Analytical Data
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Gene name
Scyb11
- Application
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Alternative Names
Interferon-inducible T-cell alpha chemoattractant ;I-TACSmall-inducible cytokine B11
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Species
Mouse
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Source
E. coli
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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
Q9JHH5
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Expression Region
22-98aa
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Molecular Weight
12.9 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
Scyb11, a member of the scylla family of proteins, has garnered attention due to its potential role in various biological processes and its applications in biotechnology and medicine. Research into Scyb11 has revealed its involvement in crucial cellular functions, including cell signaling, stress responses, and regulation of gene expression. The recombinant production of Scyb11 protein has become essential for studying its structural and functional properties, which are vital for understanding its mechanism of action. The use of recombinant DNA technology allows for the efficient expression of Scyb11 in various host organisms, facilitating large-scale production and subsequent purification of the protein. This enables researchers to conduct detailed biochemical assays, structural analyses, and functional experiments to elucidate the protein's role in cellular processes. Moreover, insights gained from Scyb11 research could lead to the development of novel therapeutic strategies for diseases linked to dysregulation of the pathways involving this protein. As such, the exploration of Scyb11 as a recombinant protein not only advances fundamental biology but also holds promise for practical applications in drug development and biotechnological innovations. Overall, understanding Scyb11's properties and functions could contribute significantly to the broader fields of molecular biology and therapeutics.
