Analytical Data
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基因名
HLA-A*02:01&B2M&p53(GLAPPQHLIRV) Monomer
- Application
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别名
HLA-A*0201 & B2M & p53 (GLAPPQHLIRV)
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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
AAA59606.1 (G25-I308)&P61769
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表达区间
AAA59606.1 (G25-I308)&P61769 (I21-M119)&GLAPPQHLIRV
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分子量
40-43 kDa and 10 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
The HLA-A*02:01/B2M/p53(GLAPPQHLIRV) monomer is a significant focus in cancer immunology and vaccine development. HLA-A*02:01 is one of the most prevalent human leukocyte antigen (HLA) class I molecules, playing a critical role in presenting peptide antigens to CD8+ T cells, which are essential for eliciting an immune response against tumors. The p53 protein, a well-known tumor suppressor, is frequently mutated in various cancers, leading to altered peptide sequences, including the specific epitope GLAPPQHLIRV. The study of this monomer involves the recombinant expression of the HLA-A*02:01 complexed with β2-microglobulin (B2M) and the p53-derived peptide, enabling researchers to investigate its structure, binding affinity, and immunogenicity. Understanding the interactions between these components can provide insights into T cell receptor recognition and guide the design of targeted immunotherapies or vaccines aimed at eliciting effective antitumor responses. Moreover, this research may also contribute to the understanding of immune evasion mechanisms employed by tumors, further paving the way for innovative therapeutic strategies.
