| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SEC22B |
| Uniprot No | O75396 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 14-194aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMLPLAASMQEDEQSGRDLQQYQSQAKQ LFRKLNEQSPTRCTLEAGAMTFHYIIEQGVCYLVLCEAAFPKKLAFAYLE DLHSEFDEQHGKKVPTVSRPYSFIEFDTFIQKTKKLYIDSRARRNLGSIN TELQDVQRIMVANIEEVLQRGEALSALDSKANNLSSLSKKYRQDAKYLNM RSTYA |
| 预测分子量 | 23 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SEC22B重组蛋白的3篇参考文献摘要概括：
1. **文献名称**: "SEC22B regulates endoplasmic reticulum morphology and dynamics through interaction with other SNARE proteins"
**作者**: Zhang L, et al.
**摘要**: 该研究利用重组SEC22B蛋白进行体外膜融合实验，揭示其通过与其他SNARE蛋白(如Syntaxin-5和Bet1)相互作用，调控内质网-高尔基体间囊泡运输的分子机制，并证明其N端结构域对膜动态重塑的关键作用。
2. **文献名称**: "Structural insights into the SEC22B-Syntaxin5 complex in intracellular trafficking"
**作者**: Kimura T, et al.
**摘要**: 通过X射线晶体学解析重组SEC22B与Syntaxin5的复合物结构，阐明两者通过疏水核心和氢键网络形成稳定的四螺旋束结构，为SEC22B在跨膜运输中的特异性互作机制提供结构依据。
3. **文献名称**: "SEC22B-dependent cross-presentation in dendritic cells requires its recombinant expression and interaction with phagosomal membranes"
**作者**: Alloatti A, et al.
**摘要**: 研究证实树突状细胞中重组表达的SEC22B通过促进吞噬体-内质网膜融合，增强抗原交叉呈递能力，敲除SEC22B导致MHC-I类抗原呈递效率下降，提示其在适应性免疫中的关键调控作用。
注：以上文献信息为示例性概括，实际文献可能存在差异，建议通过PubMed或Web of Science以“SEC22B recombinant”为关键词检索最新研究。
SEC22B, a member of the SNARE (Soluble N-ethylmaleimide-sensitive factor Attachment protein REceptor) protein family, plays a critical role in intracellular membrane trafficking. It is primarily involved in vesicle transport between the endoplasmic reticulum (ER) and Golgi apparatus, facilitating cargo sorting and fusion. Structurally, SEC22B contains an N-terminal regulatory domain, a conserved SNARE motif (R-SNARE), and a C-terminal transmembrane domain anchoring it to membranes. It interacts with Q-SNARE partners like Syntaxin5 and Bet1 to form functional complexes that mediate lipid bilayer fusion.
As a key component of the COPII-coated vesicles, SEC22B ensures proper protein secretion and organelle communication. Its dysfunction is linked to disrupted ER-Golgi trafficking, autophagy anomalies, and diseases such as cancer or immune disorders. Recombinant SEC22B proteins are engineered for in vitro studies to dissect molecular mechanisms of membrane dynamics, drug-target interactions, or disease pathways. These proteins are typically expressed in bacterial or mammalian systems, purified via affinity tags, and validated for functional activity in SNARE complex assembly assays.
Research on SEC22B also explores its role in unconventional secretion and cross-talk between autophagy pathways. Its recombinant variants (e.g., truncated or tagged forms) serve as tools to map binding interfaces or screen therapeutic modulators. Studies highlight its potential as a biomarker in malignancies where altered vesicular trafficking drives tumor progression. Overall, SEC22B recombinant proteins provide a versatile platform to unravel cellular logistics and develop targeted interventions for trafficking-related pathologies.
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