Analytical Data
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Gene name
Igfl
- Application
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Species
Mouse
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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
Q6B9Z0
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Expression Region
25-140aa
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Molecular Weight
26.1 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
IgFL (Immunoglobulin-like fold protein) recombinant proteins have garnered significant attention in the field of biomedicine due to their potential applications in immunotherapy and diagnostics. These proteins, characterized by their immunoglobulin-like domains, exhibit unique structural and functional properties that make them appealing for various therapeutic applications. Research indicates that IgFL proteins can modulate immune responses, making them candidates for developing novel treatments for autoimmune diseases, cancer, and infectious diseases. The use of recombinant DNA technology allows for the production of these proteins in a controlled environment, ensuring reproducibility and purity for experimental studies. Scientists are exploring the mechanisms by which IgFL proteins interact with immune cells, as well as their ability to enhance or inhibit specific immune pathways. Furthermore, the engineering of IgFL proteins to improve their stability and binding affinity is a focus of ongoing research, with the aim of creating more effective therapeutics. As a result, understanding the biology of IgFL proteins not only advances our knowledge of immune regulation but also paves the way for innovative approaches to combat various diseases. The collaborative efforts in structural biology, molecular engineering, and clinical research continue to expand the potential of IgFL recombinant proteins in modern medicine.
