ACO2 Protein (GST Tag)

Aconitase 2, mitochondrial Protein Datasheet

ACO2 Protein Product Information

• Synonym: ACONM, MGC20605, MGC33908
• Protein Construction: A DNA sequence encoding the human ACO2 (Q99798) (Gln 28-Gln 780) was fused with the N-terminal polyhistidine-tagged GST tag at the N-terminus.
• Source: Human
• Expression Host: Baculovirus-Insect cells

ACO2 Protein QC Testing

• Purity: > 85 % as determined by SDS-PAGE.
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method
• Stability: Samples are stable for up to twelve months from date of receipt at -70℃
• Predicted N terminal: Met
• Molecular Mass: The recombinant human ACO2/GST chimera consists of 990 amino acids and migrates as an approximately 110 KDa band in SDS-PAGE under reducing conditions as predicted.
• Formulation: Lyophilized from sterile 20mM Tris, 500mM NaCl, 10%glycerol, pH 8.0, 0.3mM DTT
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.
• SDS-PAGE: ACO2 protein

ACO2 Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

ACO2 Protein Description

Aconitase employs a cluster to catalyze the stereospecific dehydration-rehydration of citrate to isocitrate via cis-aconitase in the second and third steps of the Krebs cycle. The protein contains four domains. Residues from all four domains contribute to the active site region, which is defined by the Fe[BOND]S cluster. Three of these side chains reside on a three turn 310 helix in the first domain. Diseases relevant to aconitase are aconitase deficiency, Friedreich's ataxia (FRDA), and diabetes. Aconitase deficiency is caused by mutation in the gene for iron-sulfur cluster scaffold protein, which helps to form the Fe-S cluster. FRDA is caused when the Fe-S proteins in aconitase and succinate dehydrogenase have decreased activity. ACO2 is the mitochondrial form of aconitase different from the soluble form ACO1.

References

1. Robbins AH. et al., 1989, Proteins. 5 (4): 289-312.
2. Lauble H. et al., 1992, Biochemistry. 31 (10): 2735-48.
3. Robbins AH. et al., 1989, Proc Natl Acad Sci. 86 (10): 3639-43.