Analytical Data
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Gene name
H3L
- Application
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Alternative Names
H3L；H3F3C；Histone H3.3C
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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
Q6NXT2
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Expression Region
1-135aa
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AA Sequence
MARTKQTARKSTGGKAPRKQLATKAARKSTPSTCGVKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFNTDLRFQSAAVGALQEASEAYLVGLLEDTNLCAIHAKRVTIMPKDIQLARRIRGERA
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Molecular Weight
15.2 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
The study of H3L recombinant protein has gained significant attention due to its potential applications in immunology and virology. H3L is a gene derived from certain viruses, notably those from the poxvirus family, which plays a crucial role in evading host immune responses. By encoding proteins that inhibit the function of key immune components, such as interferons, H3L can facilitate viral replication and persistence within the host. Researchers are particularly interested in the structural and functional characterization of H3L recombinant protein to understand its mechanisms of action and its interactions with immune pathways. This understanding could lead to novel therapeutic strategies, including vaccine development and antiviral treatments. Furthermore, studying H3L in various model systems could reveal insights into viral pathogenesis and host-virus interactions. The recombinant expression of H3L offers opportunities for high-yield production and detailed biochemical analysis, paving the way for potential applications in biomedicine and biotechnology.
