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AM34 Anti-Caspase-3 (Ab-2) Mouse mAb (10C1.C9)

Anti-Caspase-3 (Ab-2) Mouse mAb (10C1.C9) : FDS (Fiches de données de sécurité), certificats d’analyse (CoA) et de qualité (CoQ), dossiers, brochures et autres documents disponibles.

Synonymes: Anti-CPP32, Anti-YAMA, Anti-Apopain, Anti-CASP3, Anti-LICE, Anti-ICE-3

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AM34
  
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      Aperçu

      Replacement Information

      Tableau de caractéristiques principal

      Species ReactivityHostAntibody Type
      HMMonoclonal Antibody
      Description
      Overview

      This product has been discontinued.



      Recognizes the ~32, ~28, and ~17 kDa forms of caspase-3. Additional unrelated proteins between ~60 and ~45 kDa may also be detected.
      Catalogue NumberAM34
      Brand Family Calbiochem®
      SynonymsAnti-CPP32, Anti-YAMA, Anti-Apopain, Anti-CASP3, Anti-LICE, Anti-ICE-3
      References
      ReferencesAlnemri, E.S. 1997. J. Cell. Biochem. 64, 33.
      Bayaert, R., et al. 1997. J. Biol. Chem. 272, 11694.
      Erhardt, P., et al. 1997. J. Biol. Chem. 272, 15049.
      Inayat-Hussain, S.H., et al. 1997. Hepatology 25, 1516.
      Krjewska, M., et al. 1997. Cancer Res. 57, 1605.
      Mashima, T., et al. 1997. Oncogene 14, 1007.
      McConnell, K.R., et al. 1997. J. Immunol. 158, 2083.
      Posmantur, R., et al. 1997. J. Neurochem. 68, 2328.
      Suzuki, A., et al. 1997. Exp. Cell. Res. 233, 48.
      Liu, X., et al. 1996. J. Biol. Chem. 271, 13371.
      Quan, L.T., et al. 1996. Proc. Natl. Acad. Sci. USA 93, 1972.
      Teraoka, H., et al. 1996. FEBS Lett. 393, 1.
      Tiso, N., et al. 1996. Biochem. Biophys. Res. Commun. 225 983.
      Xue, D., et al. 1996. Genes Dev. 10, 1073.
      Tewari, M., et al. 1995. Cell 81, 801.
      Fernandes-Alnemri, T., et al. 1994. J. Biol. Chem. 269, 30761.
      Product Information
      FormLiquid
      FormulationIn 0.05 M sodium phosphate buffer, 0.2% gelatin, pH 7.4.
      Positive controlJurkat cells
      Preservative≤0.1% sodium azide
      Applications
      Key Applications Immunoblotting (Western Blotting)
      Not Frozen Sections
      Not Immunofluorescence
      Not Immunoprecipitation
      Not Paraffin Sections
      Application NotesImmunoblotting (1 µg/ml)
      Frozen Sections (not recommended)
      Immunofluorescence (not recommended)
      Immunoprecipitation (not recommended)
      Paraffin Sections (not recommended)
      Application CommentsAdditional unrelated proteins between ~45 and ~60 kDa may also be detected. Antibody should be titrated for optimal results in individual systems.

      Recommended protocol for extracting CPP32 from cell pellets.
      1. Rinse cells 2 times with cold PBS and resuspend the final cell pellet (6 x 105 cells/µl) in 50 mM PIPES/KOH pH 6.5, 2 mM EDTA, 0.1% CHAPS, 5 mM DTT, 20 µg/ml leupeptin, 10 µg/ml pepstatin A, 10 µg/ml aprotinin, and 2 mM PMSF.
      2. Subject the cells to 3 freeze/thaw cycles in dry ice/methanol.
      3. Centrifuge the lysate at 4°C for 30 min at 20,000 x g and recover the supernatant fraction.
      4. Apply a minimum of 25 µg protein per lane (the amount may need to be optimized for individual cell lines or sample types).
      Biological Information
      Immunogenfull-length, recombinant, human caspase-3
      ImmunogenHuman
      Clone10C1.C9
      HostMouse
      IsotypeIgG₁
      Species Reactivity
      • Human
      Antibody TypeMonoclonal Antibody
      Concentration Label Please refer to vial label for lot-specific concentration
      Physicochemical Information
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Storage and Shipping Information
      Ship Code Blue Ice Only
      Toxicity Standard Handling
      Storage +2°C to +8°C
      Do not freeze Yes
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Référence GTIN
      AM34 0

      Documentation

      Anti-Caspase-3 (Ab-2) Mouse mAb (10C1.C9) FDS

      Titre

      Fiche de données de sécurité des matériaux (FDS) 

      Anti-Caspase-3 (Ab-2) Mouse mAb (10C1.C9) Certificats d'analyse

      TitreNuméro de lot
      AM34

      Références bibliographiques

      Aperçu de la référence bibliographique
      Alnemri, E.S. 1997. J. Cell. Biochem. 64, 33.
      Bayaert, R., et al. 1997. J. Biol. Chem. 272, 11694.
      Erhardt, P., et al. 1997. J. Biol. Chem. 272, 15049.
      Inayat-Hussain, S.H., et al. 1997. Hepatology 25, 1516.
      Krjewska, M., et al. 1997. Cancer Res. 57, 1605.
      Mashima, T., et al. 1997. Oncogene 14, 1007.
      McConnell, K.R., et al. 1997. J. Immunol. 158, 2083.
      Posmantur, R., et al. 1997. J. Neurochem. 68, 2328.
      Suzuki, A., et al. 1997. Exp. Cell. Res. 233, 48.
      Liu, X., et al. 1996. J. Biol. Chem. 271, 13371.
      Quan, L.T., et al. 1996. Proc. Natl. Acad. Sci. USA 93, 1972.
      Teraoka, H., et al. 1996. FEBS Lett. 393, 1.
      Tiso, N., et al. 1996. Biochem. Biophys. Res. Commun. 225 983.
      Xue, D., et al. 1996. Genes Dev. 10, 1073.
      Tewari, M., et al. 1995. Cell 81, 801.
      Fernandes-Alnemri, T., et al. 1994. J. Biol. Chem. 269, 30761.

      Brochure

      Titre
      Caspases and other Apoptosis Related Tools Brochure
      Fiche technique

      Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

      Revision17-August-2007 RFH
      SynonymsAnti-CPP32, Anti-YAMA, Anti-Apopain, Anti-CASP3, Anti-LICE, Anti-ICE-3
      ApplicationImmunoblotting (1 µg/ml)
      Frozen Sections (not recommended)
      Immunofluorescence (not recommended)
      Immunoprecipitation (not recommended)
      Paraffin Sections (not recommended)
      DescriptionPurified mouse monoclonal antibody generated by immunizing mice with the specified immunogen and fusing splenocytes with Sp2/0 mouse myeloma cells. Recognizes the ~32, ~28, and ~17 kDa forms of caspase-3.
      BackgroundCaspase-3 (CPP32/Yama/Apopain) exists as a 32 kDa inactive precursor protein in the cytoplasm of most cell types. Upon proteolytic activation the protein is cleaved at a specific site within the molecule to yield a heterodimer consisting of p20 and p11 subunits. The cleavage/activation proceeds in two steps yielding first a p3 fragment followed by the p20 and p11 fragments and is mediated by specific proteases, including serine proteases and the enzyme granzyme B. Activation of CPP32 occurs rather rapidly following the onset of apoptosis induced by a number of different signals including, but not restricted to, TGFβ1, TNF, and Fas. One of the most potent chemical activators of CPP32 is staurosporine. Once activated, CPP32 has a number of substrates; among those which have been reported are MDM2, PITSLRE kinases, actin, DNA-PK, and PARP. Related to the C. elegans protein Ced-3, CPP32 has been mapped in humans to chromosome 4q33-q35.1.
      HostMouse
      Immunogen speciesHuman
      Immunogenfull-length, recombinant, human caspase-3
      Clone10C1.C9
      IsotypeIgG₁
      Specieshuman
      Positive controlJurkat cells
      FormLiquid
      FormulationIn 0.05 M sodium phosphate buffer, 0.2% gelatin, pH 7.4.
      Concentration Label Please refer to vial label for lot-specific concentration
      Preservative≤0.1% sodium azide
      CommentsAdditional unrelated proteins between ~45 and ~60 kDa may also be detected. Antibody should be titrated for optimal results in individual systems.

      Recommended protocol for extracting CPP32 from cell pellets.
      1. Rinse cells 2 times with cold PBS and resuspend the final cell pellet (6 x 105 cells/µl) in 50 mM PIPES/KOH pH 6.5, 2 mM EDTA, 0.1% CHAPS, 5 mM DTT, 20 µg/ml leupeptin, 10 µg/ml pepstatin A, 10 µg/ml aprotinin, and 2 mM PMSF.
      2. Subject the cells to 3 freeze/thaw cycles in dry ice/methanol.
      3. Centrifuge the lysate at 4°C for 30 min at 20,000 x g and recover the supernatant fraction.
      4. Apply a minimum of 25 µg protein per lane (the amount may need to be optimized for individual cell lines or sample types).
      Storage +2°C to +8°C
      Do Not Freeze Yes
      Toxicity Standard Handling
      ReferencesAlnemri, E.S. 1997. J. Cell. Biochem. 64, 33.
      Bayaert, R., et al. 1997. J. Biol. Chem. 272, 11694.
      Erhardt, P., et al. 1997. J. Biol. Chem. 272, 15049.
      Inayat-Hussain, S.H., et al. 1997. Hepatology 25, 1516.
      Krjewska, M., et al. 1997. Cancer Res. 57, 1605.
      Mashima, T., et al. 1997. Oncogene 14, 1007.
      McConnell, K.R., et al. 1997. J. Immunol. 158, 2083.
      Posmantur, R., et al. 1997. J. Neurochem. 68, 2328.
      Suzuki, A., et al. 1997. Exp. Cell. Res. 233, 48.
      Liu, X., et al. 1996. J. Biol. Chem. 271, 13371.
      Quan, L.T., et al. 1996. Proc. Natl. Acad. Sci. USA 93, 1972.
      Teraoka, H., et al. 1996. FEBS Lett. 393, 1.
      Tiso, N., et al. 1996. Biochem. Biophys. Res. Commun. 225 983.
      Xue, D., et al. 1996. Genes Dev. 10, 1073.
      Tewari, M., et al. 1995. Cell 81, 801.
      Fernandes-Alnemri, T., et al. 1994. J. Biol. Chem. 269, 30761.