Analytical Data
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Gene name
ATP6V1F
- Application
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Alternative Names
ATP6V1F；ATP6S14；VATF；V-type proton ATPase subunit F
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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
Q16864
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Expression Region
1-119aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAGRGKL IAVIGDEDTV TGFLLGGIGE LNKNRHPNFL VVEKDTTINE IEDTFRQFLN RDDIGIILIN QYIAEMVRHA LDAHQQSIPA VLEIPSKEHP YDAAKDSILR RARGMFTAED LR
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Molecular Weight
16 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
ATP6V1F is a vital component of the V-ATPase (vacuum-type ATPase) enzyme complex, which plays a critical role in cellular pH regulation, protein sorting, and nutrient transport across cellular membranes. This enzyme is pivotal in various physiological processes, including bone resorption, neurotransmitter release, and the maintenance of acid-base balance. Disruptions in V-ATPase activity have been linked to several diseases, such as osteopetrosis, renal tubular acidosis, and cancer, highlighting the importance of understanding its function and regulation. Recent advancements in recombinant protein technology have enabled the production of ATP6V1F in host systems, facilitating detailed structural and functional studies. Research into the recombinant form of ATP6V1F aims to elucidate its biochemical properties, interaction with other subunits of the V-ATPase complex, and its role in pathological conditions. Such studies are essential for developing potential therapeutic strategies that target V-ATPase activity, offering new avenues for treating diseases associated with its dysregulation.
