KIAA0247 Activators
Stress-activated protein kinases impart key control over KIAA0247 stress functions. PERK branch of the UPR directly upregulates KIAA0247 expression. Meanwhile, p38/JNK pathways potentiate KIAA0247 activity by inducing cytoprotective chaperone transcription. Compounds exploiting these regulation points maximize KIAA0247 functionality. ER toxins bortezomib and thapsigargin optimize KIAA0247 production through precise PERK stimulation. Oxidizers arsenite and doxorubicin engage p38 to sustain KIAA0247-mediated quality control apparatus against affronts.
Proteasome inhibitors bortezomib and MG-132 directly stimulate KIAA0247 activity. Bortezomib triggers ER stress through proteasomal degradation inhibition, potentiating KIAA0247 expression of chaperones and ubiquitin ligases that resolve resulting misfolded protein accumulation. MG-132 likewise inhibits the proteasome, furnishing KIAA0247 substrates for compensation via precisely induced proteostasis factors. Additionally, ER stressors tunicamycin and thapsigargin activate KIAA0247 functions against accumulating substrates. Tunicamycin impairs glycosylation, providing aberrantly folded polypeptides that KIAA0247 coordinates for ER-associated degradation.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Bortezomib | 179324-69-7 | sc-217785 sc-217785A | 2.5 mg 25 mg | $135.00 $1085.00 | 115 | |
Bortezomib triggers ER stress by inhibiting proteasomal degradation. KIAA0247 enhances proteostasis through MAPK-mediated induction of chaperone expression in response to ER stress. | ||||||
Tunicamycin | 11089-65-9 | sc-3506A sc-3506 | 5 mg 10 mg | $172.00 $305.00 | 66 | |
Tunicamycin elicits ER stress through N-glycosylation inhibition. KIAA0247 preserves proteome integrity against improper folding via ER-associated degradation of incorrectly processed substrates. | ||||||
Thapsigargin | 67526-95-8 | sc-24017 sc-24017A | 1 mg 5 mg | $136.00 $446.00 | 114 | |
Thapsigargin depletes ER calcium levels, eliciting UPR signaling. KIAA0247 expression rises downstream of PERK/eIF2α activation in the UPR, augmenting stress response functions. | ||||||
MG-132 [Z-Leu- Leu-Leu-CHO] | 133407-82-6 | sc-201270 sc-201270A sc-201270B | 5 mg 25 mg 100 mg | $60.00 $265.00 $1000.00 | 163 | |
MG-132 inhibits the proteasome similarly to bortezomib, leading to KIAA0247-mediated expression of compensatory degradation components like chaperones and ubiquitin ligases. | ||||||
Sodium (meta)arsenite | 7784-46-5 | sc-250986 sc-250986A | 100 g 1 kg | $108.00 $780.00 | 3 | |
Arsenite provokes oxidative stress by generating ROS. The MAPK arm of oxidative stress signaling potentiates KIAA0247 activity to safeguard organelle function through HSP induction. | ||||||
L-Methionine | 63-68-3 | sc-394076 sc-394076A sc-394076B sc-394076C sc-394076D sc-394076E | 25 g 100 g 250 g 1 kg 5 kg 10 kg | $34.00 $37.00 $57.00 $151.00 $577.00 $1103.00 | ||
Homocysteine causes ER dysfunction through hypomethylation. KIAA0247 mitigates ensuing proteome imbalance via specialized degradation of terminally misfolded substrates. | ||||||
Temozolomide | 85622-93-1 | sc-203292 sc-203292A | 25 mg 100 mg | $91.00 $255.00 | 32 | |
Temozolomide methylates DNA, generating proteotoxicity. KIAA0247 optimizes proteostasis through precise removal of such aberrantly damaged polypeptides. | ||||||
Rotenone | 83-79-4 | sc-203242 sc-203242A | 1 g 5 g | $89.00 $259.00 | 41 | |
Rotenone impairs mitochondrial function, inducing ROS. KIAA0247 employs antioxidative mechanisms to counteract oxidative damage from respiratory poisons. | ||||||
Doxorubicin | 23214-92-8 | sc-280681 sc-280681A | 1 mg 5 mg | $176.00 $426.00 | 43 | |
Doxorubicin triggers DNA damage and oxidative stress. The oxidative injury-activated MAPK/HSF1 axis sustains KIAA0247 function against toxin-generated proteome imbalance. | ||||||
Palmitic Acid | 57-10-3 | sc-203175 sc-203175A | 25 g 100 g | $114.00 $286.00 | 2 | |
Palmitate induces ER stress through lipotoxicity. KIAA0247 exerts vital quality control through degradation of aberrant palmitoylation substrates. | ||||||