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HPA021565

Sigma-Aldrich

Anti-SCO1 antibody produced in rabbit

enhanced validation

Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution, Ab1

Synonym(s):

Anti-Protein SCO1 homolog, mitochondrial

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About This Item

UNSPSC Code:
12352203
Human Protein Atlas Number:
NACRES:
NA.43

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

product line

Prestige Antibodies® Powered by Atlas Antibodies

form

buffered aqueous glycerol solution

species reactivity

human

enhanced validation

independent
Learn more about Antibody Enhanced Validation

technique(s)

immunoblotting: 0.04-0.4 μg/mL
immunohistochemistry: 1:200-1:500

immunogen sequence

TREEVDQVARAYRVYYSPGPKDEDEDYIVDHTIIMYLIGPDGEFLDYFGQNKRKGEIAASIATHMRPYR

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... SCO1(6341)

General description

SCO1 (synthesis of cytochrome c oxidase 1) is a protein encoded by SCO1 gene, which is mapped to human chromosome 17p13.1. Human SCO1 is homologous to yeast protein Sco1. This protein is expressed mainly in blood vessels with higher levels in liver. Members of SCO protein family contain a CXXXC copper binding domain that aids in transferring copper to COX (cytochrome c oxidase). Human SCO1is a 301 residue polypeptide consisting of C-terminal domain projecting into the intermembrane space and an N-terminus with mitochondrial targeting signal.

Immunogen

Protein SCO1 homolog, mitochondrial Precursor recombinant protein epitope signature tag (PrEST)

Application

All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project and as a result, are supported by the most extensive characterization in the industry.

The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. We also provide Prestige Antibodies® protocols and other useful information.

Biochem/physiol Actions

SCO1 (synthesis of cytochrome c oxidase) protein plays a vital role in assembly of mitochondrial cytochrome c oxidase (COX) and maintenance of cellular copper (Cu) homeostasis. Copper metallochaperone SCO1 is involved in the maturation of the CuA site of COX2. Mutation of the gene causes mitochondrial encephalocardiomyopathies or hepatopathies.

Features and Benefits

Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.

Every Prestige Antibody is tested in the following ways:
  • IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
  • Protein array of 364 human recombinant protein fragments.

Linkage

Corresponding Antigen APREST75693

Physical form

Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide

Legal Information

Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany

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Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Sonja Brosel et al.
The American journal of pathology, 177(5), 2541-2548 (2010-09-25)
Mammalian SCO1 and SCO2 are evolutionarily-related copper-binding proteins that are required for the assembly of cytochrome c oxidase (COX), a mitochondrial respiratory chain complex, but the exact roles that they play in the assembly process are unclear. Mutations in both
Christopher J Hlynialuk et al.
Cell reports, doi:10-doi:10 (2015-02-17)
Human SCO1 fulfills essential roles in cytochrome c oxidase (COX) assembly and the regulation of copper (Cu) homeostasis, yet it remains unclear why pathogenic mutations in this gene cause such clinically heterogeneous forms of disease. Here, we establish a Sco1
I Valnot et al.
American journal of human genetics, 67(5), 1104-1109 (2000-10-03)
Cytochrome c oxidase (COX) catalyzes both electron transfer from cytochrome c to molecular oxygen and the concomitant vectorial proton pumping across the inner mitochondrial membrane. Studying a large family with multiple cases of neonatal ketoacidotic comas and isolated COX deficiency
John C Williams et al.
The Journal of biological chemistry, 280(15), 15202-15211 (2005-01-22)
Human SCO1 and SCO2 are copper-binding proteins involved in the assembly of mitochondrial cytochrome c oxidase (COX). We have determined the crystal structure of the conserved, intermembrane space core portion of apo-hSCO1 to 2.8 A. It is similar to redox
Myriam Bourens et al.
Human molecular genetics, 23(11), 2901-2913 (2014-01-10)
Cytochrome c oxidase (CIV) deficiency is one of the most common respiratory chain defects in patients presenting with mitochondrial encephalocardiomyopathies. CIV biogenesis is complicated by the dual genetic origin of its structural subunits, and assembly of a functional holoenzyme complex

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