ATP5MF蛋白|人ATP5MF蛋白|人ATP5MF重组蛋白

Research Areas

Others

Uniprot ID

P56134

Gene Names

ATP5MF

Alternative Name(s)

(ATP synthase membrane subunit f)

Lead Time

3-7 business days

Organism

Homo sapiens (Human)

Source

in vitro E.coli expression system

Expression Region

1-94aa

Protein Length

Full Length

Tag Info

N-terminal 10xHis-tagged

Target Protein Sequence

MASVGECPAPVPVKDKKLLEVKLGELPSWILMRDFSPSGIFGAFQRGYYRYYNKYINVKKGSISGITMVLACYVLFSYSFSYKHLKHERLRKYH

MW

12.4 kDa

Purity

Greater than 90% as determined by SDS-PAGE.

Endotoxin

Not test.

Biological_Activity

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Form

Liquid or Lyophilized powder

Buffer

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Storage

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.

Relevance

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. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane.

Function

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