Recombinant Human AIF protein (His tag N-Terminus)
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Recombinant Human AIF protein (His tag N-Terminus) is a Human Full Length protein, in the 98 to 609 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE.
View Alternative Names
AIF, PDCD8, AIFM1, Programmed cell death protein 8
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human AIF protein (His tag N-Terminus) (AB177656)
15% SDS-PAGE analysis of ab177656 (3 μg).
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
AIF functions as an important element in mitochondrial-mediated apoptosis. Once released from mitochondria AIF triggers a caspase-independent pathway of apoptosis making it distinct from other pathways where caspases are central. While not part of a larger protein complex AIF interacts closely with several mitochondrial and nuclear elements to execute its functions. Researchers often monitor AIF activity using apoptosis ELISA kits which help in precise detection and quantification of this protein within cellular systems.
Pathways
The presence and activity of AIF align with the broader apoptotic pathway and mitochondrial respiration. AIF links significantly with other molecules like cytochrome c released during apoptosis although cytochrome c follows a caspase-dependent pathway. It also shows involvement in various cellular injury and stress response pathways reinforcing its role as a major player in cellular fate decisions and intrinsic apoptotic mechanisms.
Specifications
Form
Liquid
Additional notes
ab177656 was purified using conventional chromatography.
General info
Function
Functions both as NADH oxidoreductase and as regulator of apoptosis (PubMed : 17094969, PubMed : 20362274, PubMed : 23217327, PubMed : 33168626). In response to apoptotic stimuli, it is released from the mitochondrion intermembrane space into the cytosol and to the nucleus, where it functions as a proapoptotic factor in a caspase-independent pathway (PubMed : 20362274). Release into the cytoplasm is mediated upon binding to poly-ADP-ribose chains (By similarity). The soluble form (AIFsol) found in the nucleus induces 'parthanatos' i.e. caspase-independent fragmentation of chromosomal DNA (PubMed : 20362274). Binds to DNA in a sequence-independent manner (PubMed : 27178839). Interacts with EIF3G, and thereby inhibits the EIF3 machinery and protein synthesis, and activates caspase-7 to amplify apoptosis (PubMed : 17094969). Plays a critical role in caspase-independent, pyknotic cell death in hydrogen peroxide-exposed cells (PubMed : 19418225). In contrast, participates in normal mitochondrial metabolism. Plays an important role in the regulation of respiratory chain biogenesis by interacting with CHCHD4 and controlling CHCHD4 mitochondrial import (PubMed : 26004228).. Isoform 4. Has NADH oxidoreductase activity. Does not induce nuclear apoptosis.. Isoform 5. Pro-apoptotic isoform.
Sequence similarities
Belongs to the FAD-dependent oxidoreductase family.
Post-translational modifications
Under normal conditions, a 54-residue N-terminal segment is first proteolytically removed during or just after translocation into the mitochondrial intermembrane space (IMS) by the mitochondrial processing peptidase (MPP) to form the inner-membrane-anchored mature form (AIFmit). During apoptosis, it is further proteolytically processed at amino-acid position 101 leading to the generation of the mature form, which is confined to the mitochondrial IMS in a soluble form (AIFsol). AIFsol is released to the cytoplasm in response to specific death signals, and translocated to the nucleus, where it induces nuclear apoptosis in a caspase-independent manner.. Ubiquitination by XIAP/BIRC4 does not lead to proteasomal degradation. Ubiquitination at Lys-255 by XIAP/BIRC4 blocks its ability to bind DNA and induce chromatin degradation, thereby inhibiting its ability to induce cell death.
Subcellular localisation
Mitochondrion intermembrane space
Target data
Product promise
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