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

Anti-Caspase-3 (Ab-2) Mouse mAb (10C1.C9) MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

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

AM34
  
Purchase on Sigma-Aldrich

Overview

Replacement Information

Key Spec Table

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-YAMA, Anti-Apopain, Anti-CASP3, Anti-LICE, Anti-ICE-3, Anti-CPP32
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
Catalogue Number GTIN
AM34 0

Documentation

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

Title

Safety Data Sheet (SDS) 

Anti-Caspase-3 (Ab-2) Mouse mAb (10C1.C9) Certificates of Analysis

TitleLot Number
AM34

References

Reference overview
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

Title
Caspases and other Apoptosis Related Tools Brochure
Data Sheet

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-YAMA, Anti-Apopain, Anti-CASP3, Anti-LICE, Anti-ICE-3, Anti-CPP32
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.