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Human MT-ATP6 Recombinant Protein (N-GST & C-His) (HD823012)

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Overview
Catalog No.HD823012
Description
Recombinant Human MT-ATP6 Protein, N-GST & C-His (HD823012) expressed in E. coli. Purity: >90% as determined by SDS-PAGE..
Highlights
  • E. coli Expression — High-yield, cost-effective production.
  • High Purity — >90% as determined by SDS-PAGE.
Expression systemE. coli
AccessionP00846
Protein lengthPhe26-Trp68&Phe117-Ile138&Ile209-Thr226
ApplicationsELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
SpeciesHomo sapiens (Human)
Nature Recombinant
Endotoxin level Please contact with the lab for this information.
Purity >90% as determined by SDS-PAGE.
Form Lyophilized
Storage buffer Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol.

Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.

Reconstitution Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details.
Shipping In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.
Stability and Storage Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt.
Alternate NamesATP synthase F(0) complex subunit a, ATP6, ATPASE6, F-ATPase protein 6, MT-ATP6, MTATP6, Proton-conducting channel, ATP synthase F(0) complex subunit a
Background

ATP synthase F(0) complex subunit a is a ~24 kDa protein. Subunit a, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that 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 (Probable). ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel. These two domains are linked by a central stalk rotating inside the F(1) region and a stationary 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). With the subunit c (ATP5MC1), forms the proton-conducting channel in the F(0) domain, that contains two crucial half-channels (inlet and outlet) that facilitate proton movement from the mitochondrial intermembrane space (IMS) into the matrix.

1. Lai, Y. et al. (2023) Molecular cell 83, 2137-2147.e4. PMID: 37244256
Note For research use only
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Formula
Mass (g) = Concentration (mol/L) × Volume (L) × MW (g/mol)
Enter any 2 of Mass, Concentration, Volume + Molecular Weight to solve for the unknown.
Mass
=
Concentration
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Volume
Molecular Weight *
g/mol
Formula
C₁ × V₁ = C₂ × V₂
Enter any 3 of the 4 values to solve for the unknown.
Stock Solution
C₁ (Stock Conc.)
×
V₁ (Stock Vol.)
=
Working Solution
C₂ (Working Conc.)
×
V₂ (Working Vol.)
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