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Recombinant Human ATP synthase subunit delta, mitochondrial (ATP5D), partial, Cat#RPC23924

$302.00

Cat#

RPC23924

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Species

Homo sapiens (Human)

Source

E.coli

Tag Info

N-terminal GST-tagged

Biological Activity

Not tested

Estimated Turnaround Time

15-25 business days

Gene Name

ATP5D

Alternative Names

F-ATPase delta subunit

Uniprot

P30049

Expression Region

43-161aa

AA Sequence

ASPTQVFFNGANVRQVDVPTLTGAFGILAAHVPTLQVLRPGLVVVHAEDGTTSKYFVSSGSIAVNADSSVQLLAEEAVTLDMLDLGAAKANLEKAQAELVGTADEATRAEIQIRIEANE

Sequence Info

Partial

Theoretical MW

39.4 kDa

Purity

>90% as determined by SDS-PAGE.

Storage Buffer

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.

Endotoxin Level

Not tested

Shipping Condition

Ice packs

Storage

Short term: -20°C; Long term: -80°C. Minimize freeze and thaw cycles.

Expiry Date

1 year

Research Area

Metabolism

Restriction

For Research Use Only. Not for use in diagnostic procedures. Not for human or animal drug or food use.

Relevance

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.

Function

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 turnover 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(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.

Subcellular location

Mitochondrion, Mitochondrion inner membrane

Protein Families

ATPase epsilon chain family

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