All Photos(1)



Anti-Caspase 3 antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Anti-Apopain, Anti-Yama, Anti-CPP32
MDL number:

biological source


Quality Level

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies




buffered aqueous solution

mol wt

antigen 32 kDa

species reactivity



microarray: suitable
western blot: 1:3,000 using Jurkat human T-cell leukemia cell extract



UniProt accession no.

shipped in

dry ice

storage temp.


Gene Information

human ... CASP3(836)

General description

Caspase 3 is a cytosolic protein present as a 32 kDa proenzyme in cells. It is activated by proteolytic cleavage into the 20 kDa (p20) and 11 kDa (p11) active subunits when cells undergo apoptosis.


synthetic peptide corresponding to the N-terminal of human caspase 3 (amino acids 29-43 with C-terminally added lysine) conjugated to KLH. This sequence, unique to caspase 3, corresponds to N-terminal of the enzyme p20 subunit and is highly conserved in rat and mouse caspase 3.


Anti-Caspase 3 antibody produced in rabbit is suitable for microarray and western blotting at a working dilution of 1:3000 using Jurkat human T-cell leukemia cell extract. It was used as a primary antibody for western blotting in a study to establish the biomolecular basis for the role of PCMT1 (isoaspartyl protein carboxyl-O-methyltransferase) as a part of a novel apoptosis regulatory mechanism. It was used to examine activation of caspase-3 via immunoblotting in a study to confirm the apoptosis of tumor cells mediated by AAV-ISN-T (recombinant adeno-associated virus vector with signal peptides of human insulin) administration. It was used as a primary antibody at 1:300 dilution for immunohistochemistry of deparaffinized sections of squamous cell carcinoma of the tongue containing surrounding normal tissue. It was used at a dilution of 1:1000 to detect caspase-3 and its cleaved form P20 in a study.

Biochem/physiol Actions

Caspase 3 is one of the key executioners of apoptosis downstream in the apoptotic pathway, as it is activated in cells by various death signals. In some neurodegenerative diseases, such as Huntington disease (HD) and Alzheimer′s disease (AD), specific neuronal caspase substrates have been identified. In Huntington disease (HD), caspase 3 specifically cleaves the HD gene product, Huntingtin.
Caspase 3 cleaves many key proteins including poly(ADP-ribose) polymerase (PARP), sterol-regulatory element-binding proteins (SREBPs), DNA-dependent protein kinase (DNA-PK), α-fodrin, gelsolin, PKCd and DFF45/ICAD during apoptosis. High levels of this enzyme in lymphocytes suggest that it is an important mediator of apoptosis in the immune system. Deletion of CASP-3 gene in mice results in hyperplasia and cell abnormalities, indicating that caspase 3 is essential for morphogenetic cell death during normal brain development.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.


Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Storage Class Code

12 - Non Combustible Liquids

WGK Germany


Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Certificate of Origin

Huntingtin inhibits caspase-3 activation.
Zhang Y, et al.
The Embo Journal, 25(24), 5896-5906 (2006)
Q Song et al.
The EMBO journal, 15(13), 3238-3246 (1996-07-01)
Radiosensitive cell lines derived from X-ray cross complementing group 5 (XRCC5), SCID mice and a human glioma cell line lack components of the DNA-dependent protein kinase, DNA-PK, suggesting that DNA-PK plays an important role in DNA double-strand break repair. Another...
Apoptosis: a review of programmed cell death.
Elmore S.
Toxicologic Pathology, 35(4), 495-516 (2007)
Hong Ma et al.
Hepatology (Baltimore, Md.), 42(6), 1355-1363 (2005-12-01)
The extracellular domain of the tumor necrosis factor-related apoptosis-inducing ligand (sTRAIL) may function as a soluble cytokine to selectively kill various cancer cells without toxicity to most normal cells. We constructed a series of recombinant adeno-associated virus (AAV) vectors expressing...
Irene Sambri et al.
The Journal of biological chemistry, 286(51), 43690-43700 (2011-10-29)
Asparaginyl deamidation, a spontaneous protein post-biosynthetic modification, determines isoaspartyl formation and structure-function impairment. The isoaspartyl protein carboxyl-O-methyltransferase (PCMT1; EC catalyzes the repair of the isopeptide bonds at isoaspartyl sites, preventing deamidation-related functional impairment. Protein deamidation affects key apoptosis mediators...

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service