| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Igk |
| Uniprot No | P0DOX7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-214aa |
| 氨基酸序列 | DIQMTQSPSTLSASVGDRVTITCRASQSINTWLAWYQQKPGKAPKLLMYKASSLESGVPSRFIGSGSGTEFTLTISSLQPDDFATYYCQQYNSDSKMFGQGTKVEVKGTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC |
| 预测分子量 | 23,3 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IgK重组蛋白的3篇参考文献及其摘要概述：
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1. **文献名称**：*Production and characterization of recombinant human immunoglobulin kappa light chains*
**作者**：Smith J.D., et al.
**摘要**：研究通过哺乳动物表达系统(HEK293细胞)高效表达重组人Igκ轻链蛋白，并验证其正确折叠及与重链的结合能力，为抗体工程提供基础工具。
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2. **文献名称**：*Structural insights into Igk-mediated B cell receptor signaling*
**作者**：Wang L., Chen R.
**摘要**：通过晶体学解析重组Igκ与B细胞受体复合物的结构，阐明Igκ在信号转导中的作用机制，揭示其调控免疫应答的关键表位。
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3. **文献名称**：*Recombinant Igk fusion proteins enhance targeted drug delivery in murine models*
**作者**：Kumar S., et al.
**摘要**：开发基于重组Igκ的靶向融合蛋白，证明其在肿瘤模型中特异性递送化疗药物的效果，为癌症治疗提供新策略。
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4. **文献名称**：*Igk allelic exclusion in recombinant antibody libraries: A comparative analysis*
**作者**：Garcia M.A., et al.
**摘要**：比较不同重组Igκ文库构建技术对B细胞受体多样性的影响，提出优化策略以提高单克隆抗体筛选效率。
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(注：以上为虚拟文献示例，实际研究中建议通过PubMed或Web of Science检索具体论文。)
Immunoglobulin kappa (Igκ) light chain recombination is a critical process in adaptive immunity, enabling B cells to generate diverse antibody repertoires. Igκ, one of the two types of light chains (κ and λ) in antibodies, pairs with heavy chains to form antigen-binding sites. During B cell development, V (variable), J (joining), and occasionally C (constant) gene segments in the Igκ locus undergo site-specific recombination mediated by the V(D)J recombinase complex (RAG1/RAG2 enzymes). This process creates combinatorial diversity essential for recognizing countless pathogens.
Recombinant Igκ proteins, produced via genetic engineering in systems like mammalian or bacterial cells, are widely used in research and therapeutics. They serve as tools to study antibody structure-function relationships, immune signaling, and B cell maturation defects linked to diseases like multiple myeloma or autoimmune disorders. Engineered Igκ-based fragments (e.g., scFv, Fab) are also utilized in diagnostic assays, bispecific antibodies, and CAR-T cell therapies due to their stability and antigen specificity. Additionally, recombinant Igκ proteins help model pathological conditions, such as light chain amyloidosis, where misfolded Igκ aggregates cause organ damage. Advances in protein engineering, including humanization and affinity maturation, further enhance their clinical applicability. Understanding Igκ recombination mechanisms and leveraging recombinant variants continue to drive innovations in immunology and precision medicine.
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