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Merck

EI8

Sigma-Aldrich

Leupeptin

lyophilized powder, protease inhibitor, Chemicon®

別名:

N-Acetyl-L-leucyl-L-leucyl-L-argininal, Ac-Leu-Leu-Arg-H, Acetyl-L-leucyl-L-leucylargininal, Leupeptin hemisulfate

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About This Item

UNSPSCコード:
51111800
eCl@ss:
32160405
NACRES:
NA.77

product name

Leupeptin,

メーカー/製品名

Chemicon®

品質水準

輸送温度

dry ice

詳細

Leupeptin is a water-soluble and cell-permeable organic compound. It is produced by various species of actinomycetes and several other fungal families.

アプリケーション

Leupeptin has been used as a protease inhibitor supplement in cell lysis buffer for sample preparation.

生物化学的/生理学的作用

Leupeptin serves as a lysosomal protease and calpain (serine- and cysteine-like protease) inhibitor. It may be used to reduce the cell death induced by excess calpain activation. Leupeptin confers significant protection against hair cell damage caused by gentamicin ototoxicity. In addition, it also impedes protein degradation in denervated rat muscles and muscles of mice with hereditary muscular dystrophy. Thus, leupeptin may be beneficial in hindering tissue atrophy.

物理的形状

Lyophilized.

保管および安定性

Maintain dry at -20ºC for up to 18 months after date of receipt. Store reconstituted product in aliquots at -20ºC for up to 6 months. Avoid repeated thaw freeze cycles.

法的情報

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

免責事項

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

保管分類コード

11 - Combustible Solids

WGK

WGK 3

引火点(°F)

Not applicable

引火点(℃)

Not applicable


適用法令

試験研究用途を考慮した関連法令を主に挙げております。化学物質以外については、一部の情報のみ提供しています。 製品を安全かつ合法的に使用することは、使用者の義務です。最新情報により修正される場合があります。WEBの反映には時間を要することがあるため、適宜SDSをご参照ください。

Jan Code

EI8:


試験成績書(COA)

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The structure and activity of leupeptins and related analogs.
K Maeda et al.
The Journal of antibiotics, 24(6), 402-404 (1971-06-01)
P Libby et al.
Science (New York, N.Y.), 199(4328), 534-536 (1978-02-03)
The protease inhibitor leupeptin decreases protein degradation in rat skeletal and cardiac muscle incubated in vitro, while protein synthesis remains unaltered. Leupeptin also lowers protein breakdown in denervated rat muscles and affected muscles from mice with hereditary muscular dystrophy. Leupeptin
Karen Maes et al.
American journal of respiratory and critical care medicine, 175(11), 1134-1138 (2007-03-24)
Controlled mechanical ventilation (CMV) has been shown to result in elevated diaphragmatic proteolysis and atrophy together with diaphragmatic contractile dysfunction. To test whether administration of leupeptin, an inhibitor of lysosomal proteases and calpain, concomitantly with 24 hours of CMV, would
Patrick J Lupardus et al.
Methods (San Diego, Calif.), 41(2), 222-231 (2006-12-27)
Our knowledge of cell cycle events such as DNA replication and mitosis has been advanced significantly through the use of Xenopus egg extracts as a model system. More recently, Xenopus extracts have been used to investigate the cellular mechanisms that
Erika Billinger et al.
FEBS open bio, 10(12), 2605-2615 (2020-10-06)
Leupeptin is a naturally occurring inhibitor of various proteases, in particular serine proteases. Following its discovery, the inhibitory properties of several other peptidyl argininals have been studied. The specificity of leupeptin is most likely due to the Leu-Leu-Argininal sequence, and

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