Analytical Data
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Gene name
IgG
- Application
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Alternative Names
Ig gamma chain C region; IgG
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Species
Rabbit
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Source
HEK293
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P01870
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Expression Region
C105-K323
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Molecular Weight
28-32 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
Immunoglobulin G (IgG) recombinant proteins have gained significant attention in the fields of biotechnology and medicine due to their critical role in immune responses and therapeutic applications. IgG is the most abundant antibody in the human bloodstream, responsible for neutralizing pathogens and facilitating immune reactions. With advancements in genetic engineering and recombinant DNA technology, scientists can now produce IgG variants in host systems such as bacteria, yeast, or mammalian cells. This enables the generation of highly specific antibodies tailored for diagnostic tools and therapeutic interventions, including treatments for autoimmune diseases, cancers, and infectious diseases. The use of recombinant IgG proteins offers several advantages, such as consistent quality, improved safety profiles, and the ability to modify specific regions for enhanced functionality. Additionally, these proteins serve as valuable tools for research, enabling the study of protein interactions and mechanisms of action in various biological systems. As research continues to evolve, the understanding and application of recombinant IgG proteins are expected to expand, leading to more effective therapies and innovative diagnostic methods. Consequently, the investigation into the structure-function relationships of IgG, along with advancements in production techniques, has the potential to revolutionize the field of immunology and therapeutic drug development.
