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208902

Sigma-Aldrich

Calpastatin Peptide

A 27-amino acid, cell-permeable peptide encoded by exon 1B of human calpastatin that acts as a potent inhibitor of calpain I and calpain II (IC₅₀ = 20 nM for purified rabbit calpain II).

Synonyme(s) :

Calpastatin Peptide, CS Peptide

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About This Item

Formule empirique (notation de Hill):
C142H230N36O44S
Poids moléculaire :
3177.63
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.77

Niveau de qualité

Pureté

≥95% (HPLC)

Forme

lyophilized solid

Fabricant/nom de marque

Calbiochem®

Conditions de stockage

OK to freeze
desiccated (hygroscopic)

Couleur

white

Solubilité

1% acetic acid: 1 mg/mL
water: 1 mg/mL

Conditions d'expédition

ambient

Température de stockage

−20°C

Description générale

A 27-amino acid, cell-permeable peptide encoded by exon 1B of human calpastatin that acts as a potent inhibitor of calpain I and calpain II (IC50 = 20 nM for purified rabbit calpain II). Does not inhibit either papain or trypsin. Blocks the down-regulation of protein kinase Cε (PKCε) in rat pituitary GH4C1 cells stimulated by thyrotropin-releasing hormone (TRH).
A 27-amino acid, peptide encoded by exon 1B of human calpastatin that acts as a cell-permeable and potent inhibitor of calpain I and calpain II (IC50 = 20 nM for purified rabbit calpain II). Does not inhibit either papain or trypsin. Blocks the down-regulation of protein kinase Cε (PKCε) in rat pituitary GH4C1 cells stimulated by thyrotropin-releasing hormone (TRH).

Actions biochimiques/physiologiques

Cell permeable: yes
Primary Target
calpain 2
Product does not compete with ATP.
Reversible: no
Target IC50: 20 nM against calpain II

Avertissement

Toxicity: Standard Handling (A)

Séquence

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

Forme physique

Supplied as a trifluoroacetate salt.

Reconstitution

Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.

Autres remarques

Eto, A., et al. 1995. J. Biol. Chem. 270, 25115.
Kawasaki, J., et al. 1989. J. Biochem. 106, 274.
Maki, M., et al. 1989. J. Biol. Chem. 264, 18866.

Informations légales

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

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Chanporn Chaosap et al.
Animal bioscience, 34(9), 1514-1524 (2021-04-27)
This study investigated the meat quality characteristics, endogenous proteolytic enzymes, collagen content, and myosin heavy chain (MyHC) isoforms of different muscles of Thai native cattle (TNC). Infraspinatus (IF), Longissimus thoracis (LT), and Supraspinatus (SS) muscles were obtained from two TNC
Xianliang Zeng et al.
Oncology letters, 21(2), 124-124 (2021-02-09)
Cancer cachexia is a life-threatening syndrome characterized by muscle atrophy. Cancer cachectic muscle atrophy (CCMA) is associated with mitochondrial injury. Mitochondrial calpains have been reported to induce mitochondrial injury in mouse cardiomyocytes and pulmonary smooth muscle. In the present study
Li Huang et al.
International journal of molecular sciences, 22(12) (2021-07-03)
Retinitis pigmentosa (RP) is an inherited form of retinal degeneration characterized by primary rod photoreceptor cell death followed by cone loss. Mutations in several genes linked to the disease cause increased levels of cyclic guanosine monophosphate (cGMP) and calcium ion

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