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MedChemExpressModel Manumycin A - 52665-74-4

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Manumycin A is a polyketide antibiotic and an inhibitor of thioredoxin reductase 1 (TrxR-1). Manumycin A can inhibit the growth of breast cancer cells and exert its anti-tumor activity through LC3. Manumycin A can downregulate the release of pro-inflammatory cytokines in human monocytes stimulated by TNF α, and has potential anti-inflammatory activity. Manumycin A can inhibit the Ras/Raf/ERK1/2 signaling and hnRNP H1 in castration resistant prostate cancer cells to suppress exosome biogenesis and secretion[1][3][4].
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Manumycin A

MCE China:Manumycin A

Brand:MedChemExpress (MCE)

Cat. No.HY-N6796

CAS:52665-74-4

Purity:99.27%

Storage:-20°C, sealed storage, away from moisture *In solvent : -80°C, 6 months; -20°C, 1 month (sealed storage, away from moisture)

Shipping:Room temperature in continental US; may vary elsewhere.

Description:Manumycin A is a polyketide antibiotic and an inhibitor of thioredoxin reductase 1 (TrxR-1). Manumycin A can inhibit the growth of breast cancer cells and exert its anti-tumor activity through LC3. Manumycin A can downregulate the release of pro-inflammatory cytokines in human monocytes stimulated by TNF α, and has potential anti-inflammatory activity. Manumycin A can inhibit the Ras/Raf/ERK1/2 signaling and hnRNP H1 in castration resistant prostate cancer cells to suppress exosome biogenesis and secretion.

In Vitro:Manumycin A (0.25-5 μM, 24 h) downregulates the release of pro-inflammatory cytokines in human monocytes stimulated by TNF α, thus possessing potential anti-inflammatory properties[1]. Manumycin A (0-25 μM, 72 h) can enhance its inhibitory effect on lung cancer cells after inhibiting HSF1 mediated heat shock response (HSR)[2]. Manumycin A (5 μM, 72 h) inhibits the growth of triple negative breast cancer cells through LC3 mediated cytoplasmic vacuolation death[3]. Manumycin A (250 nM, 48 h) inhibits exosome biogenesis and secretion by targeting Ras/Raf/ERK1/2 signaling and hnRNP H1 in castration resistant prostate cancer cells[4].

In Vivo:Manumycin A (5 mg/kg; once every two days; 2 weeks; i.p.) has anti-tumor effect in triple negative breast cancer mice[3]. Manumycin A (3 μg; once; i.m.) can correct abnormal splicing of Clcn1 in type 1 myotonic dystrophy (DM1) mice[5].

IC50 & Target:TrxR-1[1], Ras[4] In Vitro Manumycin A (0.25-5 μM, 24 h) downregulates the release of pro-inflammatory cytokines in human monocytes stimulated by TNF α, thus possessing potential anti-inflammatory properties[1]. Manumycin A (0-25 μM, 72 h) can enhance its inhibitory effect on lung cancer cells after inhibiting HSF1 mediated heat shock response (HSR)[2]. Manumycin A (5 μM, 72 h) inhibits the growth of triple negative breast cancer cells through LC3 mediated cytoplasmic vacuolation death[3]. Manumycin A (250 nM, 48 h) inhibits exosome biogenesis and secretion by targeting Ras/Raf/ERK1/2 signaling and hnRNP H1 in castration resistant prostate cancer cells[4]. MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only. 0 --> Manumycin A Related Antibodies Real Time qPCR[1]. Cell Line: Human monocytic leukemia cells THP-1

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References:

[1]. Cecrdlova E, et al. Manumycin A downregulates release of proinflammatory cytokines from TNF alpha stimulated human monocytes. Immunol Lett. 2016 Jan;169:8-14.  [Content Brief]

[2]. Sojka DR, et al. Inhibition of the Heat Shock Protein A (HSPA) Family Potentiates the Anticancer Effects of Manumycin A. Cells. 2021 Jun 7;10(6):1418.  [Content Brief]

[3]. Singha PK, et al. Manumycin A inhibits triple-negative breast cancer growth through LC3-mediated cytoplasmic vacuolation death. Cell Death Dis. 2013 Jan 17;4(1):e457.

[4]. Datta A, et al. Manumycin A suppresses exosome biogenesis and secretion via targeted inhibition of Ras/Raf/ERK1/2 signaling and hnRNP H1 in castration-resistant prostate cancer cells. Cancer Lett. 2017 Nov 1;408:73-81.  [Content Brief]

[5]. Oana K, et al. Manumycin A corrects aberrant splicing of Clcn1 in myotonic dystrophy type 1 (DM1) mice. Sci Rep. 2013;3:2142.  [Content Brief]

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