SCP0063
Calpastatin Peptide
≥95% (HPLC), Ac 184-210
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About This Item
Formule empirique (notation de Hill):
C142H230N36O44S1
Poids moléculaire :
3177.63
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.32
Produits recommandés
product name
Calpastatin Peptide Ac 184-210, ≥95% (HPLC)
Pureté
≥95% (HPLC)
Forme
lyophilized
Composition
Peptide Content, ≥75%
Conditions de stockage
protect from light
Température de stockage
−20°C
Amino Acid Sequence
Ac-Asp-Pro-Met-Ser-Ser-Thr-Tyr-Ile-Glu-Glu-Leu-Gly-Lys-Arg-Glu-Val-Thr-Ile-Pro-Pro-Lys-Tyr-Arg-Glu-Leu-Leu-Ala-NH2
Application
Calpastatin Peptide Ac 184-210 has been used as the endogenous calpain inhibitor to study its effects on myristoylated alanine-rich C kinase substrate (MARCKS) cleavage in mouse kidney cells. It has also been used as a calpain inhibitor to examine its effects on the formation of DNA-platinum adducts by cisplatin (CDDP) in neuronal cells.
Actions biochimiques/physiologiques
Calpastatin, a component of the calpain/calpastatin system, is a calpain (calcium-dependent cysteine protease) inhibitor. The calpain/calpastatin system is involved in numerous membrane fusion events, such as neural vesicle exocytosis and platelet and red-cell aggregation.
Calpastatin, located in the cytosol, is involved in selective protein cleavage in response to calcium signaling.
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
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Calpain in the cleavage of alpha-synuclein and the pathogenesis of Parkinson's disease
Shams R, et al.
Progress in Molecular Biology and Translational Science, 167, 107-124 (2019)
Aysel Cetinkaya-Fisgin et al.
Scientific reports, 10(1), 21889-21889 (2020-12-16)
Cisplatin is a commonly used chemotherapy agent with significant dose-limiting neurotoxicity resulting in peripheral neuropathy. Although it is postulated that formation of DNA-platinum adducts is responsible for both its cytotoxicity in cancer cells and side effects in neurons, downstream mechanisms
Darrice S Montgomery et al.
American journal of physiology. Cell physiology, 313(1), C42-C53 (2017-05-05)
We previously demonstrated a role for the myristoylated alanine-rich C kinase substrate (MARCKS) to serve as an adaptor protein in the anionic phospholipid phosphate-dependent regulation of the epithelial sodium channel (ENaC). Both MARCKS and ENaC are regulated by proteolysis. Calpains
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