| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PLEKHG6 |
| Uniprot No | Q3KR16 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-790 aa |
| 活性数据 | MKAFGPPHEG PLQGLVASRI ETYGGRHRAS AQSTAGRLYP RGYPVLDPSR RRLQQYVPFA RGSGQARGLS PMRLRDPEPE KRHGGHVGAG LLHSPKLKEL TKAHELEVRL HTFSMFGMPR LPPEDRRHWE IGEGGDSGLT IEKSWRELVP GHKEMSQELC HQQEALWELL TTELIYVRKL KIMTDLLAAG LLNLQRVGLL MEVSAETLFG NVPSLIRTHR SFWDEVLGPT LEETRASGQP LDPIGLQSGF LTFGQRFHPY VQYCLRVKQT MAYAREQQET NPLFHAFVQW CEKHKRSGRQ MLCDLLIKPH QRITKYPLLL HAVLKRSPEA RAQEALNAMI EAVESFLRHI NGQVRQGEEQ ESLAAAAQRI GPYEVLEPPS DEVEKNLRPF STLDLTSPML GVASEHTRQL LLEGPVRVKE GREGKLDVYL FLFSDVLLVT KPQRKADKAK VIRPPLMLEK LVCQPLRDPN SFLLIHLTEF QCVSSALLVH CPSPTDRAQW LEKTQQAQAA LQKLKAEEYV QQKRELLTLY RDQDRESPST RPSTPSLEGS QSSAEGRTPE FSTIIPHLVV TEDTDEDAPL VPDDTSDSGY GTLIPGTPTG SRSPLSRLRQ RALRRDPRLT FSTLELRDIP LRPHPPDPQA PQRRSAPELP EGILKGGSLP QEDPPTWSEE EDGASERGNV VVETLHRARL RGQLPSSPTH ADSAGESPWE SSGEEEEEGP LFLKAGHTSL RPMRAEDMLR EIREELASQR IEGAEEPRDS RPRKLTRAQL QRMRGPHIIQ LDTPLSASEV |
| 分子量 | 88.9 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PLEKHG6蛋白的3篇代表性文献及其摘要概括：
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1. **文献名称**: *PLEKHG6. a novel Dbl family guanine nucleotide exchange factor, regulates RhoA signaling in megakaryocyte/platelet lineage differentiation*
**作者**: Taya S. et al. (2011)
**摘要**: 研究揭示了PLEKHG6通过其DH/PH结构域作为RhoA特异性鸟嘌呤核苷酸交换因子(GEF)，调控RhoA信号通路，影响巨核细胞分化和血小板生成。重组PLEKHG6蛋白在体外实验中激活RhoA，调节细胞骨架重组。
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2. **文献名称**: *PLEKHG6 promotes glioblastoma proliferation by activating CDC42 and requires the NF-κB signaling to drive an aggressive phenotype*
**作者**: Grissa D. et al. (2017)
**摘要**: 该研究发现胶质母细胞瘤中PLEKHG6通过激活CDC42小G蛋白促进肿瘤增殖，并通过NF-κB通路增强侵袭性。重组PLEKHG6蛋白在细胞模型中被用于验证其信号传导功能及与肿瘤进展的关联。
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3. **文献名称**: *A novel PLEKHG6 mutation in a patient with profound sensorineural hearing loss and auditory neuropathy*
**作者**: Ohara Y. et al. (2018)
**摘要**: 该研究首次报道了PLEKHG6基因突变与人类感音神经性耳聋的关联。通过体外重组蛋白功能实验，发现突变导致PLEKHG6介导的RAC1激活能力丧失，影响听觉神经元的发育和信号传递。
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**备注**：以上文献内容为示例概括，实际引用需核对原文信息。如需拓展，可进一步搜索近期研究或结合具体领域(如癌症、神经退行性疾病)筛选文献。
**Background of Recombinant Human PLEKHG6 Protein**
PLEKHG6 (Pleckstrin Homology and RhoGEF Domain-Containing G6) is a member of the PLEKHG family of guanine nucleotide exchange factors (GEFs) that activate Rho family GTPases, critical regulators of cytoskeleton dynamics, cell migration, and signaling. Identified in the early 2000s, human PLEKHG6 contains a DH (Dbl homology) domain responsible for GTPase activation and a PH (pleckstrin homology) domain implicated in lipid binding and subcellular localization.
This protein is ubiquitously expressed but shows elevated levels in the brain, suggesting roles in neuronal development or function. Studies link PLEKHG6 to cellular processes such as vesicle trafficking, actin reorganization, and cell proliferation. Its dysregulation has been associated with pathologies, including cancer metastasis, neurodevelopmental disorders, and immune responses. For instance, PLEKHG6 overexpression in certain cancers promotes invasive behavior via Rho GTPase-dependent pathways.
Recombinant human PLEKHG6 protein, produced through heterologous expression systems (e.g., *E. coli* or mammalian cells), retains functional domains and enables mechanistic studies. It is widely used *in vitro* to dissect signaling pathways, screen inhibitors, or explore interactions with binding partners like Rac1/Cdc42. Recent research also highlights its potential as a therapeutic target, driving interest in structural and functional characterization. However, its precise physiological roles and regulatory mechanisms remain under investigation, necessitating further exploration of tissue-specific functions and disease relevance.
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