Anti-APAF1 Products

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For Research Use Only. Not For Clinical Use.

As a leading supplier of apoptosis research reagents, Creative Biolabs is committed to helping you uncover insights into the fundamental mechanisms that drive the activation of caspases. Our full portfolio of top tier anti-APAF1 recombinant antibodies have been carefully validated for outstanding quality and reliability, so that you can clearly detect APAF1 and evaluate its expression during intrinsic apoptosis in cells and tissue samples.

APAF1: The Core of the Apoptosome and Initiator of Caspase Activation

Apoptotic Peptidase Activating Factor 1, also known as APAF1, is the core scaffold of the apoptosome, a large, wheel-shaped assembly that is critical to the activation of caspases and induction of the intrinsic cell death program. Upon exposure to intracellular stress signals, cytochrome c is released from the mitochondria, and its interaction with APAF1 initiates its activation. The conformational changes in APAF1 drive its oligomerization into a large heptameric wheel complex that recruits and activates the initiator caspase-9, which subsequently targets the effector caspases that orchestrate cellular disassembly. This elegant molecular process is the basis of apoptosis, and defects in APAF1 function are commonly observed in cancers that are resistant to treatment.

Alternative Names

Apoptotic Peptidase Activating Factor 1; APAF-1; Apoptotic Protease-Activating Factor 1; Apoptotic Peptidase Activating Factor; Apoptotic Protease Activating Factor; KIAA0413; CED4;

Background

This gene encodes a cytoplasmic protein that initiates apoptosis. This protein contains several copies of the WD-40 domain, a caspase recruitment domain (CARD), and an ATPase domain (NB-ARC). Upon binding cytochrome c and dATP, this protein forms an oligomeric apoptosome. The apoptosome binds and cleaves caspase 9 preproprotein, releasing its mature, activated form. Activated caspase 9 stimulates the subsequent caspase cascade that commits the cell to apoptosis. Alternative splicing results in several transcript variants encoding different isoforms.

Anti-APAF1 rAb Products

Creative Biolabs' anti-APAF1 recombinant antibodies are of superior quality, highly specific, and amply validated to detect APAF1 in cell lysates as well as for use in Western Blot and immunoprecipitation applications. Our rAbs are capable of clearly detecting the full-length, native APAF1 protein due to their high affinity and have been confirmed to demonstrate reproducible performance experiment after experiment.

Table 1. Featured anti-APAF1 recombinant antibody products at Creative Biolabs.

Customer Reviews

rAb Production

Creative Biolabs' anti-APAF1 recombinant antibodies are generated in the most sophisticated expression systems. Optimized mammalian cell lines are used for production, which enables high folding efficiencies and allows our antibodies to recognize the most complex conformational epitopes found in the native full length APAF1 protein.

Featured Anti-APAF1 Recombinant Antibody Production Platforms
Fig.1 Milligram-scale anti-APAF1 recombinant antibody production.

Fig.2 Gram-scale anti-APAF1 recombinant antibody production.

rAb Modalities

Creative Biolabs offers a wide selection of anti-APAF1 antibodies, with customizable modalities to fit all of your research needs. We offer full length IgG antibodies for traditional immunoassays such as Western blot, ELISA, and immunohistochemistry, and a variety of engineered antibody fragments for structural studies.

Fig.3 Full-length anti-APAF1 recombinant antibody production and modalities.

Creative Biolabs is your premier source for high quality, rigorously validated anti-APAF1 recombinant antibodies that are perfect for use in apoptosis research. We are a trusted resource that helps you reveal insights into fundamental processes in caspase activation so that you can make meaningful advances in cancer and neurobiology research. We have the experience and the products to support your discoveries. Please reach out to our scientific support team today.