CALR4 Activators
Calreticulin 4 (Calr4) stands as a key player in cellular homeostasis, primarily localized in the endoplasmic reticulum membrane. Predicted to exhibit calcium ion binding activity, Calr4 is implicated in fundamental cellular processes such as protein folding and the ubiquitin-dependent endoplasmic reticulum-associated protein degradation (ERAD) pathway. Within the intricate network of the endoplasmic reticulum, Calr4 fulfills its role in ensuring the correct folding of proteins, contributing to the maintenance of cellular protein quality control. Its engagement in the ubiquitin-dependent ERAD pathway underscores its responsibility in identifying and removing misfolded proteins, preventing their accumulation and maintaining the overall integrity of the endoplasmic reticulum membrane.
The activation of Calr4 involves a nuanced interplay of various cellular mechanisms orchestrated by diverse chemical regulators. These regulators impact Calr4 indirectly or directly, influencing its predicted functions. For instance, chemical chaperones, such as those alleviating endoplasmic reticulum stress, support Calr4 in facilitating proper protein folding. Inhibition of the proteasome or disruption of ER-Golgi trafficking indirectly stimulates Calr4, emphasizing its role in recognizing and managing misfolded proteins. Calcium ionophores directly affect Calr4 by increasing cytosolic calcium levels, a crucial aspect of its calcium ion binding activity. Metabolic regulators, like those inducing ER stress through energy depletion or activating AMP-activated protein kinase (AMPK), influence Calr4 expression and function. These diverse activators collectively contribute to the orchestrated cellular response, highlighting Calr4 as a linchpin in the intricate landscape of cellular proteostasis within the endoplasmic reticulum. Understanding these molecular interactions deepens our comprehension of fundamental cellular processes and provides insights into the broader framework of maintaining cellular homeostasis.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Thapsigargin | 67526-95-8 | sc-24017 sc-24017A | 1 mg 5 mg | $136.00 $446.00 | 114 | |
Thapsigargin, a SERCA inhibitor, indirectly activates Calr4 by disrupting calcium homeostasis. Inhibition of SERCA elevates cytosolic calcium levels, leading to increased binding activity of Calr4 to calcium ions. This influences protein folding and supports the ubiquitin-dependent ERAD pathway in the endoplasmic reticulum membrane. | ||||||
Tunicamycin | 11089-65-9 | sc-3506A sc-3506 | 5 mg 10 mg | $172.00 $305.00 | 66 | |
Tunicamycin, an N-glycosylation inhibitor, indirectly upregulates Calr4 by inducing ER stress. In response to unfolded proteins, Calr4 is recruited to aid in proper protein folding, contributing to ER homeostasis. This activation supports the protein folding function and engagement in the ubiquitin-dependent ERAD pathway. | ||||||
Brefeldin A | 20350-15-6 | sc-200861C sc-200861 sc-200861A sc-200861B | 1 mg 5 mg 25 mg 100 mg | $31.00 $53.00 $124.00 $374.00 | 25 | |
Brefeldin A, an ER-Golgi transport inhibitor, indirectly activates Calr4 by disrupting ER-Golgi trafficking. Impaired protein transport induces ER stress, leading to the recruitment of Calr4 for proper folding, thereby supporting its role in the ubiquitin-dependent ERAD pathway. | ||||||
A23187 | 52665-69-7 | sc-3591 sc-3591B sc-3591A sc-3591C | 1 mg 5 mg 10 mg 25 mg | $55.00 $131.00 $203.00 $317.00 | 23 | |
A23187, a calcium ionophore, directly influences Calr4 by increasing cytosolic calcium levels. Elevated calcium binding activity of Calr4 enhances its involvement in protein folding and the ubiquitin-dependent ERAD pathway within the endoplasmic reticulum membrane. | ||||||
4-Phenylbutyric acid | 1821-12-1 | sc-232961 sc-232961A sc-232961B | 25 g 100 g 500 g | $53.00 $136.00 $418.00 | 10 | |
4-Phenylbutyric Acid (4-PBA), a chemical chaperone, indirectly upregulates Calr4 by alleviating ER stress. By facilitating proper protein folding, 4-PBA supports Calr4 function, contributing to the ubiquitin-dependent ERAD pathway and maintaining endoplasmic reticulum membrane integrity. | ||||||
Geldanamycin | 30562-34-6 | sc-200617B sc-200617C sc-200617 sc-200617A | 100 µg 500 µg 1 mg 5 mg | $39.00 $59.00 $104.00 $206.00 | 8 | |
Geldanamycin, an HSP90 inhibitor, indirectly activates Calr4 by inducing protein misfolding. Inhibition of HSP90 leads to the accumulation of misfolded proteins, requiring Calr4 for proper folding and engagement in the ubiquitin-dependent ERAD pathway within the endoplasmic reticulum membrane. | ||||||
2-Deoxy-D-glucose | 154-17-6 | sc-202010 sc-202010A | 1 g 5 g | $70.00 $215.00 | 26 | |
2-Deoxy-D-glucose (2-DG), a glycolysis inhibitor, indirectly upregulates Calr4 by inducing ER stress through energy depletion. This triggers Calr4 recruitment for proper protein folding and supports its involvement in the ubiquitin-dependent ERAD pathway within the endoplasmic reticulum membrane. | ||||||
Salubrinal | 405060-95-9 | sc-202332 sc-202332A | 1 mg 5 mg | $34.00 $104.00 | 87 | |
Salubrinal, an eIF2α phosphatase inhibitor, indirectly stimulates Calr4 by promoting ER stress. Inhibition of eIF2α dephosphorylation leads to increased misfolded proteins, necessitating Calr4 for proper folding and contributing to the ubiquitin-dependent ERAD pathway within the endoplasmic reticulum membrane. | ||||||
A-769662 | 844499-71-4 | sc-203790 sc-203790A sc-203790B sc-203790C sc-203790D | 10 mg 50 mg 100 mg 500 mg 1 g | $184.00 $741.00 $1076.00 $3417.00 $5304.00 | 23 | |
A769662, an AMPK activator, indirectly stimulates Calr4 by regulating energy homeostasis. AMPK activation influences Calr4 expression and function, supporting its role in protein folding and the ubiquitin-dependent ERAD pathway within the endoplasmic reticulum membrane. | ||||||
Sodium phenylbutyrate | 1716-12-7 | sc-200652 sc-200652A sc-200652B sc-200652C sc-200652D | 1 g 10 g 100 g 1 kg 10 kg | $77.00 $166.00 $622.00 $5004.00 $32783.00 | 43 | |
Sodium phenylbutyrate, a prodrug of 4-PBA, indirectly upregulates Calr4 by alleviating ER stress. Similar to 4-PBA, it acts as a chemical chaperone, facilitating proper protein folding and supporting Calr4 function in the ubiquitin-dependent ERAD pathway within the endoplasmic reticulum membrane. | ||||||