Analytical Data
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Gene name
col
- Application
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His-SUMO
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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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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 recombinant proteins are a focal point of research due to their significant roles in various biological processes, including cell adhesion, signaling, and tissue repair. Derived from collagen, the most abundant protein in mammals, Col proteins are vital for maintaining the structural integrity of tissues. In recent years, advances in genetic engineering and recombinant DNA technology have enabled the production of Col proteins in various systems, offering a sustainable and scalable alternative to traditional extraction methods from animal sources. This innovation is crucial, as the demand for collagen-based products in biomedical applications, such as wound healing, drug delivery, and tissue engineering, continues to rise. Furthermore, recombinant Col proteins present opportunities for developing tailored biomaterials with enhanced properties, addressing specific clinical needs while minimizing ethical concerns associated with animal-derived products. Researchers are actively exploring different recombinant expression systems, including bacteria, yeast, and mammalian cells, to optimize production efficiency and functionality. Additionally, studies on the structural and functional characteristics of these recombinant proteins are essential for understanding their interactions at the cellular level, paving the way for innovative therapeutic applications and improved health outcomes. Overall, the ongoing research into Col recombinant proteins signifies a promising advancement in biomaterial science and regenerative medicine, holding potential for breakthroughs in treating various conditions and improving quality of life.
