Analytical Data
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Gene name
calobin
- Application
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Alternative Names
Calobin I (Fibrinogen-clotting enzyme) (Snake venom serine protease) (SVSP) (SVTLE)
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Species
Gloydius ussuriensis
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q91053
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Expression Region
25-262aa
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Molecular Weight
33.7 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
Calobin is a type of recombinant protein that has garnered significant interest in various fields of biotechnology and medicine due to its unique properties and potential applications. Initially discovered in the context of immune response modulation, calobin plays a crucial role in regulating cellular functions, including differentiation, proliferation, and apoptosis. The ability to produce calobin as a recombinant protein allows for large-scale production, enabling researchers to investigate its biological activities and therapeutic potential in greater detail. Studies have shown that calobin can interact with specific cellular receptors, influencing signaling pathways linked to immune responses and inflammation. Moreover, its structural characteristics make it an attractive candidate for drug delivery systems and vaccine development. The pursuit of understanding calobin's mechanisms of action has opened new avenues in treating autoimmune diseases, cancers, and infectious diseases. As research progresses, the recombinant production of calobin expands its applications, paving the way for innovations in therapeutic strategies and enhancing our understanding of protein interactions within biological systems. This growing body of research highlights the significance of calobin in current scientific investigations and its potential impact on future medical advancements.
