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Safety Information

SCP0109

Sigma-Aldrich

Cathepsin D Substrate

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Empirical Formula (Hill Notation):
C49H55N9O7
Molecular Weight:
882.02
UNSPSC Code:
12352202
NACRES:
NA.32

Assay

≥95% (HPLC)

form

lyophilized

composition

Peptide Content, ≥85%

storage condition

protect from light

storage temp.

−20°C

Amino Acid Sequence

Bz-Arg-Gly-Phe-Phe-Pro-4M2NA

General description

Cathepsin D Substrate is a peptide with Bz-Arg-Gly-Phe-Phe-Pro-4M2NA sequence.

Application

Cathepsin D Substrate has been used in cathepsin D enzymatic assays with Dictyostelium, midgut samples of beetles Stromatium fulvum (Villers) and of P. versicolora.

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

常规特殊物品

Certificates of Analysis (COA)

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Hong-Ye Wan et al.
Advanced science (Weinheim, Baden-Wurttemberg, Germany), 5(3), 1700585-1700585 (2018-03-30)
Targeting protein degradation is recognized as a valid approach to cancer therapy. The ubiquitin-proteasome system (UPS) and the autophagy-lysosome pathway are two major pathways for intracellular protein degradation. Proteasome inhibitors such as bortezomib are clinically approved for treating malignancies, but
Digestive proteolytic profile in Stromatium fulvum Villers (Coleoptera: Cerambycidae)
ZIBAEE A, et al.
Romanian Journal of Biochemistry, 51, 17-30 (2014)
Robert J Huber et al.
Cellular signalling, 58, 79-90 (2019-02-17)
Mutations in CLN3 cause a juvenile form of neuronal ceroid lipofuscinosis (NCL). This devastating neurological disorder, commonly known as Batten disease, is currently untreatable due to a lack of understanding of the physiological role of the protein. Recently, work in
Proteolytic activity in Plagiodera versicolora Laicharting (Coleoptera: Chrysomelidae): Characterization of digestive proteases and effect of host plants
Zibaee A and Hajizadeh J
Journal of Asia-Pacific Entomology, 16, 329-334 (2013)
Tonyia Eaves-Pyles et al.
PloS one, 6(9), e24869-e24869 (2011-09-29)
Bacteria release flagellin that elicits innate responses via Toll-like receptor 5 (TLR5). Here, we investigated the fate of apically administrated full length flagellin from virulent and avirulent bacteria, along with truncated recombinant flagellin proteins in intestinal epithelial cells and cellular

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