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Merck

EI8

Leupeptin

lyophilized powder, protease inhibitor, Chemicon®

Synonym(s):

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 Code:
51111800
NACRES:
NA.77
eCl@ss:
32160405

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Product Name

Leupeptin,

manufacturer/tradename

Chemicon®

shipped in

dry ice

Quality Level

100

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This Item
L579362070L8511
Leupeptin

Sigma-Aldrich

EI8

Leupeptin

Leupeptin BioUltra, microbial, ≥95% (HPLC)

Sigma-Aldrich

L5793

Leupeptin

Leupeptin >4000 U/mg

Sigma-Aldrich

62070

Leupeptin

Leupeptin synthetic, ≥85% (HPLC)

Sigma-Aldrich

L8511

Leupeptin

manufacturer/tradename

Chemicon®

manufacturer/tradename

-

manufacturer/tradename

-

manufacturer/tradename

-

Quality Level

100

Quality Level

200

Quality Level

100

Quality Level

200

shipped in

dry ice

shipped in

-

shipped in

-

shipped in

-

Application

Leupeptin has been used as a protease inhibitor supplement in cell lysis buffer for sample preparation.[1][2][3]

Biochem/physiol Actions

Leupeptin serves as a lysosomal protease and calpain (serine- and cysteine-like protease) inhibitor.[4][5] 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.[5] 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.[6]

Disclaimer

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.

General description

Leupeptin is a water-soluble and cell-permeable organic compound.[5] It is produced by various species of actinomycetes and several other fungal families.[7]

Physical form

Lyophilized.

Preparation Note

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.

Legal Information

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

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Dalian Ding et al.
Hearing research, 164(1-2), 115-126 (2002-04-13)
Calpains, a family of calcium-activated proteases that breakdown proteins, kinases, phosphatases and transcription factors, can promote cell death. Since leupeptin, a calpain inhibitor, protected against hair cell loss from acoustic overstimulation, we hypothesized that it might protect cochlear and vestibular
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
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
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
View All Related Papers

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