Replaces Prod. #: ALX-380-029
General, cell permeable protein kinase inhibitor. Acts by binding to the ATP binding domain of the kinase. Potent inhibitor of Ca2+/calmodulin kinase II. Inhibits myosin light chain kinase (MLCK; Ki=0.147µM), cAMP- dependent protein kinase (PKA; Ki=0.09µM), protein kinase C (PKC; Ki=0.02µM), and cGMP-dependent protein kinase (PKG; Ki=0.1µM).
Product Details
| Formula: | C26H19N3O5 |
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| MW: | 453.5 |
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| CAS: | 99570-78-2 |
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| Purity: | ≥98% (HPLC) |
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| Appearance: | White solid. |
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| Solubility: | Soluble in DMSO (1mg/ml) or dimethyl formamide (1mg/ml). |
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| Shipping: | Ambient Temperature |
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| Long Term Storage: | +4°C |
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| Use/Stability: | Stable for at least 1 year after receipt when stored, as supplied, at 0-4°C. Stock solutions are stable for up to 3 months at -20°C. |
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| Handling: | Protect from light. |
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| Regulatory Status: | RUO - Research Use Only |
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Product Literature References
Staurosporine, K-252a, and K-252b stabilize calcium homeostasis and promote survival of CNS neurons in the absence of glucose: B. Cheng, et al.; J. Neurochem.
62, 1319 (1994),
Abstract;
Ecto-protein kinase and surface protein phosphorylation in PC12 cells: interactions with nerve growth factor: Z. Pawlowska, et al.; J. Neurochem.
60, 678 (1993),
Abstract;
K-252 compounds: modulators of neurotrophin signal transduction: B. Knusel & F. Hefti; J. Neurochem.
59, 1987 (1992),
Abstract;
K-252b selectively potentiates cellular actions and trk tyrosine phosphorylation mediated by neurotrophin-3: B. Knusel, et al.; J. Neurochem.
59, 715 (1992),
Abstract;
Potent and preferential inhibition of Ca2+/calmodulin-dependent protein kinase II by K252a and its derivative, KT5926: Y. Hashimoto, et al.; BBRC
181, 423 (1991),
Abstract;
Staurosporine, K-252 and UCN-01: potent but nonspecific inhibitors of protein kinases: U.T. Rüegg & G.M. Burgess; TIPS
10, 218 (1989), (Review),
Abstract;
K-252 compounds, novel and potent inhibitors of protein kinase C and cyclic nucleotide-dependent protein kinases: H. Kase, et al.; Biochem. Biophys. Res. Commun.
142, 436 (1987),
Abstract;
K-252b, c and d, potent inhibitors of protein kinase C from microbial origin: S. Nakanishi, et al.; J. Antibiot. (Tokyo)
39, 1066 (1986),
Abstract;
The structures of the novel protein kinase C inhibitors K-252a, b, c and d: T. Yasuzawa, et al.; J. Antibiot.
39, 1072 (1986),
Abstract;
