ATP5MD (NM_032747) Human Recombinant Protein
CAT#: 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
View other "ATP5MD" proteins (2)
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CNY 2,040.00
货期*
现货
规格
经常一起买 (1)
Specifications
Product Data | |
Species | Human |
Expression Host | E. coli |
Expression cDNA Clone or AA 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. |
Reference Data | |
RefSeq | NP_116136 |
Locus ID | 84833 |
UniProt ID | Q96IX5 |
Refseq Size | 609 |
Cytogenetics | 10q24.33 |
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 |
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