SCO1 Antibody (Center)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, E |
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Primary Accession | O75880 |
Reactivity | Human |
Host | Rabbit |
Clonality | polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 33814 Da |
Gene ID | 6341 |
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Other Names | Protein SCO1 homolog, mitochondrial, SCO1, SCOD1 |
Target/Specificity | This SCO1 antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 125-158 amino acids from the Central region of human SCO1. |
Dilution | WB~~1:2000 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | SCO1 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | SCO1 |
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Synonyms | SCOD1 |
Function | Copper metallochaperone essential for the maturation of cytochrome c oxidase subunit II (MT-CO2/COX2). Not required for the synthesis of MT-CO2/COX2 but plays a crucial role in stabilizing MT- CO2/COX2 during its subsequent maturation. Involved in transporting copper to the Cu(A) site on MT-CO2/COX2 (PubMed:15229189, PubMed:15659396, PubMed:16735468, PubMed:17189203, PubMed:19336478). Plays an important role in the regulation of copper homeostasis by controlling the abundance and cell membrane localization of copper transporter CTR1 (By similarity). |
Cellular Location | Mitochondrion. Mitochondrion inner membrane; Single-pass membrane protein |
Tissue Location | Predominantly expressed in tissues characterized by high rates of oxidative phosphorylation (OxPhos), including muscle, heart, and brain. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Thought to play a role in cellular copper homeostasis, mitochondrial redox signaling or insertion of copper into the active site of COX.
References
Petruzzella V.,et al.Genomics 54:494-504(1998).
Horvath R.,et al.Biochem. Biophys. Res. Commun. 276:530-533(2000).
Peng Y.,et al.Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Mural R.J.,et al.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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