Analytical Data
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Gene name
A33R
- Application
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Alternative Names
A33R；RABS10；Ras-related Protein Rab-33A
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Species
E.coli
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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
P68616
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Expression Region
57-185aa
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AA Sequence
VRLNQCMSANEAAITDAAVAVAAASSTHRKVASSTTQYDHKESCNGLYYQGSCYILHSDYQLFSDAKANCTAESSTLPNKSDVLITWLIDYVEDTWGSDGNPITKTTSDYQDSDVSQEVRKYFCVKTMN
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Molecular Weight
17.8 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
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Protein Description
The A33R protein, a key component derived from the African swine fever virus (ASFV), has garnered significant research interest due to its potential implications in both viral pathogenesis and vaccine development. ASFV is responsible for a highly contagious and lethal disease affecting domestic and wild pigs, leading to substantial economic losses in the swine industry globally. Understanding the molecular mechanisms of ASFV, particularly the role of A33R in immune evasion and viral replication, is crucial for developing effective therapeutic interventions and vaccines. Researchers have identified A33R as a glycoprotein that may play a critical role in the virus's ability to evade the host immune response by interfering with host cell signaling pathways. Studies have indicated that A33R can modulate the host's immune system, fostering an environment conducive to virus survival and replication. Furthermore, exploring the structure and function of A33R could facilitate the design of recombinant proteins for use in diagnostic tools or as potential vaccine candidates. Given the urgency in addressing ASFV, particularly in light of recent outbreaks, the study of A33R is not only vital for understanding ASFV biology but also holds promise for bolstering biosecurity measures in livestock management. As such, research on A33R encompasses a multidisciplinary approach, integrating virology, immunology, and molecular biology, paving the way for innovative strategies to combat this devastating pathogen.
