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Endonuclease G, mitochondrial is a protein in humans that is encoded by ENDOG gene. Cleaves DNA at double-stranded (DG)n.(DC)n and at single-stranded (DC)n tracts. In addition to deoxyribonuclease activities, also has ribonuclease (RNase) and RNase H activities. Capable of generating the RNA primers required by DNA polymerase gamma to initiate replication of mitochondrial DNA (By similarity).
The following ENDOG reagents supplied by CUSABIO are manufactured under a strict quality control system. Multiple applications have been validated and solid technical support is offered.
ENDOG Antibodies for Homo sapiens (Human)
| Code | Product Name | Species Reactivity | Application |
|---|---|---|---|
| CSB-PA780526 | ENDOG Antibody |
Human | ELISA,IHC |
| CSB-PA055939 | ENDOG Antibody |
Human | ELISA,IHC |
| CSB-PA007665LA01HU | ENDOG Antibody |
Human, Mouse | ELISA, WB |
| CSB-PA007665LB01HU | ENDOG Antibody, HRP conjugated |
Human | ELISA |
| CSB-PA007665LC01HU | ENDOG Antibody, FITC conjugated |
Human | |
| CSB-PA007665LD01HU | ENDOG Antibody, Biotin conjugated |
Human | ELISA |
ENDOG Proteins for Bos taurus (Bovine)
| Code | Product Name | Source |
|---|---|---|
| CSB-YP007665BO CSB-EP007665BO CSB-BP007665BO CSB-MP007665BO CSB-EP007665BO-B |
Recombinant Bovine Endonuclease G, mitochondrial (ENDOG) |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
ENDOG Proteins for Mus musculus (Mouse)
| Code | Product Name | Source |
|---|---|---|
| CSB-YP007665MO CSB-EP007665MO CSB-BP007665MO CSB-MP007665MO CSB-EP007665MO-B |
Recombinant Mouse Endonuclease G, mitochondrial (Endog) |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
ENDOG Proteins for Homo sapiens (Human)
| Code | Product Name | Source |
|---|---|---|
| CSB-YP622760HU CSB-EP622760HU CSB-BP622760HU CSB-MP622760HU CSB-EP622760HU-B |
Recombinant Human Endonuclease G, mitochondrial (ENDOG) |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
Endonuclease G (ENDOG) is one of the nucleases involved in nucleosomal fragmentation of DNA during apoptosis [1]. Genetically engineered mice lacking DFF45 or site-directed mutants of DFF45 lacking the caspase-cleavage site, still retain residual DNA fragmentation and are normal inphenotype [1][2]. These discoveries contributed to the identification and characterization of ENDOG. The ENDOG is resided within mitochondria and translocate to the nucleus upon apoptotic stimuli such as truncated Bid (tBid), tumor-necrosis factor-alpha (TNF-α), and UV irradiation [1][3]. Once released from mitochondria, ENDOG cleaves chromatin DNA into nucleosomal fragments independently of caspases. ENDOG null mice are viable and develop to adulthood with no obvious aberrations [4]. Fibroblasts generated from the EndoG null mice show no difference in susceptibility when induced to cell death by various intrinsic and extrinsic apoptotic stimuli [4]. Additionally, EndoG null mice are equally sensitive to excitotoxic stress [4]. David KK et al. therefore concluded that ENDOG is not essential for embryogenesis and apoptosis [4]. In addition to its dispensable role in apoptosis, EndoG acts as a homodimer that is thought to be implicated in mitochondrial DNA replication [5] with important roles in recombination and repair [6][7].
[1] Li LY, Luo X and Wang X. Endonuclease G is an apoptotic DNase when released from mitochondria [J]. Nature 2003, 12: 95–99.
[2] Zhang J, Liu X, et al. Resistance to DNA fragmentation and chromatin condensation in mice lacking the DNA fragmentation factor 45 [J]. Proc. Natl. Acad. Sci. 1998, USA 95: 12480–12485.
[3] van Loo G, Schotte P, et al. Endonuclease G: a mitochondrial protein released in apoptosis and involved in caspase-independent DNA degradation [J]. Cell Death Differ. 2001, 8: 1136–1142.
[4] David KK, Sasaki M, et al. EndoG is dispensable in embryogenesis and apoptosis [J]. Cell Death Differ. 2006 Jul;13(7):1147-55.
[5] Cote J and Ruiz-Carrillo A. Primers for mitochondrial DNA replication generated by endonuclease G [J]. Science 1993, 261: 765–769.
[6] Zassenhaus HP and Denniger G. Analysis of the role of the NUC1 endo/exonuclease in yeast mitochondrial DNA recombination [J]. Curr. Genet. 1994, 25: 142–149.
[7] Ikeda S and Ozaki K. Action of mitochondrial endonuclease G on DNA damaged by L-ascorbic acid, peplomycin, and cis-diamminedichloroplatinum (II) [J]. Biochem. Biophys. Res. Commun. 1997, 235: 291–294.
