Analytical Data
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Gene name
ATP5SL
- Application
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Alternative Names
DMAC2; ATP5SLDistal membrane-arm assembly complex Protein 2; ATP synthase subunit s-like Protein
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NW81
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Expression Region
1-257aa
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AA Sequence
MAAPWASLRL VAPMWNGRIR GIHRLGAAVA PEGNQKKKRT ILQFLTNYFY DVEALRDYLL QREMYKVHEK NRSYTWLEKQ HGPYGAGAFF ILKQGGAVKF RDKEWIRPDK YGHFSQEFWN FCEVPVEAVD AGDCDINYEG LDNLLRLKEL QSLSLQRCCH VDDWCLSRLY PLADSLQELS LAGCPRISER GLACLHHLQN LRRLDISDLP AVSNPGLTQI LVEEMLPNCE VVGVDWAEGL KSGPEEQPRD TASPVPA
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Molecular Weight
29.2 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
ATP5SL is a crucial component of the ATP synthase complex, which plays a vital role in cellular energy production through oxidative phosphorylation. This protein is associated with mitochondrial function and is implicated in various cellular processes, including ATP generation, reactive oxygen species management, and apoptosis regulation. Research on ATP5SL has gained momentum due to its potential implications in understanding mitochondrial diseases and metabolic disorders. Variations or malfunctions in ATP5SL expression and activity have been linked to conditions such as neurodegenerative diseases, muscle disorders, and certain types of cancer. Consequently, the recombinant expression and characterization of ATP5SL are essential for elucidating its functional roles and interactions within the mitochondrial enzyme complex. Through techniques such as molecular cloning, expression in heterologous systems, and subsequent purification, researchers aim to determine the biochemical properties and functional significance of ATP5SL. The findings from these studies could offer insights into therapeutic targets and strategies for managing diseases associated with mitochondrial dysfunction, thus advancing both basic research and clinical applications in the field of bioenergetics.
