纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | STK16 |
Uniprot No | O75716 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-305aa |
氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMGHALC VCSRGTVIID NKRYLFIQKL GEGGFSYVDL VEGLHDGHFY ALKRILCHEQ QDREEAQREA DMHRLFNHPN ILRLVAYCLR ERGAKHEAWL LLPFFKRGTL WNEIERLKDK GNFLTEDQIL WLLLGICRGL EAIHAKGYAH RDLKPTNILL GDEGQPVLMD LGSMNQACIH VEGSRQALTL QDWAAQRCTI SYRAPELFSV QSHCVIDERT DVWSLGCVLY AMMFGEGPYD MVFQKGDSVA LAVQNQLSIP QSPRHSSALR QLLNSMMTVD PHQRPHIPLL LSQLEALQPP APGQHTTQI |
预测分子量 | 37 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STK16重组蛋白的3篇代表性文献(信息已简化整理):
1. **文献名称**: "Crystal structure of the human serine/threonine kinase STK16 reveals a novel dimeric architecture"
**作者**: S. Pike et al.
**摘要**: 本研究解析了人源STK16激酶结构域的晶体结构,首次揭示了其独特的二聚体构象,并通过体外重组蛋白实验验证了其自磷酸化活性及二聚化对激酶功能的影响。
2. **文献名称**: "STK16 regulates actin dynamics to control Golgi organization and cell migration"
**作者**: L. Zhang et al.
**摘要**: 通过重组STK16蛋白的体外磷酸化实验,发现其特异性磷酸化肌动蛋白结合蛋白cofilin,揭示了STK16通过调控细胞骨架动力学影响高尔基体形态和细胞迁移的分子机制。
3. **文献名称**: "Characterization of recombinant STK16/MST4 kinase: Substrate specificity and autophosphorylation sites"
**作者**: K. Machida et al.
**摘要**: 报道了在大肠杆菌系统中重组表达并纯化STK16激酶的方法,系统分析了其体外底物选择性和自磷酸化位点,为后续功能研究提供了生化基础。
注:以上文献信息为示例性综合内容,实际引用时需核对具体论文的准确性。建议通过PubMed或Web of Science以"STK16"、"recombinant protein"等关键词检索最新文献。
**Background of STK16 Recombinant Protein**
STK16 (serine/threonine kinase 16), also known as MYO3C or MPSK1. is a member of the protein kinase superfamily involved in regulating cellular processes such as vesicle trafficking, cell cycle progression, and signal transduction. It is a ubiquitously expressed enzyme characterized by a conserved catalytic kinase domain, though its precise physiological roles remain less understood compared to other kinases. STK16 lacks a clear ortholog in lower eukaryotes, suggesting unique functional adaptations in vertebrates.
The recombinant STK16 protein is typically produced in vitro using expression systems like *E. coli* or mammalian cell lines, enabling researchers to study its biochemical properties, enzymatic activity, and interactions. Recombinant STK16 retains autophosphorylation capability and can phosphorylate exogenous substrates, making it valuable for elucidating substrate specificity and signaling mechanisms. Structural studies using recombinant STK16 have revealed insights into its ATP-binding pocket and regulatory regions, which may guide drug discovery efforts.
STK16 has been implicated in pathologies, including cancer and neurodegenerative diseases. For example, it interacts with proteins involved in Golgi apparatus dynamics, influencing secretory pathways critical for cell proliferation. Dysregulation of STK16 expression or activity may contribute to tumorigenesis, though its dual roles as both an oncogene and tumor suppressor remain context-dependent. Recombinant STK16 facilitates functional studies, such as screening inhibitors or mapping phosphorylation-dependent pathways.
Despite progress, many aspects of STK16 biology, including its upstream regulators and downstream effectors, require further exploration. The availability of recombinant STK16 protein continues to support mechanistic research, bridging gaps in understanding its contributions to cellular homeostasis and disease.
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