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

Name: Human MT-ATP8 Recombinant Protein (N-GST & C-His)
Brand: abinScience
SKU: HY325022
Price: 211 USD
Availability: InStock

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Overview

Catalog No.	HY325022
Description	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.
Expression system	E. coli
Accession	P03928
Protein length	Lys27-Ser68
Applications	ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
Species	Homo 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 Names	A6L, ATP synthase F(0) complex subunit 8, ATP8, ATPASE8, F-ATPase subunit 8, MT-ATP8, MTATP8
Background	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
Note	For research use only

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

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

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