ATP5MD (NM_032747) Human Recombinant Protein

SKU TP761123

Purified recombinant protein of Human up-regulated during skeletal muscle growth 5 homolog (mouse) (USMG5), transcript variant 2, full length, with N-terminal HIS tag, expressed in E. coli, 50ug

Product Data

• Species: Human
• Expression Host: E. coli
• Expression cDNA Clone or AA Sequence:
  Protein Sequence

  A DNA sequence encoding human full-length USMG5
• Tag: N-His
• Predicted MW: 6.3 kDa
• Concentration: >0.05 µg/µL as determined by microplate BCA method
• Purity: > 80% as determined by SDS-PAGE and Coomassie blue staining
• Buffer: 25 mM Tris-HCl, pH 8.0, 150 mM NaCl, 1% sarkosyl, 10% glycerol
• Note: For testing in cell culture applications, please filter before use. Note that you may experience some loss of protein during the filtration process.
• Storage: Store at -80°C.
• Stability: Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles.
• Shipping: Dry Ice

Reference Data

• RefSeq: NP_116136
• Locus ID: 84833
• UniProt ID: Q96IX5
• Cytogenetics: 10q24.33
• RefSeq Size: 609
• RefSeq ORF: 174
• Synonyms: bA792D24.4; DAPIT; HCVFTP2; MC5DN6; USMG5
• Summary: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (Probable). Minor subunit required to maintain the ATP synthase population in the mitochondria (PubMed:21345788).[UniProtKB/Swiss-Prot Function]
• Protein Families: Transmembrane