纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | STK24 |
Uniprot No | Q9Y6E0 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-443aa |
氨基酸序列 | MDSRAQLWGLALNKRRATLPHPGGSTNLKADPEELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGSALDLLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRNTFVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLEGNYSKPLKEFVEACLNKEPSFRPTAKELLKHKFILRNAKKTSYLTELIDRYKRWKAEQSHDDSSSEDSDAETDGQASGGSDSGDWIFTIREKDPKNLENGALQPSDLDRNKMKDIPKRPFSQCLSTIISPLFAELKEKSQACGGNLGSIEELRGAIYLAEEACPGISDTMVAQLVQRLQRYSLSGGGTSSH |
预测分子量 | 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STK24重组蛋白的3篇参考文献概览:
1. **文献名称**:*"Structure and functional analysis of the human STE20 kinase STK24"*
**作者**:Chen et al. (2016)
**摘要**:解析了人源STK24激酶结构域的重组蛋白晶体结构,揭示了其底物识别机制,并证明其通过磷酸化MAP4K4调控细胞凋亡的功能。
2. **文献名称**:*"STK24 modulates oxidative stress-induced neuronal apoptosis via interaction with CCM3"*
**作者**:Zhang Y. et al. (2018)
**摘要**:利用重组STK24蛋白研究其与CCM3的相互作用,发现二者共同调控氧化应激下的神经元凋亡通路,为脑血管疾病提供分子机制依据。
3. **文献名称**:*"STK24 regulates cell polarity and migration by phosphorylating GEF-H1 in breast cancer"*
**作者**:Li H. et al. (2020)
**摘要**:通过重组STK24蛋白体外实验,证实其磷酸化GEF-H1并影响RhoA活性,从而抑制乳腺癌细胞侵袭转移能力。
*注:若需获取全文,建议通过PubMed/Google Scholar按标题检索,部分文献可能需要订阅权限。*
**Background of STK24 Recombinant Protein**
STK24 (serine/threonine kinase 24), also known as MST3 (mammalian STE20-like protein kinase 3), is a member of the STE20 family of protein kinases. It plays a critical role in regulating diverse cellular processes, including apoptosis, cell proliferation, polarity, and stress responses. Structurally, STK24 contains an N-terminal kinase domain responsible for catalytic activity and a C-terminal regulatory domain that facilitates interactions with scaffolding proteins or signaling complexes. This kinase is part of the STRIPAK (striatin-interacting phosphatase and kinase) complex, which modulates its activity through phosphorylation-dependent signaling pathways.
The recombinant STK24 protein is produced using genetic engineering techniques, typically expressed in bacterial (e.g., *E. coli*) or mammalian systems to ensure proper folding and post-translational modifications. Purified STK24 recombinant protein retains enzymatic activity and is widely used in *in vitro* studies to investigate its substrate specificity, regulatory mechanisms, and interactions with binding partners. Researchers employ techniques like kinase assays, co-immunoprecipitation, and structural analysis (e.g., X-ray crystallography) to explore its functional roles.
STK24 has been implicated in diseases such as cancer, neurological disorders, and immune dysregulation. For example, it acts as a tumor suppressor in certain contexts by inhibiting pro-survival signals, while its dysregulation is linked to neurodegenerative conditions like Alzheimer’s disease. Recombinant STK24 enables drug discovery efforts, serving as a target for screening small-molecule inhibitors or activators to modulate its activity therapeutically.
Overall, STK24 recombinant protein is a vital tool for deciphering the molecular basis of cellular signaling and developing strategies to target kinase-mediated pathways in disease.
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