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K-252b

PKC inhibitor



BML-EI234-0100	100 µg	162.00 USD

BML-EI234-1000	1 mg	670.00 USD
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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; K_i=0.147µM), cAMP- dependent protein kinase (PKA; K_i=0.09µM), protein kinase C (PKC; K_i=0.02µM), and cGMP-dependent protein kinase (PKG; K_i=0.1µM).

Product Details

Formula:	C₂₆H₁₉N₃O₅

MW:	453.5

CAS:	99570-78-2

Purity:	≥98% (HPLC)

Appearance:	White solid.

Solubility:	Soluble in DMSO (1mg/ml) or dimethyl formamide (1mg/ml).

Shipping:	Ambient

Long Term Storage:	+4°C

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.

Handling:	Protect from light.

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;