| 纯度 | >80%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SLA2 |
| Uniprot No | Q9H6Q3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-261aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMGSLPSRRKSLPSPSLSSSVQGQGPVT MEAERSKATAVALGSFPAGGPAELSLRLGEPLTIVSEDGDWWTVLSEVSG REYNIPSVHVAKVSHGWLYEGLSREKAEELLLLPGNPGGAFLIRESQTRR GSYSLSVRLSRPASWDRIRHYRIHCLDNGWLYISPRLTFPSLQALVDHYS ELADDICCLLKEPCVLQRAGPLPGKDIPLPVTVQRTPLNWKELDSSLLFS EAATGEESLLSEGLRESLSFYISLNDEAVSLDDA |
| 预测分子量 | 31 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于SLA2重组蛋白的参考文献列表，包含文献名称、作者及摘要概括：
1. **文献名称**：*Structural insights into the actin-binding domain of SLA2 in yeast*
**作者**：Smith J, et al.
**摘要**：通过X射线晶体学解析了酵母SLA2蛋白的肌动蛋白结合域结构，揭示其与肌动蛋白丝的相互作用机制，并利用重组蛋白验证结合活性。
2. **文献名称**：*Functional characterization of recombinant SLA2 in endocytic vesicle formation*
**作者**：Lee H, Kim S
**摘要**：通过重组SLA2蛋白表达，研究其在网格蛋白介导的内吞过程中与接头蛋白的互作，证实SLA2在膜弯曲和囊泡形成中的关键作用。
3. **文献名称**：*Expression and purification of recombinant SLA2 for biochemical assays*
**作者**：Zhang L, et al.
**摘要**：优化了SLA2重组蛋白在大肠杆菌中的表达与纯化流程，验证其适用于体外肌动蛋白结合及酶动力学实验。
4. **文献名称**：*Role of SLA2 in actin cytoskeleton organization: Studies using recombinant proteins*
**作者**：Brown K, White R
**摘要**：利用重组SLA2蛋白进行体外实验，证明其通过调控肌动蛋白动态组装影响酵母细胞形态和运动性。
**注**：以上文献为模拟示例，实际引用时建议通过学术数据库(如PubMed、Web of Science)检索最新或经典文献。
**Background of SLA2 Recombinant Protein**
The Swine Leukocyte Antigen class II (SLA-II) is a critical component of the porcine adaptive immune system, responsible for presenting antigenic peptides to CD4+ T cells to initiate immune responses. Among SLA-II molecules, SLA-DR (SLA2) plays a central role in binding exogenous antigens and triggering immune recognition. Recombinant SLA2 proteins are engineered to mimic the native structure and function of SLA-DR molecules, typically produced using heterologous expression systems such as mammalian cells, insect cells, or prokaryotic platforms. These systems enable large-scale production of SLA2 with preserved antigen-binding grooves and β-chain domains, essential for studying immune interactions.
The development of recombinant SLA2 stems from the need to understand and combat swine-specific pathogens, including African swine fever virus (ASFV) and porcine reproductive and respiratory syndrome virus (PRRSV). By reconstituting SLA2 in vitro, researchers can analyze peptide-binding motifs, evaluate T cell epitopes, and design vaccines tailored to enhance MHC-restricted immunity. Additionally, recombinant SLA2 serves as a tool for investigating cross-species compatibility, particularly in xenotransplantation research, where SLA compatibility impacts graft survival in human recipients.
Recent advances in structural biology and protein engineering have refined SLA2 production, enabling crystallographic studies to resolve its 3D architecture and interaction mechanisms. Such insights aid in developing immunotherapies and diagnostic tools for swine diseases. Furthermore, recombinant SLA2 contributes to comparative immunology, bridging gaps between porcine and human MHC systems. Its applications extend to monitoring vaccine efficacy, optimizing adjuvants, and modeling autoimmune diseases in pigs. As zoonotic threats and agricultural demands grow, SLA2 recombinant proteins remain pivotal in advancing veterinary medicine and translational immunology.
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