Rabbit anti Caspase-3


Rabbit anti Caspase-3

100 μg

Catalog no.



304 EUR

Buy Rabbit anti Caspase-3 at gentaur.com

Antibody's reacts with


Antibody is raised in




Protein number

see ncbi




Western Blot

Antibody's specificity

No Data Available


Primary Antibodies

Latin name

Oryctolagus cuniculus

Antigen-antibody binding interaction

Rabbit anti Caspase-3 Antibody

Antibody come from

Full length recombinant caspase-3 protein

Antibody's suited for

Applications: western blot, use at 2-10 µg/ml

Antibody's reacts with these species

This antibody doesn't cross react with other species

Other description

Provided as solution in phosphate buffered saline, pH 7.3, with 1.0 mg/ml BSA and 0.05% sodium azide. Ammonium Sulfate Precipitation


This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals. This datasheet is as accurate as reasonably achievable, but Nordic-MUbio accepts no liability for any inaccuracies or omissions in this information.


This antibody needs to be stored at + 4°C in a fridge short term in a concentrated dilution. Freeze thaw will destroy a percentage in every cycle and should be avoided.Human and some mouse caspases are active in apoptosis and cell death and even in necrosis and inflammation. CASP Gene and orthologous enzymes have been identifies successfully in the signal transduction cascade and pathways.


Rabbits are used for polyclonal antibody production by nordc. Rabbit antibodies are very stable and can be stored for several days at room temperature. nordc adds sodium azide and glycerol to enhance the stability of the rabbit polyclonal antibodies. Anti-human, anti mouse antibodies to highly immunogenic selected peptide sequences are" monoclonal like" since the epitope to which they are directed is less than 35 amino acids long.

Relevant references

1] Ordering the cytochrome c-initiated caspase cascade: hierarchical activation of caspases-2, -3, -6, -7, -8, and -10 in a caspase-9-dependent manner. Slee EA; Harte MT; Kluck RM; Wolf BB; Casiano CA; Newmeyer DD; Wang HG; Reed JC; Nicholson DW; Alnemri ES; Green DR; Martin SJ. J Cell Biol, 144(2):281-92 1999 Jan 25 _x000B__x000B_2] Redox regulation of caspase-3(-like) protease activity: regulatory roles of thioredoxin and cytochrome c. Ueda S; Nakamura H; Masutani H; Sasada T; Yonehara S; Takabayashi A; Yamaoka Y; Yodoi J. J Immunol, 161(12):6689-95 1998 Dec 15 _x000B__x000B_3] Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells. Samali A; Cai J; Zhivotovsky B; Jones DP; Orrenius S. EMBO J, 18(8):2040-8 1999 Apr 15

Long description

Caspase-3 along with caspase 7 and 6 form the group of effector caspases that are responsible for the cleavage of multiple substrates including the cytokeratins, PARP, alpha fodrin, NuMA and others. Caspase-7 occurs in three varient forms. Caspase-3-like activities are required for Fas-mediated apoptosis. However, the role of caspase-1 and caspase-3 in mediating Fas-induced cell death is not clear. Although wild-type, caspase-1(-/-), and caspase-3(-/-) hepatocytes were killed at a similar rate when cocultured with FasL expressing NIH 3T3 cells, caspase-3(-/-) hepatocytes displayed drastically different morphological changes as well as significantly delayed DNA fragmentation. For both wild-type and caspase-1 (-/-) apoptotic hepatocytes, typical apoptotic features such as cytoplasmic blebbing and nuclear fragmentation are seen within 6 hr, but neither event was observed for caspase-3(-/-) hepatocytes. In thymocytes apoptotic caspase-3 (-/-) thymocytes exhibit similar abnormal morphological changes and delayed DNA fragmentation observed in hepatocytes. Cleavage of various caspase substrates implicates apoptotic events, including gelsolin, fodrin, laminB, and DFF45/ICAD are delayed or absent. The altered cleavage of these key substrates is likely responsible for the aberrant apoptosis observed in both hepatocytes and thymocytes deficient in caspase-3.