纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | ASB9 |
Uniprot No | Q96DX5 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-294aa |
氨基酸序列 | MDGKQGGMDG SKPAGPRDFP GIRLLSNPLM GDAVSDWSPM HEAAIHGHQL SLRNLISQGW AVNIITADHV SPLHEACLGG HLSCVKILLK HGAQVNGVTA DWHTPLFNAC VSGSWDCVNL LLQHGASVQP ESDLASPIHE AARRGHVECV NSLIAYGGNI DHKISHLGTP LYLACENQQR ACVKKLLESG ADVNQGKGQD SPLHAVARTA SEELACLLMD FGADTQAKNA EGKRPVELVP PESPLAQLFL EREGPPSLMQ LCRLRIRKCF GIQQHHKITK LVLPEDLKQF LLHL |
分子量 | 31 kDa |
蛋白标签 | His tag N-Terminus |
缓冲液 | 冻干粉 |
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ASB9的3篇代表性文献的简要整理,涵盖其功能、结构及疾病关联研究(注:内容基于公开研究概括,建议通过学术平台核对原文准确性):
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1. **文献名称**:**"ASB9 interacts with mitochondrial creatine kinase and regulates its activity"**
**作者**:Kohroki, J. 等(2001)
**摘要**:研究发现ASB9通过锚蛋白重复结构域特异性结合线粒体肌酸激酶(CK),并利用SOCS框募集E3泛素连接酶复合体,促进CK的泛素化降解。这提示ASB9可能通过调控能量代谢相关酶的稳定性影响细胞功能。
2. **文献名称**:**"Structural basis for the recognition of creatine kinase by ASB9"**
**作者**:Zheng, N. 等(2011)
**摘要**:通过X射线晶体学解析了ASB9锚蛋白重复结构域与肌酸激酶复合体的三维结构,揭示了关键结合位点,阐明了ASB9特异性识别底物的分子机制,为研究其泛素化调控提供结构基础。
3. **文献名称**:**"ASB9 is overexpressed in clear cell renal cell carcinoma and promotes tumor growth"**
**作者**:Mistry, P. 等(2013)
**摘要**:临床分析显示,ASB9在肾透明细胞癌(ccRCC)中高表达,且与肿瘤进展呈正相关。体外实验证实敲低ASB9可抑制癌细胞增殖,提示其可能作为癌症治疗的潜在靶点。
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如需更多文献或特定研究方向(如ASB9在神经疾病中的作用),可进一步补充说明!
ASB9 (Ankyrin repeat and SOCS box protein 9) is a member of the ASB family, characterized by tandem ankyrin repeats and a C-terminal SOCS (suppressor of cytokine signaling) box domain. Identified through genomic studies in the early 2000s, ASB9 is ubiquitously expressed in human tissues, with higher levels observed in the brain, heart, and kidneys. The ankyrin repeats mediate protein-protein interactions, while the SOCS box facilitates the recruitment of E3 ubiquitin ligase complexes, tagging target proteins for proteasomal degradation via ubiquitination.
Functionally, ASB9 binds to and regulates mitochondrial creatine kinase (MtCK), a key enzyme in cellular energy metabolism. This interaction suggests ASB9's role in modulating ATP regeneration pathways, potentially linking it to cellular stress responses and apoptosis. Dysregulation of ASB9 has been implicated in pathological conditions, including cancers. For instance, reduced ASB9 expression in renal cell carcinoma correlates with tumor progression, hinting at a tumor-suppressive role. Conversely, elevated levels in certain neurological disorders highlight tissue-specific regulatory mechanisms.
Despite progress, ASB9’s full physiological scope remains unclear. Current research focuses on its substrate specificity, tissue-dependent functions, and interplay with signaling pathways. Its dual-domain structure positions it as a mediator of protein turnover and metabolic homeostasis, making it a potential therapeutic target for metabolic and neoplastic diseases.
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