Analytical Data
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Gene name
H2-Ea
- Application
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Alternative Names
H2-Ea；H2-Ea-ps；H-2 class II histocompatibility antigen. E-U alpha chain
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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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AA Sequence
IKEEHTIIQAEFYLLPDKRGEYMFDFDGDEIFHVDIEKSETIWRLEEFAKFASFEAQGALANIAVDKANLDVMKKRSNNTPDANVAPEVTVLSRSPVNLGEPNILVCFIDKFSPPVVNVTWLRNGQPVTEGVSETVFLPRDDHLFRKFHYLTFLPSTDDFYDCEVDHWGLEEPLRKHWEFEEKTLLPETKEN
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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
The study of the H2-Ea recombinant protein is situated at the intersection of immunology and molecular biology, focusing on its pivotal role in the immune response. H2-Ea is a class II major histocompatibility complex (MHC) molecule that is essential for presenting peptide antigens to CD4+ T cells, a critical step in activating adaptive immunity. Understanding the structure and function of H2-Ea is vital for elucidating how the immune system discriminates between self and non-self antigens, which has profound implications in autoimmune diseases, transplant rejection, and vaccine design. Recent advances in recombinant protein technology have enabled the production of H2-Ea in sufficient quantities for detailed biochemical and biophysical studies. Through techniques such as X-ray crystallography and cryo-electron microscopy, researchers aim to map the three-dimensional structure of H2-Ea, providing insights into its peptide-binding groove and interaction with T cell receptors. Moreover, the engineering of H2-Ea variants could facilitate the development of novel immunotherapies and enhance our understanding of T cell activation. As the landscape of immunology evolves, the exploration of H2-Ea is integral to unlocking new therapeutic avenues for combating infectious diseases and cancer, thus making it a significant focus in contemporary biomedical research.
