Product Pathways - Apoptosis
Cleaved Caspase-3 (Asp175) (D3E9) Rabbit mAb #9579
|9579S||100 µl (200 tests)||---||In Stock||---|
|9579||carrier free and custom formulation / quantity||email request|
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Applications Key: IHC-P=Immunohistochemistry (Paraffin), IF-IC=Immunofluorescence (Immunocytochemistry), F=Flow Cytometry
Species predicted to react based on 100% sequence homology: Mouse, Rat, Monkey, Bovine, Pig.
Specificity / Sensitivity
Cleaved Caspase-3 (Asp175) (D3E9) Rabbit mAb recognizes endogenous levels of caspase-3 protein only when cleaved at Asp175. This antibody is preferred for immunofluorescence, flow cytometry, and immunohistochemistry applications. This antibody detects non-specific caspase substrates by western blot.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Asp175 of human caspase-3 protein.
Immunohistochemical analysis of paraffin-embedded Jurkat cell pellets, untreated (left) or etoposide-treated (right), using Cleaved Caspase-3 (Asp175) (D3E9) Rabbit mAb on SignalSlide® Cleaved Caspase-3 (Asp175) IHC Controls #8104.
Immunohistochemical analysis of paraffin-embedded HT-29 xenograft using Cleaved Caspase-3 (Asp175) (D3E9) Rabbit mAb in the presence of control peptide (left) or Cleaved Caspase-3 (Asp175) Blocking Peptide #1050 (right).
Immunohistochemical analysis of paraffin-embedded human malignant stromal tumor using Cleaved Caspase-3 (Asp175) (D3E9) Rabbit mAb.
Flow cytometric analysis of Jurkat cells, untreated (blue) or etoposide-treated (green), using Cleaved Caspase-3 (Asp175) (D3E9) Rabbit mAb.
Confocal immunofluorescent analysis of HeLa cells, untreated (left) or treated with Staurosporine #9953 (1 μM, 4 hr; right), using Cleaved Caspase-3 (Asp175) (D3E9) Rabbit mAb (green). Actin filaments were labeled with DY-554 phalloidin (red). Blue pseudocolor = DRAQ5® #4084 (fluorescent DNA dye).
Caspase-3 (CPP-32, Apoptain, Yama, SCA-1) is a critical executioner of apoptosis, as it is either partially or totally responsible for the proteolytic cleavage of many key proteins, such as the nuclear enzyme poly (ADP-ribose) polymerase (PARP) (1). Activation of caspase-3 requires proteolytic processing of its inactive zymogen into activated p17 and p12 fragments. Cleavage of caspase-3 requires the aspartic acid residue at the P1 position (2).
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For Research Use Only. Not For Use In Diagnostic Procedures.
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