|Related Categories||Bioactive Small Molecules, Biochemicals and Reagents, Cell Biology, Cell Signaling and Neuroscience, Core Bioreagents,|
|mp||233 °C (dec.)(lit.)|
Can be used in conjunction with E64-d and Leupeptin A to inhibit the degradation of autophagic cargo inside autophagosomes. For this application, the working concentration is typically between 1-10 μM.
Pepstatin can be dissolved at 1 mg/ml in 10% (v/v) acetic acid in methanol (9:1 methanol:acetic acid). The inclusion of acetic acid may be necessary to dissolve this peptide in methanol or DMSO. It has been dissolved at 1 to 2 mg/ml in ethanol, but heat may be required for complete dissolution. Solutions of Pepstatin A can be heated as high as 60 °C without any decomposition of the peptide.
Stock solutions at 1 mg/ml are stable at least a week at 4 °C. A 1 mM solution in methanol or DMSO is stable for months at -20 °C. If solutions become darker yellow, the reagent is hydrolyzing.
A working concentration of 1 μM is stable for at least one day at room temperature.
Pepstatin A is an inhibitor of acid proteases (aspartyl peptidases). It forms a 1:1 complex with proteases such as pepsin, renin, cathepsin D, bovine chymosin, and protease B (Aspergillus niger). The inhibitor is highly selective and does not inhibit thiol proteases, neutral proteases, or serine proteases. Solubilized γ-secretase and retroviral protease are also inhibited by Pepstatin A. It has been used to characterize proteases from several sources.
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Cellular expression and antimicrobial function of a phylogenetically conserved novel histone 1x-like protein on mouse cells: a potential new class of pattern recognition receptor. Evans, D.L., et al. J. Neurochem. 86, 133-41, (2009)
Cardiac Oxytocin Receptor Blockade Stimulates Adverse Cardiac Remodeling In Ovariectomized Spontaneously Hypertensive Rats. Jankowski, M., et al. Am. J. Physiol. Heart Circ. Physiol. 299, H265-74, (2010)
RaPID: An Aptamer-based MRNA Affinity Purification Technique For The Identification Of RNA And Protein Factors Present In Ribonucleoprotein Complexes. Slobodin, B., and Gerst, J.E. Methods Mol. Biol. 714, 387-406, (2011)
Preimplantation embryo development in the mouse requires the latency of TRP53 expression, which is induced by a ligand-activated PI3 kinase/AKT/MDM2-mediated signaling pathway. X.L. Jin et al Biol. Reprod. 80, 286-94, (2008)
FT-IR 2 (1), 1336:A / RegBook 1 (1), 921:E / Sax 6, 2143 / Structure Index 1, 143:D:2
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