Analytical Data
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Gene name
p30
- Application
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Alternative Names
p30；RNASEP2；Ribonuclease P Protein subunit p30
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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
O14931-1
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Expression Region
19-135aa
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AA Sequence
LWVSQPPEIRTLEGSSAFLPCSFNASQGRLAIGSVTWFRDEVVPGKEVRNGTPEFRGRLAPLASSRFLHDHQAELHIRDVRGHDASIYVCRVEVLGLGVGTGNGTRLVVEKEHPQLG
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Molecular Weight
41.8 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
Related Products
Protein Description
The P30 protein, derived from various plant viruses, has garnered significant attention in the field of molecular biology and plant pathology due to its multifaceted roles in viral replication and host interaction. This protein is particularly notable for its involvement in viral movement within plant tissues, facilitating the spread of the virus and enhancing pathogenicity. Studies have shown that P30 can interact with host proteins, modulating the plant's immune responses and allowing the virus to evade detection. Researchers have focused on understanding the molecular mechanisms underlying these interactions, as well as the potential applications of P30 in biotechnology, such as developing disease-resistant plant varieties or using it as a tool for protein engineering. Furthermore, the expression and characterization of P30 as a recombinant protein have been explored to elucidate its structure-function relationships and to investigate its potential as a target for antiviral strategies. This research has far-reaching implications not only for combating viral infections in crops but also for advancing our knowledge of plant-virus interactions and enhancing agricultural productivity.
