In vitro transcription of capped mRNA with modified nucleotides and Poly(A) tail
Tyramide Signal Amplification (TSA)
TSA (Tyramide Signal Amplification), used for signal amplification of ISH, IHC and IC etc.
Phos Binding Reagent Acrylamide
Separation of phosphorylated and non-phosphorylated proteins without phospho-specific antibody
Cell Counting Kit-8 (CCK-8)
A convenient and sensitive way for cell proliferation assay and cytotoxicity assay
SYBR Safe DNA Gel Stain
Safe and sensitive stain for visualization of DNA or RNA in agarose or acrylamide gels.
Protect the integrity of proteins from multiple proteases and phosphatases for different applications.
Description:IC50: 100 nm (antiproliferative IC50) 
The proteasome is a member of the growing N-terminal nucleophile (Ntn) hydrolase family, whose aminoterminal side chains act as nucleophiles and free amino groups as proton acceptors. Proteasome inhibitors have been increasingly used to help define the role of the proteasome in cell biology. Dihydroeponemycin labels the catalytic threonine residues of the immunoproteasome subunits LMP2 and LMP7 and the constitutive proteasome subunit X, while epoxomicin covalently modifies the N-terminal catalytic threonine residues of the constitutive proteasome (X and Z) and immunoproteasome (LMP7 and MECL1) subunits.
In vitro: Previoius study reports that dihydroeponemycin, an analogue of the antitumor and antiangiogenic natural product eponemycin, selectively targets the 20S proteasome. Dihydroeponemycin covalently modifies a subset of catalytic proteasomal subunits, binding preferentially to the IFN-g-inducible subunits LMP2 and LMP7. Moreover, the three major peptidolytic activities of the proteasome are inhibited by dihydroeponemycin at different rates. In addition, dihydroeponemycin-mediated proteasome inhibition induces a spindle-like cellular morphological change and apoptosis. These results validate the proteasome as a target for antitumor pharmacological intervention and are relevant for the design of novel chemotherapeutic strategies .
In vivo: Recent study in the mouse model of dihydrosterptomycin shows that hair cells are targeted because aminoglycosides enter outer hair cells through large mechanically gated channels in the mechanosensory hair boundles. The aminoglycoside molecules then block the channels through which they entered. When this occurs, the aminoglycoside goes through the channel and effectively traps itself in the hair cell .
Clinical trial: Dihydroeponemycin is currently in the preclinical development and non clinical trial is ongoing.
 Kim KB, Myung J, Sin N, Crews CM. Proteasome inhibition by the natural products epoxomicin and dihydroeponemycin: insights into specificity and potency. Bioorg Med Chem Lett. 1999;9(23):3335-40.
 Meng L, Kwok BH, Sin N, Crews CM. Eponemycin exerts its antitumor effect through the inhibition of proteasome function. Cancer Res. 1999;59(12):2798-801.
 Marcotti W, van Netten SM, Kros CJ. The aminoglycoside antibiotic dihydrostreptomycin rapidly enters mouse outer hair cells through the mechano-electrical transducer channels. J Physiol. 2005;567(Pt 2):505-21.
|Storage||Store at 2-8°C|
|Solubility||≥15.6mg/mL in DMSO|
可溶于DMSO。若配制更高浓度的溶液，一般步骤如下：请将试管置于37 °C加热10分钟和/或将其置于超声波浴中震荡一段时间。原液于-20 °C可放置数月。
. Meng L, Kwok BH, Sin N, Crews CM. Eponemycin exerts its antitumor effect through the inhibition of proteasome function. Cancer Res. 1999;59(12):2798-801.