Analytical Data
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基因名
HLA-A*24:02&B2M&EBV EBNA3A(RYSIFFDYM) Monomer
- Application
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别名
HLA-A*2402 & B2M & EBV EBNA3A (RYSIFFDYM)
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种属
Human
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表达系统
HEK293
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标签
C-Avi;C-His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
AAA59600.1 (G25-T305)&P61769
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表达区间
AAA59600.1 (G25-T305)&P61769 (I21-M119)&RYSIFFDYM
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分子量
40-43 kDa and 12 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
HLA-A*24:02 is a prevalent human leukocyte antigen (HLA) class I molecule, particularly associated with certain autoimmune diseases and cancers in East Asian populations. Understanding its interaction with various peptides is crucial for advancing immunotherapy and vaccine design. Among the peptides presented by HLA-A*24:02, EBV (Epstein-Barr Virus) EBNA3A (specifically the peptide RYSIFFDYM) is of significant interest due to its role in viral persistence and its potential as a target for T cell-based therapies. The combination of HLA-A*24:02 and the peptide can provide insights into T cell receptor (TCR) recognition and specificity, which is vital for developing effective immunotherapeutic strategies against EBV-associated malignancies. Recombinant protein studies of the HLA-A*24:02, beta-2-microglobulin (B2M), and EBNA3A complex allow for the exploration of structural and functional aspects of the peptide-MHC interaction. These investigations can enhance our understanding of the immune response mechanisms and facilitate the design of targeted therapies for diseases related to EBV, thereby contributing to the broader field of immunology and personalized medicine.
