Analytical Data
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Gene name
ATP6V1D
- Application
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Alternative Names
ATP6V1D; ATP6M; VATD; V-type proton ATPase subunit D
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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
Q9Y5K8
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Expression Region
1-247aa
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AA Sequence
MSGKDRIEIF PSRMAQTIMK ARLKGAQTGR NLLKKKSDAL TLRFRQILKK IIETKMLMGE VMREAAFSLA EAKFTAGDFS TTVIQNVNKA QVKIRAKKDN VAGVTLPVFE HYHEGTDSYE LTGLARGGEQ LAKLKRNYAK AVELLVELAS LQTSFVTLDE AIKITNRRVN AIEHVIIPRI ERTLAYIITE LDEREREEFY RLKKIQEKKK ILKEKSEKDL EQRRAAGEVL EPANLLAEEK DEDLLFE
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Molecular Weight
52.91 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
ATP6V1D is a vital subunit of the V-ATPase (vacuolar-type H+-ATPase) complex, which plays a crucial role in various cellular processes by mediating the transport of protons across cellular membranes. This proton pump is essential for maintaining pH homeostasis, regulating ion gradients, and facilitating nutrient uptake in eukaryotic cells. Research has shown that V-ATPase, and specifically the ATP6V1D subunit, is involved in diverse physiological functions including endocytosis, receptor-mediated signaling, and bone resorption, indicating its importance in both normal cellular function and pathological conditions such as cancer and osteoporosis. The overexpression or dysregulation of ATP6V1D has been associated with tumor progression and metastasis, making it a potential target for therapeutic intervention. To better understand its function and implications in disease, recombinant ATP6V1D protein is often studied in vitro and in vivo, enabling researchers to elucidate its molecular mechanisms and develop strategies for modulating its activity. The production and study of this recombinant protein are therefore critical for advancing our knowledge of V-ATPase's role in health and disease.
