Flow cytometric analysis of Jurkat cells, untreated (blue) or etoposide-treated (green), using Cleaved PARP (Asp214) (D64E10) XP® Rabbit mAb.
Flow cytometric analysis of Jurkat cells using PARP (46D11) Rabbit mAb (solid line) compared to concentration-matched Rabbit (DA1E) mAb IgG XP® Isotype Control #3900 (dashed line). Anti-rabbit IgG (H+L), F(ab')2 Fragment (Alexa Fluor® 488 Conjugate) #4412 was used as a secondary antibody.
Confocal immunofluorescent analysis of HeLa cells, untreated (left) or treated with Staurosporine #9953 (right), using Cleaved PARP (Asp214) (D64E10) XP® Rabbit mAb (green). Actin filament were labeled with DY-554 phalloidin. Blue pseudocolor = DRAQ5® #4084 (fluorescent DNA dye).
Confocal immunofluorescent analysis of untreated HeLa cells labeled with PARP (46D11) Rabbit mAb (green). Actin filaments have been labeled with Alexa Fluor® 555 phalloidin (red).
Immunohistochemical analysis of paraffin-embedded human tonsil using Cleaved PARP (Asp214) (D64E10) XP® Rabbit mAb.
Western blot analysis of HEK293 cell extracts, untreated (-) or PARP knock-out (+), using PARP (46D11) Rabbit mAb #9532 (upper), or β-actin (13E5) Rabbit mAb #4970 (lower).
Western blot analysis of extracts from HeLa cells, untreated or treated with Staurosporine #9953 (1 μM, 3 hr), Jurkat cells, untreated or etoposide-treated (25 μM, overnight), and THP-1 cells, untreated or cycloheximide-treated (CHX, 10 μg/ml, overnight) followed by treatment with TNF-α #8902 (20 ng/ml, 4 hr), using Cleaved PARP (Asp214) (D64E10) XP® Rabbit mAb (upper), or total PARP Antibody #9542 (lower).
Western blot analysis of extracts from THP-1 cells, untreated or treated with TNF-α and cycloheximide as well as control extracts from SW620 and A20 cell lines, using PARP (46D11) Rabbit mAb.
PhosphoPlus® Duets from Cell Signaling Technology (CST) provide a means to assess protein activation status. Each Duet contains an activation-state and total protein antibody to your target of interest. These antibodies have been selected from CST's product offering based upon superior performance in specified applications.
PARP, a 116 kDa nuclear poly (ADP-ribose) polymerase, appears to be involved in DNA repair in response to environmental stress (1). This protein can be cleaved by many ICE-like caspases in vitro (2,3) and is one of the main cleavage targets of caspase-3 in vivo (4,5). In human PARP, the cleavage occurs between Asp214 and Gly215, which separates the PARP amino-terminal DNA binding domain (24 kDa) from the carboxy-terminal catalytic domain (89 kDa) (2,4). PARP helps cells to maintain their viability; cleavage of PARP facilitates cellular disassembly and serves as a marker of cells undergoing apoptosis (6).
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