Analytical Data
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Gene name
ELA3A
- Application
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Alternative Names
ELA3A；ELA3；ELA3A；Chymotrypsin-like elastase family member 3A
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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
P09093
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Expression Region
29-270aa
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AA Sequence
VVHGEDAVPYSWPWQVSLQYEKSGSFYHTCGGSLIAPDWVVTAGHCISRDLTYQVVLGEYNLAVKEGPEQVIPINSEELFVHPLWNRSCVACGNDIALIKLSRSAQLGDAVQLASLPPAGDILPNKTPCYITGWGRLYTNGPLPDKLQQARLPVVDYKHCSRWNWWGSTVKKTMVCAGGYIRSGCNGDSGGPLNCPTEDGGWQVHGVTSFVSAFGCNFIWKPTVFTRVSAFIDWIEETIASH
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Molecular Weight
42.6kDa
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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
ELA3A is a recombinant protein that has garnered significant attention in the field of molecular biology and biotechnology due to its potential applications in various therapeutic and diagnostic contexts. Originating from the Venezuelan equine encephalitis virus, ELA3A is a component of the viral early non-structural proteins that play a crucial role in the pathogenesis of viral infections. Research into ELA3A focuses on its enzymatic properties, particularly its ability to function as an efficient protease, which is essential for the processing of viral polyproteins. This processing is vital for the viral life cycle, making ELA3A a target for antiviral drug development. Furthermore, its recombinant expression offers a valuable tool for studying host-pathogen interactions, enabling scientists to explore the mechanisms of viral replication and host immune response. The study of ELA3A is not only pivotal for understanding the biology of Venezuelan equine encephalitis but also provides insights into the broader category of flavivirus-related diseases. Given the increasing incidence of flavivirus outbreaks globally, including Zika and West Nile viruses, the exploration of ELA3A could contribute significantly to the development of novel therapeutic strategies. The ongoing research is also directed towards the engineering of ELA3A for use in vaccine development, enhancing immune responses against viral infections. Overall, the study of ELA3A presents a promising avenue for advancing our understanding of viral pathogenesis and improving public health responses to emerging viral threats.
