Replaces Prod. #: ALX-260-014
Membrane permeable inhibitor of calpain I and II, cathepsin L and cathepsin K (IC50=0.11 nM). Promotes neurite elongation in differentiating PC12 cells. Prevents Ca2+-ionophore induced degradation of actin binding protein and P235 in platelets. Inhibits myosin light chain phosphorylation in platelets stimulated by collagen, ionomycin (Prod. No. ALX-450-006) or thrombin. Inhibits LPS induced iNOS transcription and NF-κB activation, possibly via proteasome inhibition.
Product Details
Alternative Name: | Z-Leu-norleucinal, N-Benzyloxycarbonyl-L-leucyl-norleucinal |
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Formula: | C20H30N2O4 |
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MW: | 362.5 |
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CAS: | 117591-20-5 |
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Purity: | ≥98% (HPLC) |
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Appearance: | White to off-white powder. |
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Solubility: | Soluble in DMSO (25mg/ml), 100% ethanol (25mg/ml or dimethyl formamide (5mg/ml). |
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Shipping: | Blue Ice |
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Long Term Storage: | -20°C |
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Use/Stability: | Stable for up to 1 year when stored at -20°C. Stock solutions are stable for up to 3 months at -20°C. |
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Handling: | Protect from light and moisture. Packaged under inert gas. After reconstitution, prepare aliquots and store at -20°C. |
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Technical Info/Product Notes: | Concentrations for intact cells: 30µM (platelets), 10µM (myoblast cells)
Note: Product is not sterile. |
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Regulatory Status: | RUO - Research Use Only |
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Product Literature References
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9, 4606 (2019),
Abstract;
Full Text
The Coagulation and Immune Systems Are Directly Linked through the Activation of Interleukin-1α by Thrombin: L.C. Burzynski, et al.; Immunity
50, 1033 (2019),
Abstract;
Effect of SI-591, a new class of cathepsin K inhibitor with peptidomimetic structure, on bone metabolism in vitro and in vivo: T. Fujii, et al.; Bone
81, 427 (2015),
Application(s): Human and Rat Cathepsin K assays,
Abstract;
Human normal bronchial epithelial cells: a novel in vitro cell model for toxicity evaluati: W. Feng, et al.; PLoS One
10, e0123520 (2015),
Application(s): Cell Culture,
Abstract;
Full Text
Membrane-Permeable Calpain Inhibitors Promote Rat Oral Mucosal Epithelial Cell Proliferation by Inhibiting IL-1α Signaling: M. Kondo, et al. ; PLoS One
10, e0134240 (2015),
Application(s): Cell culture,
Abstract;
Full Text
Exploration of the P1 SAR of aldehyde cathepsin K inhibitors: J.G. Catalano, et al.; Bioorg. Med. Chem. Lett.
14, 275 (2004),
Abstract;
Inhibitors of the proteasome pathway interfere with induction of nitric oxide synthase in macrophages by blocking activation of transcription factor NF-kappa B: J.M. Griscavage, et al.; PNAS
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Abstract;
Full Text
Endogenous cleavage of phospholipase C-beta 3 by agonist-induced activation of calpain in human platelets: Y. Banno, et al.; J. Biol. Chem.
270, 4318 (1995),
Abstract;
Calpeptin, a calpain inhibitor, promotes neurite elongation in differentiating PC12 cells: M. Pinter, et al.; Neurosci. Lett.
170, 91 (1994),
Abstract;
Comparison of the effect of calpain inhibitors on two extralysosomal proteinases: the multicatalytic proteinase complex and m-calpain: M.E. Figueiredo-Pereira, et al.; J. Neurochem.
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Abstract;
Role of intracellular proteases in differentiation of L6 myoblast cells: C. Ebisui, et al.; Biochem. Mol. Biol. Int.
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Abstract;
Specificity of calcium-activated neutral proteinase (CANP) inhibitors for human mu CANP and mCANP: K. Saito and R.A. Nixon; Neurochem. Res.
18, 231 (1993),
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Cell-penetrating inhibitors of calpain: S. Mehdi; TIBS
16, 150 (1991),
Abstract;
Inhibitory effect of di- and tripeptidyl aldehydes on calpains and cathepsins: T. Sasaki, et al.; J. Enz. Inhib.
3, 195 (1990),
Abstract;
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