纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | ABCF2 |
Uniprot No | Q9UG63 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-623aa |
氨基酸序列 | MPSDLAKKKA AKKKEAAKAR QRPRKGHEEN GDVVTEPQVA EKNEANGRET TEVDLLTKEL EDFEMKKAAA RAVTGVLASH PNSTDVHIIN LSLTFHGQEL LSDTKLELNS GRRYGLIGLN GIGKSMLLSA IGKREVPIPE HIDIYHLTRE MPPSDKTPLH CVMEVDTERA MLEKEAERLA HEDAECEKLM ELYERLEELD ADKAEMRASR ILHGLGFTPA MQRKKLKDFS GGWRMRVALA RALFIRPFML LLDEPTNHLD LDACVWLEEE LKTFKRILVL VSHSQDFLNG VCTNIIHMHN KKLKYYTGNY DQYVKTRLEL EENQMKRFHW EQDQIAHMKN YIARFGHGSA KLARQAQSKE KTLQKMMASG LTERVVSDKT LSFYFPPCGK IPPPVIMVQN VSFKYTKDGP CIYNNLEFGI DLDTRVALVG PNGAGKSTLL KLLTGELLPT DGMIRKHSHV KIGRYHQHLQ EQLDLDLSPL EYMMKCYPEI KEKEEMRKII GRYGLTGKQQ VSPIRNLSDG QKCRVCLAWL AWQNPHMLFL DEPTNHLDIE TIDALADAIN EFEGGMMLVS HDFRLIQQVA QEIWVCEKQT ITKWPGDILA YKEHLKSKLV DEEPQLTKRT HNV |
预测分子量 | 71,2 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ABCF2重组蛋白的3篇代表性文献概览(注:以下内容基于领域内常见研究方向模拟,实际文献需通过学术数据库验证):
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1. **文献名称**: *ABCF2 recombinant protein enhances chemoresistance in ovarian cancer cells by regulating drug efflux*
**作者**: Zhang Y, et al.
**摘要**: 本研究通过构建ABCF2重组蛋白,发现其在卵巢癌细胞中高表达可激活ATP依赖的药物外排泵功能,导致顺铂耐药性增强。重组蛋白的体外表达实验证实ABCF2通过调控跨膜转运通路影响化疗敏感性。
2. **文献名称**: *Purification and functional characterization of human ABCF2 as a recombinant ATP-binding cassette transporter*
**作者**: Liu X, et al.
**摘要**: 作者利用大肠杆菌表达系统成功纯化ABCF2重组蛋白,并验证其ATP酶活性。实验表明ABCF2的ATP结合结构域对其在细胞内囊泡运输中的功能至关重要,为后续靶向药物设计提供依据。
3. **文献名称**: *ABCF2 recombinant protein interacts with Bcl-2 family proteins to modulate apoptosis*
**作者**: Wang H, et al.
**摘要**: 通过重组ABCF2蛋白的体外结合实验,发现其与促凋亡蛋白Bax存在直接相互作用,可能通过抑制线粒体凋亡通路参与肿瘤细胞存活调控,提示ABCF2在癌症治疗中的潜在靶点价值。
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建议通过PubMed或Web of Science以关键词“ABCF2 recombinant”检索最新文献以获取准确信息。
ABCF2 (ATP-binding cassette subfamily F member 2) is a conserved eukaryotic protein belonging to the ABCF family, a subgroup of ATP-binding cassette (ABC) transporters distinguished by their lack of transmembrane domains. Unlike typical ABC transporters involved in substrate translocation across membranes, ABCF proteins like ABCF2 are primarily associated with intracellular regulatory processes, particularly in translation and ribosome function. Structurally, ABCF2 contains two nucleotide-binding domains (NBDs) that bind and hydrolyze ATP, a feature critical for its molecular interactions.
Research has linked ABCF2 to cancer biology and drug resistance. It is overexpressed in certain cancers, including non-small cell lung cancer and breast cancer, where it may promote tumor progression by inhibiting apoptosis or enhancing chemoresistance. Conversely, some studies suggest tumor-suppressive roles in specific contexts, highlighting its complex, context-dependent functions. ABCF2 is also implicated in mitochondrial regulation, endoplasmic reticulum stress responses, and viral infection processes through interactions with ribosomes or translational machinery.
Recombinant ABCF2 protein is typically produced using expression systems like *E. coli* or mammalian cell lines to preserve post-translational modifications. Purification involves affinity chromatography (e.g., His-tag or GST-tag systems) followed by functional validation via ATPase activity assays or protein interaction studies. Its recombinant form enables structural analysis (e.g., cryo-EM or X-ray crystallography) to elucidate mechanisms in translation regulation and disease pathways. Current research focuses on ABCF2 as a potential therapeutic target or biomarker, particularly in cancers resistant to conventional therapies. However, its precise molecular targets and regulatory networks remain under investigation, necessitating further studies to clarify its dual roles in health and disease.
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