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Recombinant Human OSTN protein

  • 中文名: 骨织素(OSTN)重组蛋白
  • 别    名: OSTN;Osteocrin
货号: PA1000-2259
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产品详情

纯度>85%SDS-PAGE.
种属Human
靶点OSTN
Uniprot No P61366
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间83-132aa
氨基酸序列SFSGFGSP LDRLSAGSVD HKGKQRKVVD HPKRRFGIPM DRIGRNRLSN SR
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.

参考文献

以下是关于OSTN重组蛋白的模拟参考文献示例(实际文献需通过学术数据库验证):

1. **《高效表达OSTN重组蛋白的大肠杆菌系统构建及活性分析》**

作者:张伟等

摘要:研究通过优化密码子及表达条件,在大肠杆菌中高效表达可溶性OSTN重组蛋白,并验证其促进成骨细胞分化的生物学活性。

2. **《重组OSTN蛋白对代谢综合征小鼠模型的治疗作用》**

作者:Chen L, et al.

摘要:利用哺乳动物细胞表达体系制备OSTN重组蛋白,实验证明其可通过调节脂代谢通路改善小鼠胰岛素抵抗及肥胖表型。

3. **《OSTN-Fc融合蛋白的制备及其长效促骨愈合效应研究》**

作者:Kim J, et al.

摘要:通过基因工程技术构建OSTN与IgG Fc段的融合蛋白,证实其半衰期延长且显著加速大鼠骨折模型中的骨痂形成。

4. **《重组人OSTN蛋白晶体结构解析及功能域鉴定》**

作者:Smith RD, et al.

摘要:利用X射线衍射技术解析OSTN蛋白三维结构,确定其关键活性区域,为靶向药物设计提供结构基础。

**注**:以上为模拟内容,实际文献需通过PubMed、Web of Science等平台检索关键词(如"recombinant osteocrin"或"OSTN protein expression")。

背景信息

OSTN (osteocrin), also known as Musclin, is a secreted protein encoded by the OSTN gene, initially identified as a skeletal muscle-derived factor with structural homology to natriuretic peptides. Discovered in 2004. it shares partial sequence similarity with atrial natriuretic peptide (ANP) and brain natriuretic peptide (BNP) but lacks their characteristic ring structure. OSTN is predominantly expressed in skeletal muscle, bone, and adipose tissue, suggesting roles in energy metabolism and musculoskeletal interactions.

Recombinant OSTN protein is engineered using expression systems like E. coli or mammalian cells to study its biological functions. Research highlights its dual regulatory capacity: 1) It binds natriuretic peptide receptors (NPRs), particularly NPR-C, modulating cyclic GMP signaling pathways involved in cardiovascular and metabolic processes; 2) It enhances energy expenditure by promoting mitochondrial biogenesis and thermogenesis in brown adipose tissue. Animal studies indicate OSTN improves glucose tolerance, reduces fat accumulation, and enhances bone formation. Notably, exercise upregulates OSTN expression, linking it to exercise-induced metabolic benefits.

Potential therapeutic applications include treating obesity, diabetes, osteoporosis, and cardiovascular diseases. However, its clinical relevance remains exploratory, with ongoing studies addressing its receptor specificity, tissue-specific effects, and long-term safety. OSTN’s unique position at the muscle-bone-fat axis makes it a compelling target for metabolic disorder therapeutics.

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