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Human ATP5MG Recombinant Protein (N-GST & C-His) (HF744032)

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Aperçu
Numéro de catalogueHF744032
Description
Recombinant Human ATP5MG Protein, N-GST & C-His (HF744032) 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.
Système d'expressionE. coli
Numéro d'accèsO75964
Longueur de protéineAla2-Val103
ApplicationsELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
EspècesHomo sapiens (Human)
Nature Recombinant
Niveau d'endotoxines Please contact with the lab for this information.
Pureté >90% as determined by SDS-PAGE.
Forme Lyophilized
Tampon de stockage Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol.

Reférez-vous aux informations spécifiques sur le tampon dans la copie papier du datasheet ou dans le COA spécifique au lot.

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.
Expédition In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.
Stabilité et stockage 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.
Noms alternatifsATP synthase F(0) complex subunit g, mitochondrial, ATP synthase membrane subunit g, ATP5L, ATP5MG, ATPase subunit g
Contexte

ATP synthase F(0) complex subunit g, mitochondrial is a ~11 kDa protein. Subunit g, 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
Note For research use only
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Reférences
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.)
Recommandation

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