Date published: 2026-5-15

1-800-457-3801

SCBT Portrait Logo
Seach Input

EOGT_A130022J15Rik Activators

EOGT activators encompass a range of chemical compounds that can enhance the functional activity of EOGT through their influence on various cellular processes. These activators often disrupt cellular homeostasis, particularly related to protein folding and processing in the endoplasmic reticulum (ER). For instance, thapsigargin and cyclopiazonic acid disrupt calcium homeostasis, which can lead to an increase in misfolded proteins in the ER. EOGT, which is involved in O-glycosylation of proteins within the ER, can enhance its functional activity to cope with this increased load. Similarly, dithiothreitol, a reducing agent, can lead to misfolded proteins in the ER, necessitating enhanced EOGT activity.

Furthermore, compounds such proteasome inhibitors like MG132 and epoxomicin, lead to an accumulation of unfolded or unprocessed proteins. This increased protein load necessitates an enhancement in the functional activity of EOGT as part of the ER's protein folding machinery. Additionally, microtubule-disrupting agents such as vinblastine can cause disturbances in intracellular transport, potentially enhancing EOGT activity asmore proteins might require folding and processing within the ER. Moreover, ionophores like ionomycin, which disrupts normal ion gradients within the cell, can increase the load of misfolded proteins in the ER and thus lead to enhanced EOGT activity. This is due to EOGT's role in the glycosylation of proteins, a process integral to proper protein folding and function.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Thapsigargin

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

Thapsigargin is a non-competitive inhibitor of the sarco/endoplasmic reticulum Ca2+ ATPase (SERCA). It disrupts calcium homeostasis within the cell. EOGT, which is involved in O-glycosylation of proteins within the ER, can be functionally enhanced to cope with the resulting imbalance in protein folding and processing.

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 induce ER stress by interfering with calcium homeostasis. This can lead to an increase in misfolded proteins, potentially enhancing the functional activity of EOGT in protein folding and processing within the ER.

Ionomycin, free acid

56092-81-0sc-263405
sc-263405A
1 mg
5 mg
$96.00
$264.00
2
(2)

Ionomycin is a calcium ionophore that disrupts calcium homeostasis within the cell. This can increase the load of misfolded proteins in the ER, enhancing the functional activity of EOGT in protein folding and processing.

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 is a proteasome inhibitor that prevents protein degradation. This can lead to protein accumulation within the cell, enhancing EOGT activity as it deals with the increased protein folding and processing load.

Epoxomicin

134381-21-8sc-201298C
sc-201298
sc-201298A
sc-201298B
50 µg
100 µg
250 µg
500 µg
$137.00
$219.00
$449.00
$506.00
19
(2)

Epoxomicin is a proteasome inhibitor that prevents protein degradation. The resulting protein accumulation enhances EOGT activity to cope with the increased protein folding and processing load.

Vinblastine

865-21-4sc-491749
sc-491749A
sc-491749B
sc-491749C
sc-491749D
10 mg
50 mg
100 mg
500 mg
1 g
$102.00
$235.00
$459.00
$1749.00
$2958.00
4
(0)

Vinblastine is a microtubule-disrupting agent. The disruption of intracellular transport can enhance EOGT function, as it may need to deal with an increased load of proteins requiring folding and processing in the ER.

Cyclopiazonic Acid

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

Cyclopiazonic Acid is a specific inhibitor of SERCA leading to disruption in calcium homeostasis. This disturbance can enhance EOGT activity due to increased protein folding and processing demands in the ER.