COX17 Antibody (monoclonal) (M01)
Mouse monoclonal antibody raised against a partial recombinant COX17.
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, IHC, E |
---|---|
Primary Accession | Q14061 |
Other Accession | NM_005694 |
Reactivity | Human |
Host | mouse |
Clonality | Monoclonal |
Isotype | IgG2b Kappa |
Clone Names | 4G2 |
Calculated MW | 6915 Da |
Gene ID | 10063 |
---|---|
Other Names | Cytochrome c oxidase copper chaperone, COX17 |
Target/Specificity | COX17 (NP_005685, 1 a.a. ~ 63 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa. |
Dilution | WB~~1:500~1000 |
Format | Clear, colorless solution in phosphate buffered saline, pH 7.2 . |
Storage | Store at -20°C or lower. Aliquot to avoid repeated freezing and thawing. |
Precautions | COX17 Antibody (monoclonal) (M01) is for research use only and not for use in diagnostic or therapeutic procedures. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Cytochrome c oxidase (COX), the terminal component of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. This component is a heteromeric complex consisting of 3 catalytic subunits encoded by mitochondrial genes and multiple structural subunits encoded by nuclear genes. The mitochondrially-encoded subunits function in electron transfer, and the nuclear-encoded subunits may function in the regulation and assembly of the complex. This nuclear gene encodes a protein which is not a structural subunit, but may be involved in the recruitment of copper to mitochondria for incorporation into the COX apoenzyme. This protein shares 92% amino acid sequence identity with mouse and rat Cox17 proteins. This gene is no longer considered to be a candidate gene for COX deficiency. A pseudogene COX17P has been found on chromosome 13.
References
1.Dysregulation of intracellular copper homeostasis is common to transgenic mice expressing human mutant superoxide dismutase-1s regardless of their copper-binding abilities.Tokuda E, Okawa E, Watanabe S, Ono SI, Marklund SL.Neurobiol Dis. 2013 Jan 13. doi:pii: S0969-9961(13)00013-2. 10.1016/j.nbd.2013.01.001. [Epub ahead of print]
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