Analytical Data
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基因名
HLA-C*07:02:01&B2M Monomer
- Application
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别名
HLA-C*070201 & B2M
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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
P10321-1 (C25-I308)&P61769
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表达区间
P10321-1 (C25-I308)&P61769 (I21-M119)
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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
HLA-C*07:02:01 is a highly polymorphic class I major histocompatibility complex (MHC) molecule critical for immune response regulation, presenting peptide antigens to CD8+ T cells. Its association with various autoimmune diseases and its role in determining transplant compatibility underscore the importance of understanding its structure and function. Beta-2-microglobulin (B2M) is an essential component of MHC class I molecules, stabilizing their structure and facilitating the presentation of peptides. The study of HLA-C*07:02:01 complexed with B2M as a monomeric recombinant protein offers insights into its antigen presentation mechanism, the implications of its polymorphism on T cell activation, and the potential for targeted therapeutic approaches. This research is particularly significant in the context of vaccine development and immunotherapy, where knowledge of specific peptide-MHC interactions can enhance therapeutic efficacy and minimize adverse effects. By elucidating this complex's structural and functional characteristics, we can better understand individual immune responses and their implications for health and disease.
