Analytical Data
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Gene name
H2-Ea
- Application
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Species
Mouse
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P14439
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Expression Region
26-217aa
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Molecular Weight
29.8 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
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Protein Description
H2-Ea recombinant protein is a significant focus in immunological research due to its role in the presentation of antigens to T cells within the major histocompatibility complex (MHC) in mice. The H2-Ea molecule is an MHC class II protein found in the H-2 haplotype, which is crucial for the adaptive immune response, particularly in mediating the recognition of foreign antigens. Understanding the structure and function of H2-Ea is vital for elucidating the mechanisms of T cell activation and tolerance. Studies on H2-Ea recombinant protein aim to define its interactions with peptides and T cell receptors, which is essential for designing effective vaccines and immunotherapies. Furthermore, the H2-Ea protein serves as a model for investigating the effects of genetic variations on immune responses, thereby contributing to our understanding of autoimmune diseases and transplant rejections. By employing techniques such as protein engineering and crystallography, researchers can gain insights into the conformational changes that occur upon antigen binding, enhancing our knowledge of immune system dynamics. Overall, the investigation into H2-Ea recombinant protein plays a crucial role in advancing therapeutics aimed at modulating immune responses for better health outcomes.
