-200509
sc-200509A
sc-200509B
sc-200509C
sc-200509D
sc-200509F
sc-200509E
1 g
5 g
25 g
100 g
250 g
1 kg
2.5 kg
$37.00
$69.00
$109.00
$218.00
$239.00
$879.00
$1968.00
47
(1)

Curcumin can modulate ER stress and the unfolded protein response, possibly influencing KDELR1's role in protein retrieval.

Resveratrol

501-36-0sc-200808
sc-200808A
sc-200808B
100 mg
500 mg
5 g
$80.00
$220.00
$460.00
64
(2)

Resveratrol influences several cellular stress pathways, potentially affecting KDELR1 activity indirectly through its role in ER stress response.