Analytical Data
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Gene name
G75V,T76I,SYLTPGD247-253del
- Application
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Alternative Names
(S glycoprotein)(Peplomer protein)(Spike protein S1)(Spike protein S2)
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Species
SARS-CoV-2
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Source
HEK293
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0DTC2
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Expression Region
16-318aa(G75V,T76I,SYLTPGD247-253del)
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Molecular Weight
37.4 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 G75V, T76I, and SYLTPGD247-253del mutations represent significant variants observed in certain proteins that are pivotal for understanding disease mechanisms, particularly in neuromuscular and neurodegenerative disorders. These mutations can alter protein structure and function, potentially leading to aberrant signaling pathways and cellular dysfunction. The G75V and T76I mutations are known to affect the stability and interaction of the protein with its partners, while the deletion of the SYLTPGD247-253 segment has implications for the protein's functional domains. Research into these specific mutations is crucial as they may provide insights into the etiology of conditions such as amyotrophic lateral sclerosis (ALS) and other related neurodegenerative diseases. By studying the biophysical and biochemical properties of the recombinant proteins that harbor these mutations, scientists aim to elucidate their roles in pathogenesis, explore molecular mechanisms of disease, and evaluate their potential as therapeutic targets. Additionally, understanding how these mutations influence protein dynamics and cellular interactions can lead to the development of novel molecular therapies or diagnostic tools, marking a critical advancement in precision medicine for affected patients.
