Recombinant Human Protein Sco2 Homolog, Mitochondrial (SCO2) Protein (His-SUMO)

Name: Recombinant Human Protein Sco2 Homolog, Mitochondrial (SCO2) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09855P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Protein Sco2 Homolog, Mitochondrial (SCO2) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O43819
Target Symbol	SCO2
Synonyms	Cytochrome oxidase deficient homolog 2; MGC125823; MGC125825; OTTHUMP00000196774; OTTHUMP00000196775; Protein SCO2 homolog; mitochondrial; SCO (cytochrome oxidase deficient; yeast) homolog 2; SCO 1L; SCO 2; SCO cytochrome oxidase deficient homolog 2 (yeast); SCO cytochrome oxidase deficient homolog 2; SCO1L; SCO2; SCO2_HUMAN; Synthesis of cytochrome c oxidase 2
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	PAETGGQGQPQGPGLRTRLLITGLFGAGLGGAWLALRAEKERLQQQKRTEALRQAAVGQGDFHLLDHRGRARCKADFRGQWVLMYFGFTHCPDICPDELEKLVQVVRQLEAEPGLPPVQPVFITVDPERDDVEAMARYVQDFHPRLLGLTGSTKQVAQASHSYRVYYNAGPKDEDQDYIVDHSIAIYLLNPDGLFTDYYGRSRSAEQISDSVRRHMAAFRSVLS
Expression Range	43-266aa
Protein Length	Full Length of Mature Protein
Mol. Weight	41.1kDa
Research Area	Metabolism
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Copper metallochaperone essential for the synthesis and maturation of cytochrome c oxidase subunit II (MT-CO2/COX2). Involved in transporting copper to the Cu(A) site on MT-CO2/COX2. Also acts as a thiol-disulfide oxidoreductase to regulate the redox state of the cysteines in SCO1 during maturation of MT-CO2/COX2.
Subcellular Location	Mitochondrion inner membrane; Single-pass membrane protein.
Protein Families	SCO1/2 family
Database References	HGNC: 10604 OMIM: 256000 KEGG: hsa:9997 STRING: 9606.ENSP00000252785 UniGene: Hs.180903
Associated Diseases	Cardioencephalomyopathy, fatal infantile, due to cytochrome c oxidase deficiency 1 (CEMCOX1); Myopia 6 (MYP6); Leigh syndrome (LS)
Tissue Specificity	Ubiquitous.

Gene Functions References

We identified one novel possibility of an extreme myopia-causing mutation in SCO2. No other disease-causing mutation was found in 101 extremely myopic Japanese patients, suggesting that SCO2 plays a limited role in Japanese extreme myopia. PMID: 27052445
In gastric cancer, the expression of SCO2 and COX were not shown to be associated with the regulatory role of p53, unlike TIGAR expression. Nevertheless, a significantly high recurrence rate was found in a patient group with high COX expression PMID: 27499152
oxidative stress-induced glycolysis-to-OXPHOS switch is mediated by synthesis of cytochrome c oxidase 2 (SCO2). These findings demonstrate p53-mediated OXPHOS function as a compensatory alteration in Fanconi anemia (FA)hematopoietic stem cells to ensure a functional but mildly impaired energy metabolism and suggest a cautious approach to manipulating p53 signaling in FA. PMID: 26676373
Geranylgeranoic acid increased the SCO2 gene expression, which might enhance aerobic respiration. PMID: 26700591
oncoprotein HBXIP enhances glucose metabolism reprogramming through suppressing SCO2 and PDHA1 in breast cancer PMID: 26309161
Cooperation between COA6 and SCO2 in COX2 maturation during cytochrome c oxidase assembly links two mitochondrial cardiomyopathies. PMID: 25959673
Sco1 is a metallochaperone that selectively transfers Cu(I) ions based on loop recognition, whereas Sco2 is a copper-dependent thiol reductase of the cysteine ligands in the oxidase. PMID: 26351686
Letter/Case Report: SCO2 mutations resulting in Leigh disease revealed at autopsy. PMID: 25720770
mutation in LRPAP1 is associated with high myopia. Further studies are expected to evaluate the pathogenicity of the variants in CTSH, LEPREL1, ZNF644, SLC39A5, and SCO2. PMID: 25525168
COX20 cooperates with SCO1 and SCO2 to mature COX2 and promote the assembly of cytochrome c oxidase. PMID: 24403053
alpha-particle-induced bystander effect is regulated by p53 and its downstream SCO2 in the irradiated hepatoma cells PMID: 23786650
oroxylin A could increase protein and mRNA expression of TP53-induced glycolysis and apoptosis regulator (TIGAR) and synthesis of cytochrome c oxidase 2 (SCO2), which are the key metabolic modulators regulated by p53. PMID: 23612020
Autosomal recessive mutations in SCO2 are known to be associated with COX deficiency recognized as fatal infantile cardio-encephalomyopathy PMID: 23364397
Exogenous addition of the SCO2 gene to hypoxic cancer cells and hypoxic tumors induces apoptosis. PMID: 23319048
Mutations in SCO2 are associated with autosomal-dominant high-grade myopia. PMID: 23643385
Analysis of the mtDNA revealed that COX deficiency is caused by high levels of mtDNA deletions which accumulate with age in alzheimer disease. PMID: 21925769
wild-type p53 gene silencing reduced the expression of synthesis of cytochrome c oxidase 2 (SCO2), an effector necessary for respiratory chain function PMID: 22120717
These results suggest that p53 can modulate the metabolic pathways via the proteins SCO2 and TIGAR in human breast cancer. PMID: 21820150
Results describe the tissue distribution of SCO1 and SCO2 in mouse and human tissues. PMID: 20864674
Mutations of SCO2 gene should be considered as a possible cause of neurogenic skeletal muscle features (including SMA-like) in infants with encephalomyopathy even in the absence of heart involvement and COX deficit. PMID: 19879173
recombinant fusion L-Sco2 protein was successfully transduced into the mitochondria of primary fibroblasts derived from SCO2/COX deficient patient and facilitated recovery of COX activity PMID: 20193760
Mutations can cause fatal cytochrome c oxidase deficiency. Affected myoblasts can be rescued in vitro by transduction of the normal SCO2 gene or by copper administration. PMID: 11751685
Copper supplementation restores cytochrome c oxidase activity in cultured cells from patients with SCO2 mutations. PMID: 11931660
One novel SCO2 mutation has been identified in a patient with hypertrophic cardiomyopathy. PMID: 12538779
SCO2 mutation is associated spinal muscular atrophy type I phenotype PMID: 14994243
SCO2 transfers copper to the CuA site at an early stage of COX assembly in mitochondria. PMID: 15229189
The consequences of SCO2 and SURF1 mutations suggest the existence of tissue-specific functional differences of these proteins that may serve different tissue-specific requirements for the regulation of COX biogenesis. PMID: 16083427
data suggest that both Cu(I) and Cu(II) binding are critical for normal Sco function. PMID: 16091356
findings show that p53 modulates the balance between the utilization of respiratory and glycolytic pathways; identifed Synthesis of Cytochrome c Oxidase 2 (SCO2) as the downstream mediator of this effect PMID: 16728594
These results suggest a mitochondrial pathway for the regulation of cellular copper content that involves signaling through SCO1 and SCO2, perhaps by their thiol redox or metal-binding state. PMID: 17189203
structural and metal binding features of human Cu(I)Sco2 are similar to the Sco1 homolog, although the dynamic properties and the conformational disorder are quite different when apo forms and the copper(I)-loaded forms of the two proteins are compared PMID: 17850752
report extends knowledge of the pathology of COX deficiency caused by mutations in the SCO2 gene PMID: 18254779
Spinal muscular atrophy has been associated with mtDNA depletion or with mutations in the cytochrome-c oxidase assembly gene (SCO2; OMIM 604377). PMID: 18332255
Mutations in the SCO2 gene are a cause of prenatal-onset hypertrophic cardiomyopathy. PMID: 18924171
SCO2 acts upstream of SCO1, and that it is indispensable for CO II synthesis. PMID: 19336478
observations confirm that mutations in the SCO2 gene are frequently associated with the neurogenic pattern of skeletal muscle involvement accompanied by mitochondrial abnormalities PMID: 19353431

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.