Analytical Data
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基因名
HLA-B*27:05&B2M Monomer
- Application
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别名
HLA-B*2705 & 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
ACR83851.1 (G25-V309)&P61769
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表达区间
ACR83851.1 (G25-V309)&P61769 (I21-M119)
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分子量
48-53 kDa and 17 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 research into the recombinant protein HLA-B*27:05 and beta-2-microglobulin (B2M) monomer primarily stems from its critical role in understanding autoimmune diseases, particularly ankylosing spondylitis (AS). HLA-B27 is a major histocompatibility complex (MHC) class I molecule that is strongly associated with AS, a chronic inflammatory condition that primarily affects the spine and sacroiliac joints. The structure and function of HLA-B*27:05, in conjunction with B2M, are essential for presenting antigens to T cells, thus triggering immune response. However, the presence of the HLA-B27 allele is not solely responsible for AS; it is believed that certain conformational and molecular characteristics of the HLA-B27 molecule may predispose individuals to autoimmune pathology. The creation of HLA-B*27:05 and B2M monomer as a recombinant protein allows for detailed structural and functional studies, facilitating the exploration of its epitopes and interaction with T cell receptors. Furthermore, understanding the molecular basis of how HLA-B*27:05 contributes to disease mechanisms may uncover new therapeutic targets and diagnostics for AS and related conditions, making this research pivotal for advancing both basic immunology and clinical outcomes in patients with HLA-B27-related disorders.












