Analytical Data
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Gene name
vpl1
- Application
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Alternative Names
vpl1；Versatile peroxidase VPL1
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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
Q9UR19
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Expression Region
31-361aa
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AA Sequence
ATCADGRTTANAACCVLFPILDDIQENLFDGAQCGEEVHESLRLTFHDAIGFSPTLGGGGADGSIIAFDTIETNFPANAGIDEIVSAQKPFVAKHNISAGDFIQFAGAVGVSNCPGGVRIPFFLGRPDAVAASPDHLVPEPFDSVDSILARMSDAGFSPVEVVWLLASHSIAAADKVDPSIPGTPFDSTPGVFDSQFFIETQLKGRLFPGTADNKGEAQSPLQGEIRLQSDHLLARDPQTACEWQSMVNNQPKIQNRFAATMSKMALLGQDKTKLIDCSDVIPTPPALVGAAHLPAGFSLSDVEQACAATPFPALTADPGPVTSVPPVPGS
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Molecular Weight
42.0 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
VPL1, or Virus Protein L1, is a recombinant protein derived from certain viral structures, primarily studied for its potential applications in vaccine development and therapeutic interventions. Its significance stems from its role in the viral life cycle, particularly in the assembly and release of viral particles. Research into VPL1 has gained momentum due to the increasing need for effective vaccines against various viral infections, including those responsible for significant public health challenges. By characterizing the structure and function of VPL1, scientists aim to understand how it interacts with host immune systems, which can inform the design of recombinant vaccines that elicit robust immune responses. Additionally, the recombinant production of VPL1 in various expression systems, such as yeast, bacteria, or mammalian cells, allows for the mass production of this protein, which can be utilized in immunological studies and as a potential target for antiviral drug development. The ongoing research on VPL1 not only contributes to the foundational knowledge of viral pathogenesis but also holds promise for innovative strategies in disease prevention and treatment, thereby addressing global health needs.
