Analytical Data
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Gene name
BB3856
- Application
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Alternative Names
BB3856；
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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
P0A321
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Expression Region
22-150aa
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AA Sequence
AECSVDIAGTDQMQFDKKAIEVSKSCKQFTVNLKHTGKLPRNVMGHNWVLTKTADMQAVEKDGIAAGLDNQYLKAGDTRVLAHTKVLGGGESDSVTFDVAKLAAGDDYTFFCSFPGHGALMKGTLKLVD
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Molecular Weight
15.8 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
BB3856 is a recombinant protein derived from the polyomavirus JC virus (JCV), which is known for its role in various neurological diseases, particularly progressive multifocal leukoencephalopathy (PML). PML is an opportunistic infection that predominantly affects immunocompromised individuals, leading to severe neurological deficits due to the lytic infection of oligodendrocytes. The study of BB3856 has gained attention due to its potential implications in understanding JCV pathogenesis and the broader implications in viral oncogenesis and neurovirology. The recombinant nature of BB3856 allows for the exploration of its functional properties, including its interaction with host cells and immune response mechanisms. Research on this protein aims to elucidate the molecular mechanisms underlying JCV infection and its impact on the central nervous system. By investigating the structural and functional characteristics of BB3856, scientists hope to identify novel therapeutic targets and strategies for managing JCV-related diseases. Furthermore, this research contributes to the broader field of virology by providing insights into viral behavior in host organisms and the implications for immunology and neurobiology.
