Anti-RAIDD (Human) mAb

WB - 1 ug/mL (chemiluminescence detection system)

Apoptosis is a major form of cell death characterized by morphological features including chromatin condensation and fragmentation, cell membrane blebbing, and formation of apoptotic bodies. These morphological changes occur via signaling pathways that lead to the recruitment and activation of caspases, a family of cysteine-containing, aspartate-specific proteases. Caspases exist as inactive proenzymes in cells and are activated through their processing into two subunits in response to apoptotic stimulation. Activated caspases cleave a variety of important cellular proteins, other caspases, and Bcl-2 family members, leading to a commitment to cell death. Caspase-7 (also known as Mch-3/ ICE-LAP3 / CMH-1) is a 35 kDa protein that has the highest similarity to caspase-3 (52% amino acid identity) among all caspase members. It has been identified as one of the ''effector'' caspases (which include caspase 3, 6, 7) that are cleaved by ''initiator'' caspases (which include caspase 8, 9) into active form, and then, in turn, cleave various cellular proteins for apoptosis. Recent study says that in Fas-mediated hepatocyte apoptosis, active caspase-7 is associated almost exclusively with the mitochondrial and microsomal fractions, whereas active caspase-3 is confined primarily to the cytosol. It implies a different role of caspase-3 and -7 in the execution of apoptosis.

1 mg/mL

100 ug IgG in 100 ul volume of PBS containing 50% glycerol, pH 7.2. Contains nopreservatives.

Human: 8738 Mouse: 12905

Length Recombinant human RAIDD (200 a.a.)

This antibody reacts with human RAIDD (~22 kDa) on Western blotting.

1 year

This antibody was purified from mouse ascites fluid using protein A agarose. This hybridoma was established by fusion of mouse myeloma cell P3U1 with Balb/c mouse splenocyte immunized with the recombinant full-length human RAIDD (200 a.a.).

RAIDD