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Key Documents

06-735

Sigma-Aldrich

Anti-Caspase 3 Antibody

Upstate®, from rabbit

Synonyme(s) :

Anti-CASP-3, Anti-Caspase-3

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About This Item

Code UNSPSC :
12352203
eCl@ss :
32160702
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Niveau de qualité

Forme d'anticorps

purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

polyclonal

Espèces réactives

mouse, human, rat

Fabricant/nom de marque

Upstate®

Technique(s)

immunohistochemistry: suitable
western blot: suitable

Isotype

IgG

Numéro d'accès NCBI

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... CASP3(836)

Description générale

Caspase-3 (UniProt: P42574; also known as EC:3.4.22.56, CASP-3, Apopain, Cysteine protease CPP32, CPP-32, Protein Yama, SREBP cleavage activity 1, SCA-1) is encoded by the CASP3 (also known as CPP32) gene (Gene ID: 836) in human. Cysteine-aspartic proteases or Caspases play essential roles in apoptosis, necrosis, and inflammation. Historically, caspases were numbered in the order in which they were identified. Caspase-3 is a heterotetrameric enzyme that consists of two anti-parallel arranged heterodimers, each one formed by a 17 kDa (p17) and a 12 kDa (p12) subunit. Caspase-3 is initially produced with a propeptide sequence (aa 1-9), the removal of which yields the 268 aa. caspase-3 proenzyme. Upon activation, the proenzyme is proteolytically cleaved first between Asp175-Ser176 to generate a p20 (aa 10-175) fragment and the p12 (aa 176-277) subunit. Further cleavage of the p20 fragment between Asp28-Ser29 produces the p17 (aa 29-175) subunit. The p17 and p12 subunits dimerize and forms the active caspase-3 enzyme. Caspase-3 has a strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-|- with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3, although Val or Ala are also accepted at this position. Caspase-3 is involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis, it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a Asp216-|-Gly217 bond. Caspase-3 mediates the proteolytic activation of caspases-6 and -7, while caspase-3 itself is processed and activated by caspase-8, -9, or -10.

Spécificité

Recognizes full-length Caspase 3 (Yama/Apopain) and proteolytic fragments.

Immunogène

Human full-length Caspase 3 fusion protein containing a histidine-6 tag

Application

This Anti-Caspase 3 Antibody is validated for use in Immunihistochmistry and Western Blotting for the detection of Caspase 3.
Western Blotting Analysis: 1μg/mL of this antibody detects Caspase-3 in A431 cell lysate.

Immunohistochemistry (Paraffin) Analysis: A 1:250 dilution of this antibody detected Caspase-3 in Human tonsil tissue sections.

Qualité

routinely evaluated by immunoblot on RIPA lysates from non-stimulated human A431 cells, mouse 3T3/A31 or rat PC12 cells

Description de la cible

32 kDa

Liaison

Replaces: 04-1090; 04-439

Forme physique

Format: Purified
Protein A purified IgG in of 0.1M Tris-glycine, pH 7.4, 0.15M NaCl,and 0.05% sodium azide.

Stockage et stabilité

Stable for 2 years at 2-8°C from date of shipment. For maximum recovery of product, centrifuge the original vial prior to removing the cap.

Remarque sur l'analyse

Control
Positive Antigen Control: Catalog #12-301, non-stimulated A431 cell lysate. Add 2.5µL of 2-mercaptoethanol/100µL of lysate and boil for 5 minutes to reduce the preparation. Load 20µg of reduced lysate per lane for mingels.

Informations légales

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

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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1


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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

M Leist et al.
Biochemical and biophysical research communications, 258(1), 215-221 (1999-05-01)
The endogenous mediator nitric oxide (NO) blocked apoptosis of Jurkat cells elicited by staurosporine, anti-CD95 or chemotherapeutics, and switched death to necrosis. The switch in the mode of cell death was dependent on the ATP loss elicited by NO. This
Antiandrogen-induced cell death in LNCaP human prostate cancer cells.
Lee, EC; Zhan, P; Schallhom, R; Packman, K; Tenniswood, M
Cell Death and Differentiation null
Prisca Boisguérin et al.
Cardiovascular research, 116(3), 633-644 (2019-05-31)
Regulated cell death is a main contributor of myocardial ischaemia-reperfusion (IR) injury during acute myocardial infarction. In this context, targeting apoptosis could be a potent therapeutical strategy. In a previous study, we showed that DAXX (death-associated protein) was essential for
A caspase cascade regulating developmental axon degeneration.
Simon, DJ; Weimer, RM; McLaughlin, T; Kallop, D; Stanger, K; Yang, J; O'Leary et al.
The Journal of Neuroscience null
Oral inoculation of probiotics Lactobacillus acidophilus NCFM suppresses tumour growth both in segmental orthotopic colon cancer and extra-intestinal tissue.
Chen, CC; Lin, WC; Kong, MS; Shi, HN; Walker, WA; Lin, CY; Huang, CT; Lin, YC; Jung, SM; Lin, TY
The British Journal of Nutrition null

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