Bcl-G Inhibitors
Bcl-G inhibitors as a chemical class are not well-defined due to the absence of direct inhibitors specific to Bcl-G. However, the class of compounds that can act as indirect inhibitors generally targets the broader Bcl-2 family of proteins. These compounds modulate the delicate balance between pro-apoptotic and anti-apoptotic proteins, thereby influencing apoptosis, a process in which Bcl-G is involved. The members of this chemical class often mimic the structure of BH3-only proteins or bind to the same domains on pro-survival Bcl-2 family members that BH3-only proteins would typically interact with.
Inhibitors of Bcl-G function indirectly by modulating the activity of the broader Bcl-2 family of proteins. These proteins play a key role in the intrinsic pathway of apoptosis, which is a form of programmed cell death that occurs in response to internal signals. The Bcl-2 family is composed of both pro-apoptotic and anti-apoptotic members, and the balance between these determines the cell's fate. Inhibitors that target pro-survival Bcl-2 family proteins can shift this balance in favor of cell death, thereby counteracting the anti-apoptotic function of Bcl-G.
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Items 1 to 10 of 12 total
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
ABT 263 | 923564-51-6 | sc-207241 | 5 mg | $245.00 | 16 | |
Navitoclax binds to Bcl-2 family proteins, displacing pro-apoptotic proteins like Bax, facilitating apoptosis which can reduce the functional impact of Bcl-G by freeing pro-apoptotic proteins that Bcl-G may otherwise sequester. | ||||||
Obatoclax Mesylate | 803712-79-0 | sc-364221 sc-364221A | 5 mg 10 mg | $96.00 $141.00 | ||
Obatoclax inhibits Bcl-2 family proteins, including Bcl-2, Bcl-xL, and Bcl-w, promoting apoptosis that can diminish Bcl-G's anti-apoptotic function by disrupting the mitochondrial membrane potential. | ||||||
ABT-199 | 1257044-40-8 | sc-472284 sc-472284A sc-472284B sc-472284C sc-472284D | 1 mg 5 mg 10 mg 100 mg 3 g | $118.00 $337.00 $520.00 $832.00 $1632.00 | 10 | |
Venetoclax selectively binds to Bcl-2, enhancing apoptosis. While Bcl-G is not a direct target, reducing Bcl-2 levels can indirectly influence Bcl-G's relative balance within the cell, affecting its function. | ||||||
Gossypol | 303-45-7 | sc-200501 sc-200501A | 25 mg 100 mg | $116.00 $230.00 | 12 | |
Gossypol, a polyphenolic aldehyde, interacts with multiple Bcl-2 family proteins, potentially altering the interactions of Bcl-G with its pro-apoptotic counterparts, thus promoting apoptosis. | ||||||
TW-37 | 877877-35-5 | sc-361387 sc-361387A | 10 mg 50 mg | $200.00 $860.00 | 2 | |
TW-37 binds to the BH3 domain of Bcl-2 proteins, possibly affecting Bcl-G's interaction with BH3-containing pro-apoptotic proteins, leading to apoptosis. | ||||||
ABT 737 | 852808-04-9 | sc-207242 | 2.5 mg | $204.00 | 54 | |
ABT-737 targets Bcl-2, Bcl-xL, and Bcl-w, which may facilitate the release of pro-apoptotic proteins such as Bax and Bak, thereby indirectly affecting Bcl-G's role within the cell. | ||||||
S63845 | 1799633-27-4 | sc-507518 | 1 mg | $150.00 | ||
S63845 selectively inhibits Mcl-1, a close relative of Bcl-2 family proteins. By inhibiting Mcl-1, it can shift the balance of pro- and anti-apoptotic proteins, possibly reducing Bcl-G's anti-apoptotic activity. | ||||||
AS703026 | 1236699-92-5 | sc-364412 sc-364412A | 5 mg 10 mg | $80.00 $130.00 | ||
A-1155463 is a highly selective Bcl-xL inhibitor. By inhibiting Bcl-xL, it can modify the cellular balance of Bcl-2 family members, indirectly influencing Bcl-G-mediated apoptosis. | ||||||
Chelerythrine chloride | 3895-92-9 | sc-3547 sc-3547A | 5 mg 25 mg | $90.00 $317.00 | 17 | |
Chelerythrine, a benzophenanthridine alkaloid, has been reported to induce apoptosis through a mechanism that involves mitochondrial depolarization, potentially affecting Bcl-G's activity indirectly. | ||||||
HA14-1 | 65673-63-4 | sc-205911 sc-205911A | 5 mg 25 mg | $59.00 $209.00 | ||
HA14-1 interacts with Bcl-2 at the surface pocket involved in BH3 binding, potentially disrupting Bcl-G's ability to inhibit apoptosis by modulating the accessibility of its BH3 domain. | ||||||