Analytical Data
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Gene name
atpG2
- Application
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Alternative Names
(ATP synthase F1 sector gamma subunit 2)(F-ATPase gamma subunit 2)
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Species
Photobacterium profundum
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q6LKZ7
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Expression Region
1-291aa
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Molecular Weight
40.1 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
The ATPG2 protein, a member of the ATP-binding cassette (ABC) transporter family, plays a crucial role in various cellular processes, including energy metabolism and protein transport. Research on ATPG2 is driven by its potential implications in understanding complex diseases, particularly those associated with mitochondrial dysfunction and energy imbalance. Mitochondria serve as the powerhouse of cells, and the proper functioning of ATP transporters is essential for maintaining cellular energy homeostasis. Studies have indicated that mutations or dysregulation of ATPG2 can lead to metabolic disorders and contribute to the pathology of conditions such as neurodegenerative diseases, cancer, and metabolic syndromes. Recombinant ATPG2 protein has emerged as a valuable tool for elucidating its functional mechanism and interactions within cellular pathways. By utilizing advanced techniques such as site-directed mutagenesis and structural biology methods, researchers aim to unravel the detailed molecular architecture of ATPG2, which could pave the way for therapeutic strategies targeting ATPG2-related diseases. As our understanding of ATPG2 deepens, it may also facilitate the development of novel drugs that enhance its function or correct its deficiencies, offering new avenues for treatment in conditions associated with its impairment.
