Ugrás a tartalomra
Merck
Összes fotó(1)

Fontos dokumentumok

208719

Sigma-Aldrich

ALLN

≥95% (HPLC), solid, calpain inhibitor, Calbiochem®

Szinonimák:

ALLN, LLNL, MG 101, Calpain Inhibitor I, Proteasome Inhibitor V

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

Tapasztalati képlet (Hill-képlet):
C20H37N3O4
CAS-szám:
Molekulatömeg:
383.53
MDL-szám:
UNSPSC kód:
12352200
NACRES:
NA.77

Terméknév

ALLN, Cell-permeable inhibitor of calpain I (Ki = 190 nM), calpain II (Ki = 220 nM), cathepsin B (Ki = 150 nM), and cathepsin L (Ki = 500 pM).

Minőségi szint

Teszt

≥95% (HPLC)

Forma

solid

gyártó/kereskedő neve

Calbiochem®

tárolási körülmény

OK to freeze

szín

white to off-white

oldhatóság

DMSO: 10 mg/mL
ethanol: 5 mg/mL

kiszállítva

ambient

tárolási hőmérséklet

2-8°C

SMILES string

N([C@@H](CC(C)C)C(=O)N[C@@H](CCCC)C=O)C(=O)[C@@H](NC(=O)C)CC(C)C

InChI

1S/C20H37N3O4/c1-7-8-9-16(12-24)22-19(26)18(11-14(4)5)23-20(27)17(10-13(2)3)21-15(6)25/h12-14,16-18H,7-11H2,1-6H3,(H,21,25)(H,22,26)(H,23,27)/t16-,17-,18-/m0/s1

Nemzetközi kémiai azonosító kulcs

FMYKJLXRRQTBOR-BZSNNMDCSA-N

Általános leírás

Cell-permeable inhibitor of calpain I (Ki = 190 nM), calpain II (Ki = 220 nM), cathepsin B (Ki = 150 nM), and cathepsin L (Ki = 500 pM). Inhibits neutral cysteine proteases and the proteasome (Ki = 6 µM). Modulates the processing of the β-amyloid precursor protein (βAPP) to β-amyloid (Aβ). Protects against neuronal damage caused by hypoxia and ischemia. Inhibits apoptosis in thymocytes and metamyelocytes. Also inhibits reovirus-induced apoptosis in L929 cells. Inhibits the proteolysis of IκB-α and IκB-β by the ubiquitin-proteasome complex. Inhibits cell cycle progression at G1/S and metaphase/anaphase in CHO cells by inhibiting cyclin B degradation. Also prevents nitric oxide production by activated macrophages by interfering with transcription of the inducible nitric oxide synthase gene. A 10 mM (5 mg/1.30 ml) solution of ALLN (Cat. No. 208750) in DMSO is also available.
Inhibitor of calpain I (Ki = 190 nM), calpain II (Ki = 220 nM), cathepsin B (Ki = 150 nM), and cathepsin L (Ki = 500 pM). Inhibits neutral cysteine proteases and proteasome (Ki = 6 µM). Protects against neuronal damage caused by hypoxia and ischemia. Inhibits apoptosis in thymocytes and metamyelocytes. Inhibits cell cycle progression at the G1/S border and metaphase/anaphase in CHO cells by inhibiting cyclin B degradation. Also prevents nitric oxide production by activated macrophages by interfering with transcription of the inducible nitric oxide synthase gene. Inhibits the proteolysis of IκBα and IκBβ by the ubiquitin-proteasome complex.

Biokémiai/fiziológiai hatások

Cell permeable: yes
Primary Target
Calpain-1
Product does not compete with ATP.
Reversible: no
Target Ki: 190 nM, 220 nM, 150 nM, 500 pM, against calpain I, calpain II, cathepsin B, and cathepsin L, respectively

Figyelmeztetés

Toxicity: Standard Handling (A)

Szekvencia

N-Acetyl-Leu-Leu-Nle-CHO

Feloldás

Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.

Egyéb megjegyzések

Debiasi, R.L., et al. 1999. J. Virol. 73, 695.
Zhang, L., et al. 1999. J. Biol. Chem.274, 8966.
Milligan, S.A., et al. 1996. Arch. Biochem. Biophys. 335, 388.
Griscavage, J.M., et al. 1995. Biochem. Biophys. Res. Commun. 215, 721.
Squier, M.K., et al. 1994. J. Cell Physiol.159, 229.
Rami, J., and Kreiglstein, J. 1993. Brain Res.609, 67.
Sherwood, S.W., et al. 1993. Proc. Natl. Acad. Sci.USA90, 3353.
Vinitsky, A., et al. 1992. Biochemistry31, 9421.
Sasaki, T., et al. 1990. J. Enzyme Inhib. 3, 195.

Jogi információk

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Tárolási osztály kódja

11 - Combustible Solids

WGK

WGK 3

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable


Analitikai tanúsítványok (COA)

Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.

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Az Ön által nemrégiben megvásárolt termékekre vonatkozó dokumentumokat a Dokumentumtárban találja.

Dokumentumtár megtekintése

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Methods in molecular biology (Clifton, N.J.), 301, 293-303 (2005-05-27)
Components of the ubiquitin-proteasome system function on the surface of the endoplasmic reticulum (ER) to select misfolded proteins for degradation. Herein we describe methods that allow for the study of the pathway for proteasomal degradation of the cystic fibrosis transmembrane
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