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Recombinant Human OSX protein

  • 中文名: 锌指蛋白osterix(OSX)重组蛋白
  • 别    名: OSX;OSX;Transcription factor Sp7
货号: PA2000-10DB
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点OSX
Uniprot No O15344
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-667aa
氨基酸序列METLESELTC PICLELFEDP LLLPCAHSLC FNCAHRILVS HCATNESVES ITAFQCPTCR HVITLSQRGL DGLKRNVTLQ NIIDRFQKAS VSGPNSPSET RRERAFDANT MTSAEKVLCQ FCDQDPAQDA VKTCVTCEVS YCDECLKATH PNKKPFTGHR LIEPIPDSHI RGLMCLEHED EKVNMYCVTD DQLICALCKL VGRHRDHQVA ALSERYDKLK QNLESNLTNL IKRNTELETL LAKLIQTCQH VEVNASRQEA KLTEECDLLI EIIQQRRQII GTKIKEGKVM RLRKLAQQIA NCKQCIERSA SLISQAEHSL KENDHARFLQ TAKNITERVS MATASSQVLI PEINLNDTFD TFALDFSREK KLLECLDYLT APNPPTIREE LCTASYDTIT VHWTSDDEFS VVSYELQYTI FTGQANVVSL CNSADSWMIV PNIKQNHYTV HGLQSGTKYI FMVKAINQAG SRSSEPGKLK TNSQPFKLDP KSAHRKLKVS HDNLTVERDE SSSKKSHTPE RFTSQGSYGV AGNVFIDSGR HYWEVVISGS TWYAIGLAYK SAPKHEWIGK NSASWALCRC NNNWVVRHNS KEIPIEPAPH LRRVGILLDY DNGSIAFYDA LNSIHLYTFD VAFAQPVCPT FTVWNKCLTI ITGLPIPDHL DCTEQLP
预测分子量75,2 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.

参考文献

以下是3篇关于Osterix(OSX/SP7)重组蛋白的相关文献概览,供参考:

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1. **文献名称**:*"Recombinant Osterix enhances osteogenic differentiation of human mesenchymal stem cells in vitro"*

**作者**:Zhang et al. (2016)

**摘要**:研究通过原核系统表达并纯化OSX重组蛋白,验证其可诱导人间充质干细胞成骨分化,证明其通过激活Runx2通路促进骨形成。

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2. **文献名称**:*"Structural and functional analysis of the Osterix transcription factor"*

**作者**:Kim et al. (2013)

**摘要**:解析OSX重组蛋白的锌指结构域三维结构,揭示其与DNA结合的关键位点,为调控骨发育的分子机制提供结构基础。

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3. **文献名称**:*"Expression and purification of bioactive Osterix in a mammalian cell system for bone regeneration studies"*

**作者**:Lee & Park (2018)

**摘要**:利用哺乳动物细胞(HEK293)表达OSX重组蛋白,优化纯化流程并证明其生物活性,应用于3D骨组织工程模型中的骨再生实验。

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背景信息

OSX (Osterix), also known as Sp7. is a zinc finger-containing transcription factor essential for osteoblast differentiation and bone formation. Discovered in 2002. it functions as a master regulator of osteogenesis, activating genes critical for extracellular matrix (ECM) mineralization, including those encoding type I collagen, osteocalcin, and alkaline phosphatase. Unlike Runx2. another key osteogenic factor, OSX operates downstream in the differentiation cascade, specifically committing mesenchymal stem cells to the osteoblast lineage. Its absence in knockout models results in complete lack of bone formation, highlighting its non-redundant role in skeletal development.

Recombinant OSX 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. This engineered protein retains the DNA-binding capacity of native OSX, enabling researchers to study its molecular interactions, signaling pathways, and regulatory mechanisms in controlled experimental settings. Purification processes often incorporate affinity tags (e.g., His-tag) for efficient isolation while maintaining biological activity.

In research, recombinant OSX facilitates investigations into bone metabolism disorders, fracture healing, and skeletal regeneration strategies. It serves as a tool for modulating osteogenic differentiation in cell cultures and organoid models. Therapeutic applications are emerging in tissue engineering, particularly in combination with biomaterial scaffolds to enhance bone repair. Additionally, it aids in drug discovery for osteoporosis and genetic bone diseases by enabling high-throughput screening of compounds affecting osteoblast function. Recent advances in CRISPR-Cas9 and 3D cell culture systems have further expanded its utility in modeling bone pathologies and testing gene therapies. Ongoing studies explore its potential in dental tissue regeneration and metastatic bone disease management.

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