Ascomycin (11011-38-4) is an analog of FK-506 (Cat.# 10-1103). Potent immunosuppressant1. Binds to FKBP122 and inhibits calcineurin and NFAT. Ascomycin displays anti-inflammatory effects in skin diseases3. Cell permeable and active in vivo.
White powder, soluble in organic solvents such as methanol, ethanol, DMSO, etc., derived from biological fermentation.
A potent immunosuppressive agent and could be used as a potential therapeutic agent for autoimmune diseases.
An ethyl analog of FK506 with similar immunosuppressant properties. Acts by binding to immunophilins. Inhibits the synthesis of Th-1 and Th-2 type cytokines in target cells.
Product does not compete with ATP.
This antifungal antibiotic (FW = 792.02 g/mol; CAS 104987-12-4;
Solubility: 50 mM in DMSO), also known as FK520, isolated from
Streptomyces hygroscopicus, is also a powerful immunosuppressant. Note
that ascomycin is a structural analogue of tacrolimus (or FK506) and, as
such, operates by a similar mechanism of action (See Tacrolimus).
Ascomycin inhibits allogenic T-lymphocyte proliferation and calcineurin
phosphatase activity.
Ascomycin is a 23-membered macrolide lactone produced from the fermentation of Streptomyces hygroscopicus. A natural analogue of FK506, Ascomycin has the ability to bind to FK506-binding protein 12, inhibiting calcineurin phosphatase activity, and disrupting the activation of nuclear factor of activated T cells and other various substrates. Primarily described as an antifungal antibiotic, Ascomycin has shown to be a potent immunosuppressant used to prevent the rejection of organ transplants and skin allografts. Ascomycin displays powerful antimalarial properties independent of its immunosuppressive mechanisms of action.
[1] H HATANAKA. FR-900520 and FR-900523, novel immunosuppressants isolated from a Streptomyces. II. Fermentation, isolation and physico-chemical and biological characteristics.[J]. Journal of Antibiotics, 1988, 41 11: 1592-1601. DOI:
10.7164/antibiotics.41.1592[2] A. M. PETROS. NMR studies of an FK-506 analog [U-13C]ascomycin, bound to FKBP: conformation and regions of ascomycin involved in binding[J]. Journal of Medicinal Chemistry, 1991, 34 9: 2925-2928. DOI:
10.1021/jm00113a037[3] KARL W. MOLLISON. A Macrolactam Inhibitor of T Helper Type 1 and T Helper Type 2 Cytokine Biosynthesis for Topical Treatment of Inflammatory Skin Diseases1[J]. Journal of Investigative Dermatology, 1999, 112 5: Pages 729-738. DOI:
10.1046/j.1523-1747.1999.00567.x
