| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SGCD |
| Uniprot No | Q92629 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 57-289aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH RSHMKVMNFT IDGMGNLRIT EKGLKLEGDS EFLQPLYAKE IQSRPGNALY FKSARNVTVN ILNDQTKVLT QLITGPKAVE AYGKKFEVKT VSGKLLFSAD NNEVVVGAER LRVLGAEGTV FPKSIETPNV RADPFKELRL ESPTRSLVME APKGVEINAE AGNMEATCRT ELRLESKDGE IKLDAAKIRL PRLPHGSYTP TGTRQKVFEI CVCANGRLFL SQAGAGSTCQ INTSVCL |
| 预测分子量 | 28 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. |
以下是基于SGCD(δ-sarcoglycan)重组蛋白相关研究的模拟参考文献示例(实际文献需根据具体数据库检索)：
1. **文献名称**: "Expression and Purification of Recombinant Human δ-Sarcoglycan in Mammalian Cells"
**作者**: Smith J, et al.
**摘要**: 研究报道了在HEK293细胞中高效表达并纯化功能性人源SGCD重组蛋白的方法，证实其在体外可恢复肌细胞膜稳定性，为肌萎缩症治疗提供潜在工具。
2. **文献名称**: "Structural Characterization of δ-Sarcoglycan and Its Role in Dystrophin-Glycoprotein Complex Assembly"
**作者**: Tanaka K, et al.
**摘要**: 通过重组SGCD蛋白的晶体结构解析，揭示了其与γ-sarcoglycan的相互作用机制，阐明了其在维持肌纤维膜完整性中的关键结构功能。
3. **文献名称**: "Adenoviral Delivery of Recombinant SGCD Ameliorates Muscular Dystrophy in δ-SG Deficient Mice"
**作者**: Liu Y, et al.
**摘要**: 利用腺病毒载体递送重组SGCD蛋白至δ-SG缺陷小鼠模型，显著改善肌肉病理表型，验证了基因治疗策略对肢带型肌营养不良症的可行性。
注：以上为模拟文献，实际引用需以具体检索结果为准。建议通过PubMed或Web of Science以“delta-sarcoglycan recombinant”为关键词查找最新研究。
**Background of SGCD Recombinant Protein**
Sarcoglycan delta (SGCD), a key component of the sarcoglycan complex, plays a critical role in maintaining the structural integrity of muscle cell membranes. This transmembrane protein is predominantly expressed in skeletal, cardiac, and smooth muscle tissues, where it forms a subcomplex with other sarcoglycans (α, β, γ) as part of the dystrophin-glycoprotein complex (DGC). The DGC stabilizes the muscle membrane during contraction by linking the cytoskeleton to the extracellular matrix, thereby protecting cells from mechanical stress.
Mutations in the *SGCD* gene are associated with limb-girdle muscular dystrophy type 2F (LGMD2F) and dilated cardiomyopathy, highlighting its essential function in muscle health. Studying SGCD’s molecular mechanisms has been challenging due to its hydrophobic nature and complex post-translational modifications. Recombinant SGCD protein, produced via heterologous expression systems (e.g., mammalian cells, bacteria, or insect cells), enables researchers to overcome these hurdles.
The recombinant protein is typically engineered with tags (e.g., His, GST) for purification and detection. It serves as a vital tool for investigating SGCD’s interactions within the DGC, its role in signaling pathways, and the pathological effects of mutations. Additionally, it facilitates drug screening for LGMD2F and the development of gene or protein replacement therapies.
Recent advances in structural biology and protein engineering have improved the yield and stability of recombinant SGCD, enhancing its utility in both basic research and therapeutic applications. By providing a controlled source of functional SGCD, recombinant variants continue to drive progress in understanding and treating sarcoglycanopathies.
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