Analytical Data
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Gene name
atpB
- Application
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Alternative Names
atpB;ATP5B;ATPMB;ATPSB;ATP synthase subunit beta. mitochondrial
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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
P06576
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Expression Region
230-529aa
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AA Sequence
YSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGAR ARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAV GYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHL DATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQ DYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHMG KLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEEHSS
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Molecular Weight
53 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 study of ATPB recombinant protein is rooted in its critical role in cellular energy metabolism. ATPB encodes a component of ATP synthase, an essential enzyme complex found in both prokaryotic and eukaryotic organisms, responsible for synthesizing adenosine triphosphate (ATP) during cellular respiration and photosynthesis. ATP, as the primary energy currency of the cell, is fundamental for various biochemical processes necessary for life. Understanding the structure and function of ATPB can provide insights into the mechanisms of energy production and regulation within cells. Moreover, recombinant technology has enabled the production of ATPB in heterologous systems, facilitating detailed studies on its enzymatic activity, interaction with other protein complexes, and the effects of mutations on its function. This research is particularly significant in areas such as bioenergetics, evolutionary biology, and biomedicine, as alterations in ATP synthesis pathways are linked to a range of diseases, including metabolic disorders and mitochondrial dysfunction. By investigating ATPB recombinant protein, scientists aim to unravel its intricate functions and potential applications in biotechnology and therapeutic interventions.











