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In vitro transcription of capped mRNA with modified nucleotides and Poly(A) tail
TSA (Tyramide Signal Amplification), used for signal amplification of ISH, IHC and IC etc.
Separation of phosphorylated and non-phosphorylated proteins without phospho-specific antibody
A convenient and sensitive way for cell proliferation assay and cytotoxicity assay
Protect the integrity of proteins from multiple proteases and phosphatases for different applications.
Berninamycin A is a macrocyclic thiopeptide antibiotic first isolated from S. bernensis [1]. Thiopeptides are sulfur containing highly modified macrocyclic antibiotics with a central pyridine/tetrapyridine/dehydropiperidine ring with up to three thiazole substituents on positions 2, 3 and 6. Thiazole antibiotics thiostrepton behaves as proteasome inhibitor in mammalian tumor cells. Berninamycin showed no proteasome inhibitory activity [2]. It has been reported that the action mode of berninamycin on bacterial protein synthesis was related to that of a dissimilar compound thiostrepton. The antibiotics could bind to the complex of 23S RNA with protein L11 and both affect multiple functions of the ribosomal A site [3]. Berninamycin A was involved in inducing the transcriptional activator TipA in Streptomyces [4].
References:[1] Lau R C M, Rinehart K L. Berninamycins B, C, and D, minor metabolites from Streptomyces bernensis[J]. The Journal of antibiotics, 1994, 47(12): 1466-1472.[2] Pandit B, Bhat U G, Gartel A L. Proteasome inhibitory activity of thiazole antibiotics[J]. Cancer biology & therapy, 2011, 11(1): 43-47.[3] J. Thompson, E. Cundliffe and M. J. R. Stark. The mode of action of berninamycin and mechanism of resistance in the producing organism, Streptomyces bernensis. J.Gen.Microbiol. 128(4), 875-884 (1982). [4]. M. L. Chiu, M. Folcher, T. Katoh, et al. Broad spectrum thiopeptide recognition specificity of the Streptomyces lividans TipAL protein and its role in regulating gene expression. The Journal of Biological Chemisty 274(29), 20578-20586 (1999).