Apoptosis or programmed cell death is a fundamental cellular process that is essential for normal tissue development and abnormal growth. Apoptosis is driven by two classes of specialized proteases known as caspases (Cysteine Aspartase). The initiator caspases can be activated by self-cleavage. The effector caspases are then activated in an amplification cascade. Several key factors are released from the mitochondria that regulate apoptosis. The first such factor (Cytochrome-C) to be described binds to a cytoplasmic scaffolding protein called Apaf-1 (Apoptosis Protease activating factor-1), a homolog of C. elegans Ced-4. Both Apaf-1 and Ced-4 are composed of an N-terminal Caspase Recrutiment domain (CARD) linked to a Nuceoltide-bidning domain (NBD), also known as NB-ARC or NOD domain. Ced-4 and Apaf-1 self-associate via the NBD and activate Casp-3 and -9. The C-terminal region of Apaf-1 lacks homology with Ced-4 and contains 12 WD-40 repeats. IN response to certain apoptotic stimuli, Cytochrome-C is released from the mitochondria and binds to Apaf-1 to form a ternary complex with, and activate, the initiator pro-caspase-9. Active caspase-9 then turns on downstream effector caspases, initiating apoptosis. The presence of CARD motifs in a variety of other effector and signaling molecules, including numerous caspases, NF- B-activating kinase, suggests that other CED-4/Apaf-1 family members likely exist in humans to coordinate downstream stress responses. Recently, Additional members of Apaf-1 family, NOD1/CARD4 and NOD2 have been cloned and characterized.
Apaf-1 (human 1205 aa; chromosome 12q23; mosue 1238 aa; rat 1249 aa; mol wt ~130kD) has significant (~20%) homology with ced-3 and ced-4. It is a cytoplsamic protein found in most tissues with highest expression in adult spleen and peripheral blood leukocytes, fetal brain, kidney, and lung correlating with high level of apoptosis in these tissues. Apaf-1 participates in the cytochrome-c dependent activation of caspase-3. The N-terminal 85-aa of Apaf-1 show 21% identity with C. elegans CED3. The next 320-aa show ~22% idneitty with CED4. C-terminus of Apaf-1 comprised of 12 WD repeats (TRP-Asp domains), which mediate proteinpprotein interactions. Apaf-1 is alternatively spliced to three forms that vary in length.
仕様
Size：100ug
Source Antigen：Human synthetic peptide
Grade：Highly Purified
Purity：Highly purified
Form：Supplied as a liquid in PBS, pH 7.2
Specificity：100% conserved in mouse and 94% in rat Apaf-1. It has no significant homology with ced-3/4, Nod-1 and NOD-2 family of proteins
