| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | STAC |
| Uniprot No | Q99469 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-402aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMIPPSSPREDGVDGLPKEAVGAEQPPS PASTSSQESKLQKLKRSLSFKTKSLRSKSADNFFQRTNSEDMKLQAHMVA EISPSSSPLPAPGSLTSTPARAGLHPGGKAHAFQEYIFKKPTFCDVCNHM IVGTNAKHGLRCKACKMSIHHKCTDGLAPQRCMGKLPKGFRRYYSSPLLI HEQFGCIKEVMPIACGNKVDPVYETLRFGTSLAQRTKKGSSGSGSDSPHR TSTSDLVEVPEEANGPGGGYDLRKRSNSVFTYPENGTDDFRDPAKNINHQ GSLSKDPLQMNTYVALYKFVPQENEDLEMRPGDIITLLEDSNEDWWKGKI QDRIGFFPANFVQRLQQNEKIFRCVRTFIGCKEQGQITLKENQICVSSEE EQDGFIRVLSGKKKGLIPLDVLENI |
| 预测分子量 | 47 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STAC重组蛋白研究的示例参考文献(内容为虚构示例，仅供格式参考)：
1. **文献名称**: "Functional Characterization of Recombinant STAC1 Protein in Skeletal Muscle Signaling"
**作者**: Smith A, et al.
**摘要**: 本研究利用昆虫细胞系统表达重组STAC1蛋白，验证其通过SH3结构域与CaV1.1通道相互作用，调节骨骼肌兴奋-收缩耦合的功能，为肌肉疾病机制提供新见解。
2. **文献名称**: "Expression and Purification of STAC3 Recombinant Protein for Malignant Hyperthermia Studies"
**作者**: Chen L, et al.
**摘要**: 通过大肠杆菌表达系统优化STAC3重组蛋白的纯化流程，并证明其在体外模型中影响RyR1通道活性，可能与恶性高热症病理相关。
3. **文献名称**: "Structural Analysis of STAC2 Recombinant Protein Using Cryo-EM"
**作者**: Tanaka K, et al.
**摘要**: 首次解析重组STAC2蛋白的冷冻电镜结构，揭示其与T型钙通道(CaV3.1)的结合模式，为靶向药物设计提供结构基础。
4. **文献名称**: "Role of Recombinant STAC Proteins in Cardiac Arrhythmia Models"
**作者**: Müller R, et al.
**摘要**: 在心肌细胞中过表达重组STAC家族蛋白，发现STAC2通过调控钙离子稳态影响心律失常的发生，提示其潜在治疗靶点价值。
**注意**：以上文献名称及内容为示例，实际研究中请通过PubMed、Web of Science等平台检索真实文献。
**Background of STAC Proteins**
The STAC (SH3 and cysteine-rich domain-containing) family of proteins, comprising STAC1. STAC2. and STAC3. plays critical roles in cellular signaling and ion channel regulation. Discovered in the late 1990s, these adaptor proteins are characterized by their conserved structural domains: an N-terminal SH3 domain, which mediates protein-protein interactions, and one or two cysteine-rich regions implicated in membrane association or redox sensing.
STAC proteins are widely expressed, with notable roles in skeletal muscle, neurons, and immune cells. STAC3. the most studied member, is essential for excitation-contraction (EC) coupling in skeletal muscle. It interacts with the voltage-gated calcium channel Cav1.1 (CACNA1S) and the ryanodine receptor (RyR1), facilitating calcium release during muscle contraction. Mutations in *STAC3* are linked to congenital myopathy, highlighting its physiological importance.
STAC1 and STAC2 also modulate ion channels and signaling pathways. STAC1 regulates TRPV1 and TRPA1 channels in pain perception, while STAC2 influences Cav1.2 and Cav1.3 channels in neurons and cardiomyocytes. Emerging evidence suggests STAC proteins act as scaffolds, integrating signals from kinases like PKC and PKA to fine-tune cellular responses.
Dysregulation of STAC proteins is associated with diseases, including muscular disorders, neuropathies, and cancer. STAC3’s role in EC coupling has driven research into therapies for neuromuscular diseases, while STAC1/2 are explored as targets for pain management or cardiac arrhythmias.
Despite progress, many mechanisms remain unclear, particularly how cysteine-rich domains contribute to signaling or stress responses. Ongoing studies aim to unravel STAC-specific interactomes and their therapeutic potential, leveraging structural biology and disease models. Understanding STAC proteins offers insights into calcium signaling and adaptive cellular processes, with implications for treating channelopathies and beyond.
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