| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SRR |
| Uniprot No | Q9GZT4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-340aa |
| 氨基酸序列 | MCAQYCISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALERKPKAVVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGTIALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPNLYPPETIADGVKSSIGLNTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTVSPEVKNICIVLSGGNVDLTSSITWVKQAERPASYQSVSV |
| 预测分子量 | 37.1 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. |
以下是模拟生成的3篇关于SRR重组蛋白的参考文献(注：示例为虚构，仅作格式参考)：
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1. **文献名称**: *Expression and functional analysis of recombinant SRR protein in prokaryotic systems*
**作者**: Zhang L, et al.
**摘要**: 该研究利用大肠杆菌表达系统成功表达了SRR重组蛋白，通过亲和层析纯化获得高纯度蛋白，并验证了其与RNA结合的功能活性，为后续结构研究奠定基础。
2. **文献名称**: *SRR family proteins in alternative splicing: Recombinant SRRM2 characterization*
**作者**: Kim S, et al.
**摘要**: 作者构建了SRRM2重组蛋白的真核表达载体，在HEK293细胞中验证其参与pre-mRNA剪接调控的作用，揭示了SRR结构域在剪接体组装中的关键功能。
3. **文献名称**: *Therapeutic potential of recombinant SRR proteins in cancer models*
**作者**: Gupta R, et al.
**摘要**: 通过昆虫细胞表达系统制备了功能性SRR重组蛋白，实验证明其能抑制肿瘤细胞增殖，并调控致癌基因的可变剪接，提示其作为癌症治疗靶点的潜力。
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**备注**：以上文献为示例性内容，实际研究中请通过PubMed或Web of Science以关键词“SRR recombinant protein”或“serine arginine-rich recombinant”检索最新文献。
**Background of SRR Recombinant Proteins**
SRR (serine-rich repeat) proteins are a family of bacterial surface-associated glycoproteins predominantly found in Gram-positive pathogens, such as *Streptococcus* species (e.g., *S. pneumoniae*, *S. sanguinis*). These proteins are characterized by extensive serine-rich repeat regions, which undergo post-translational modifications, particularly O-linked glycosylation, contributing to their structural and functional diversity. SRR proteins play critical roles in bacterial adhesion, colonization, and immune evasion, making them key virulence factors in infections like endocarditis, pneumonia, and meningitis.
Structurally, SRR proteins typically contain an N-terminal signal peptide, a serine-rich central domain, and a C-terminal cell wall-anchoring motif. The serine-rich regions are often decorated with glycans, which enhance protein stability, mediate interactions with host receptors, and shield bacterial surfaces from immune recognition. For example, in *S. sanguinis*, the SRR glycoprotein SrpA facilitates binding to platelets and endothelial cells, promoting thrombus formation in infective endocarditis. Similarly, *S. pneumoniae* SRR proteins aid in mucosal colonization and evasion of phagocytic clearance.
Research on SRR proteins has expanded due to their potential as therapeutic targets. Their surface-exposed epitopes and role in pathogenesis make them candidates for vaccines or monoclonal antibody therapies. Recombinant SRR proteins, produced via expression systems like *E. coli* or yeast, are instrumental in studying glycosylation patterns, host-pathogen interactions, and immune responses. Challenges include reproducing native-like glycosylation in heterologous systems, necessitating advanced glycoengineering approaches.
Overall, SRR recombinant proteins provide insights into bacterial virulence mechanisms and pave the way for novel anti-infective strategies, emphasizing their significance in both basic research and translational applications.
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