C19orf21 Activators
MISP activators primarily influence the intricate cellular machinery associated with actin dynamics and mitotic spindle positioning. Given MISP's vital role as an actin-bundling protein, any alterations or stresses to actin structure and dynamics can intensify the significance of MISP within the cell. Chemicals such as Latrunculin A, Cytochalasin D, and Jasplakinolide distinctly modulate actin polymerization and filament stability. By either hindering polymerization or stabilizing the filaments, these chemicals place a compensatory demand on the cell, highlighting the role of actin-bundling proteins like MISP. As the balance of actin dynamics is perturbed, MISP's function becomes increasingly crucial in determining proper cell morphology and ensuring accurate mitotic spindle orientation.
On the other hand, chemicals such as Nocodazole, Vinblastine, Colchicine, and Taxol target the microtubule network, the core structure of mitotic spindles. By inhibiting microtubule polymerization, stabilizing microtubules, or affecting spindle formation, these chemicals shed light on the intricate orchestration of mitotic progression and spindle dynamics. As these dynamics are modulated, proteins like MISP, responsible for spindle positioning, become vital for the successful completion of mitosis. Moreover, chemicals like Roscovitine, which influence cell cycle progression, further underscore the importance of correct spindle positioning, amplifying the essential function of MISP in the cellular division process.
SEE ALSO...
Items 1 to 10 of 11 total
Display:
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Latrunculin A, Latrunculia magnifica | 76343-93-6 | sc-202691 sc-202691B | 100 µg 500 µg | $265.00 $815.00 | 36 | |
Latrunculin A binds actin monomers, preventing their polymerization. With reduced actin polymerization, cells can compensate by modulating actin-bundling proteins, potentially highlighting MISP's role in determining cell morphology. | ||||||
Cytochalasin D | 22144-77-0 | sc-201442 sc-201442A | 1 mg 5 mg | $165.00 $486.00 | 64 | |
Cytochalasin D binds to actin filament ends, blocking their elongation. This alteration in actin dynamics can enhance the requirement for actin-bundling proteins like MISP for proper cell morphology and spindle positioning. | ||||||
Jasplakinolide | 102396-24-7 | sc-202191 sc-202191A | 50 µg 100 µg | $184.00 $305.00 | 59 | |
Jasplakinolide promotes actin polymerization and stabilizes actin filaments. Enhanced actin dynamics may indirectly increase the need for actin-bundling proteins such as MISP, which in turn can help maintain proper mitotic spindle positioning. | ||||||
Nocodazole | 31430-18-9 | sc-3518B sc-3518 sc-3518C sc-3518A | 5 mg 10 mg 25 mg 50 mg | $59.00 $85.00 $143.00 $247.00 | 38 | |
Nocodazole disrupts microtubule dynamics, influencing mitotic spindle formation. Disturbance in spindle assembly can emphasize the importance of MISP in ensuring proper spindle positioning and orientation during mitosis. | ||||||
Vinblastine | 865-21-4 | sc-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 | |
Vinblastine binds tubulin, inhibiting microtubule polymerization. By affecting spindle dynamics, the role of MISP in positioning the mitotic spindle may become increasingly vital for cellular division processes. | ||||||
Colchicine | 64-86-8 | sc-203005 sc-203005A sc-203005B sc-203005C sc-203005D sc-203005E | 1 g 5 g 50 g 100 g 500 g 1 kg | $100.00 $321.00 $2289.00 $4484.00 $18207.00 $34749.00 | 3 | |
Colchicine binds tubulin, inhibiting its polymerization and affecting mitotic spindle formation. This emphasizes the importance of proteins like MISP that ensure proper spindle orientation and positioning during cell division. | ||||||
Taxol | 33069-62-4 | sc-201439D sc-201439 sc-201439A sc-201439E sc-201439B sc-201439C | 1 mg 5 mg 25 mg 100 mg 250 mg 1 g | $41.00 $74.00 $221.00 $247.00 $738.00 $1220.00 | 39 | |
Taxol stabilizes microtubules, preventing their depolymerization. Increased microtubule stability can enhance the role of MISP in positioning the mitotic spindle properly, especially during the metaphase-anaphase transition of mitosis. | ||||||
S-Trityl-L-cysteine | 2799-07-7 | sc-202799 sc-202799A | 1 g 5 g | $32.00 $66.00 | 6 | |
An inhibitor of mitotic kinesin Eg5, it affects spindle pole separation. Such disturbances in spindle dynamics can heighten the importance of proteins like MISP in maintaining proper spindle positioning during mitotic progression. | ||||||
Monastrol | 254753-54-3 | sc-202710 sc-202710A | 1 mg 5 mg | $120.00 $233.00 | 10 | |
Monastrol is a specific inhibitor of the mitotic kinesin Eg5, affecting spindle formation. As spindle dynamics are altered, the regulatory role of MISP in ensuring proper spindle positioning can be magnified. | ||||||
Azathioprine | 446-86-6 | sc-210853D sc-210853 sc-210853A sc-210853B sc-210853C | 500 mg 1 g 2 g 5 g 10 g | $203.00 $176.00 $349.00 $505.00 $704.00 | 1 | |
Azathioprine affects purine synthesis, influencing DNA replication and cell cycle progression. By altering cell cycle dynamics, the requirement for proteins like MISP, ensuring spindle orientation during mitosis, can be emphasized. | ||||||