Analytical Data
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Gene name
ATP5G3
- Application
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Alternative Names
MFACAKLACTPSLIRAGSRVAYRPISASVLSRPEASRTGEGSTVFNGAQNGVSQLIQREFQTSAISRDIDTAAKFIGAGAATVGVAGSGAGIGTVFGSLIIGYARNPSLKQQLFSYAILGFALSEAMGLFCLMVAFLILFAM
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P48201
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Expression Region
1-142aa
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AA Sequence
MFACAKLACTPSLIRAGSRVAYRPISASVLSRPEASRTGEGSTVFNGAQNGVSQLIQREFQTSAISRDIDTAAKFIGAGAATVGVAGSGAGIGTVFGSLIIGYARNPSLKQQLFSYAILGFALSEAMGLFCLMVAFLILFAM
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Molecular Weight
41.1 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
ATP5G3, a subunit of the ATP synthase complex, plays a crucial role in mitochondrial function and energy production within eukaryotic cells. Research into ATP5G3 has gained momentum due to its involvement in various cellular processes and its potential implications in health and disease. This protein is known to influence oxidative phosphorylation, the primary mechanism by which cells convert nutrients into adenosine triphosphate (ATP), the energy currency of the cell. Dysregulation of ATP5G3 has been linked to several disorders, including neurodegenerative diseases and certain cancers, highlighting its importance in both normal physiology and pathological conditions. The recombination and expression of ATP5G3 in model systems enable researchers to investigate its biochemical properties and interactions with other mitochondrial components. Studies employing recombinant ATP5G3 have provided insights into its functional roles and may aid in the development of therapeutic strategies aimed at correcting mitochondrial dysfunction. Additionally, understanding the structure-function relationship of ATP5G3 can pave the way for innovative drug designs targeting mitochondrial-related diseases. Thus, ATP5G3-recombinant protein research is a pivotal area of investigation that bridges fundamental biology with translational medical applications, underscoring the importance of this protein in cellular bioenergetics and human health.
