ATPC1 Protein (AA 23-168) (His-SUMO Tag)
ATPC1
Origin: Human
Host: Escherichia coli (E. coli)
Recombinant
> 90 %
SDS
1 image
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- Target See all ATPC1 Proteins
- ATPC1 (ATP Synthase gamma Chain 1 (ATPC1))
- Protein Type
- Recombinant
- Protein Characteristics
- AA 23-168
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Origin
- Human
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Source
- Escherichia coli (E. coli)
- Purification tag / Conjugate
- This ATPC1 protein is labelled with His-SUMO Tag.
- Application
- SDS-PAGE (SDS)
- Sequence
- AEAAAAPAAA SGPNQMSFTF ASPTQVFFNG ANVRQVDVPT LTGAFGILAA HVPTLQVLRP GLVVVHAEDG TTSKYFVSSG SIAVNADSSV QLLAEEAVTL DMLDLGAAKA NLEKAQAELV GTADEATRAE IQIRIEANEA LVKALE
- Purification
- SDS-PAGE
- Purity
- > 90 %
- Top Product
- Discover our top product ATPC1 Protein
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ATP Synthase gamma Chain 1 (ATPC1) (AA 43-161), (partial) protein (GST tag)
ATPC1 Origin: Human Host: Escherichia coli (E. coli) Recombinant > 90 % SDS
ATP Synthase gamma Chain 1 (ATPC1) (AA 23-168) protein (His tag)ATPC1 Origin: Human Host: Yeast Recombinant > 90 % SDS
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- Application Notes
- Optimal working dilution should be determined by the investigator.
- Restrictions
- For Research Use only
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- Format
- Liquid
- Concentration
- 0.1-2 mg/mL
- Buffer
- 20 mM Tris-HCl based buffer, pH 8.0
- Storage
- -80 °C,4 °C,-20 °C
- Storage Comment
- Store at -20°C, for extended storage, conserve at -20°C or -80°C. Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
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- Target
- ATPC1 (ATP Synthase gamma Chain 1 (ATPC1))
- Alternative Name
- ATPD (ATPC1 Products)
- Synonyms
- T19J18.4 Protein, T19J18_4 Protein, ATPase, F1 complex, gamma subunit protein Protein, ATPC1 Protein
- Background
- Mitochondrial mbrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the mbrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extrambraneous catalytic core, and F0 - containing the mbrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP turnover in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F1 domain and of the central stalk which is part of the complex rotary elent. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
- Molecular Weight
- 31.01 kDa
- UniProt
- P30049
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