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Human MT-ATP8 Recombinant Protein (N-GST & C-His) (HY325022)

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Vista general
Número de catálogoHY325022
Descripción
Recombinant Human MT-ATP8 Protein, N-GST & C-His (HY325022) 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.
Sistema de expresiónE. coli
Número de accesoP03928
Longitud de proteínaLys27-Ser68
AplicacionesELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
EspeciesHomo sapiens (Human)
Naturaleza Recombinant
Nivel de endotoxinas Please contact with the lab for this information.
Pureza >90% as determined by SDS-PAGE.
Forma Lyophilized
Buffer de almacenamiento Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol.

Consulte la información específica del buffer en la copia impresa del datasheet o en el COA específico del lote.

Reconstitución Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details.
Envío In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.
Estabilidad y almacenamiento 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.
Nombres alternativosA6L, ATP synthase F(0) complex subunit 8, ATP8, ATPASE8, F-ATPase subunit 8, MT-ATP8, MTATP8
Fondo

ATP synthase F(0) complex subunit 8 is a ~7 kDa protein. Subunit 8, 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. 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). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro.

1. Lai, Y. et al. (2023) Molecular cell 83, 2137-2147.e4. PMID: 37244256
Nota 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
×
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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