Analytical Data
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Gene name
IgG1
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简介
The IgG1 protein is the constant region of the immunoglobulin heavy chain and serves as a receptor during the recognition phase of humoral immunity. It triggers clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. IgG1 Protein, Human (C103S, M135Y, S137T, T139E, H316K, N317F, HEK293, His) is the recombinant human-derived IgG1 protein, expressed by HEK293, with C-His labeled tag.
- Application
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Alternative Names
Ig gamma-1 chain C region; IGHG1
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Species
Human
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Source
HEK293
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Tag
C-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P01857-1
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Expression Region
E99-K330, C103S, M135Y, S137T, T139E, H316K, N317F
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Molecular Weight
33-35 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
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Protein Description
IgG1 recombinant proteins play a crucial role in various biomedical applications, particularly in immunology and therapeutic development. Immunoglobulin G (IgG) is the most abundant antibody type in serum, with IgG1 being the predominant subclass in humans, known for its ability to effectively neutralize pathogens and activate various immune responses. The recombinant production of IgG1 proteins enables researchers to generate well-defined, high-purity antibodies for diagnostic and therapeutic uses. Advances in recombinant DNA technology, particularly the use of mammalian cell systems for expression, have significantly improved the yield and functionality of IgG1 proteins. These engineered antibodies are essential for the development of targeted therapies, especially in the treatment of cancers, autoimmune diseases, and infectious diseases. Additionally, the engineering of IgG1 to improve its properties, such as stability and binding affinity, has become a focus of research, allowing for the creation of bispecific antibodies and antibody-drug conjugates that enhance therapeutic efficacy while minimizing side effects. Understanding the structure-function relationship of IgG1 recombinant proteins is vital for optimizing their use in clinical settings, making this area of research not only scientifically intriguing but also of significant therapeutic relevance.
