K-252b

BML-EI234

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PKC inhibitor

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).

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Product Details

Appearance	White solid.
CAS	99570-78-2
Couple Target	CaM kinase, MLCK, PKA, PKC, PKG
Couple Type	Inhibitor
Formula	C₂₆H₁₉N₃O₅
MW	453.5
Purity	≥98% (HPLC)
Solubility	Soluble in DMSO (1mg/ml) or dimethyl formamide (1mg/ml).

Handling & Storage

Use/Stability	As indicated on product label or CoA when stored as recommended. 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.
Long Term Storage	+4°C
Shipping	Ambient Temperature

Regulatory Status	RUO – Research Use Only

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
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
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

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K-252b

BML-EI234

Product Details

Handling & Storage

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