NDUFS1 Antibody #60153
Filter:
- WB
- IP
Supporting Data
| REACTIVITY | H M R |
| SENSITIVITY | Endogenous |
| MW (kDa) | 75 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:50 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
NDUFS1 Antibody recognizes endogenous levels of total NDUFS1 protein. It can detect the carboxyl terminal 47 kDa fragment produced by caspase cleavage during apoptosis.
Species Reactivity:
Human, Mouse, Rat
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ile286 of human NDUFS1 protein. Antibodies are purified by peptide affinity chromatography.
Background
NDUFS1 (NADH dehydrogenase Fe-S protein 1) is a nuclear encoded structural subunit of NADH: ubiquinone oxidoreductase (complex 1) in the mitochondrial electron transport chain (1). Mutations in NDUFS1 and other complex 1 subunits leading to mitochondrial dysfunction are associated with a number of neurological disorders (2-5). High-fat diet associated with type 2 diabetes leads to decreased expression of complex 1 subunits, including NDUFS1 (6). NDUFS1 is the target of cleavage by apoptotic caspases contributing to the loss of mitochondrial transmembrane potential, compromised mitochondrial respiration, increased mitochondrial reactive oxygen species (ROS) production, and loss of lysosomal integrity (7,8). NDUFS1 can also be cleaved by the lymphocyte protease granzyme B (9). Studies have also found that MDM2, which has a canonical role as an inhibitor of the tumor suppressor p53, can also sequester NDUFS1 in the cytoplasm, leading to respiratory dysfunction and increases in ROS (10).
- Duncan, A.M. et al. (1992) Cytogenet Cell Genet 60, 212-3.
- Petruzzella, V. et al. (2012) Adv Exp Med Biol 942, 371-84.
- Pagniez-Mammeri, H. et al. (2012) Mol Genet Metab 105, 163-72.
- Kashani, A. et al. (2014) Neurogenetics 15, 161-4.
- Zhu, Y. et al. (2015) J Hum Genet 60, 11-6.
- Sparks, L.M. et al. (2005) Diabetes 54, 1926-33.
- Ricci, J.E. et al. (2004) Cell 117, 773-86.
- Huai, J. et al. (2013) J Cell Sci 126, 4015-25.
- Dildine, S.L. and Semler, B.L. (1989) J Virol 63, 847-62.
- Elkholi, R. et al. (2019) Mol Cell 74, 452-465.e7.
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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