Analytical Data
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Gene name
col
- Application
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Alternative Names
col；Colipase
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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
P18000
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Expression Region
74-180aa
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AA Sequence
LAKNKGKIPGLKIDQKIRGQMPERGWTEDDIKNTVSNGATGTSFDKRSPKKTPPDYLGRNDPATVYGSPGKYVVVNDRTGEVTQISDKTDPGWVDDSRIQWGNKNDQ
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Molecular Weight
24.8 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
Col recombinants, particularly in the context of protein research, refer to proteins that are engineered through recombinant DNA technology. This approach has become significant due to its ability to produce large quantities of proteins that can be used for various applications, including therapeutic agents, vaccines, and enzyme production. The background of Col recombinant protein research lies in the advancements of molecular biology techniques, such as cloning, expression systems, and purification methods. These innovations have enabled scientists to isolate specific genes that encode for desired proteins and insert them into host organisms, such as bacteria, yeast, or mammalian cells, to express the protein efficiently. Furthermore, understanding protein structure and function has opened avenues for designing proteins with enhanced characteristics, driving interest in fields such as biotechnology and pharmaceutical development. As scientists delve deeper into the intricacies of protein interactions, post-translational modifications, and folding mechanisms, Col recombinant protein studies continue to contribute significantly to the understanding of biological processes and the development of novel therapeutic strategies. Overall, the exploration of Col recombinant proteins is pivotal in addressing complex health challenges and advancing biotechnological applications.
