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Recombinant Human CYGB protein

  • 中文名: 细胞球蛋白(CYGB)重组蛋白
  • 别    名: CYGB;STAP;Cytoglobin
货号: PA1000-4345
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点CYGB
Uniprot No Q8WWM9
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-190aa
氨基酸序列MGSSHHHHHHSSGLVPRGSHMEKVPGEMEIERRERSEELSEAERKAVQAM WARLYASCEDVGVAILVRFFVNFPSAKQYFSQFKHMEDPLEMERSPQLRK HACRVMGALNTVVENLHDPDKVSSVLALVGKAHALKHKVEPVYFKILSGV ILEVVAEEFASDFPPETQRAWAKLRGLIYSHVTAAYKEVGWVQQVPNATT PPATLPSSGP
预测分子量24 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CYGB(细胞球蛋白)重组蛋白的模拟参考文献示例(非真实文献,仅供格式参考):

1. **标题**: "Recombinant Human Cytoglobin: Expression, Purification, and Antioxidant Activity"

**作者**: Smith A, et al.

**摘要**: 研究报道了在大肠杆菌中高效表达并纯化重组人CYGB蛋白的方法,验证其体外抗氧化活性,提示其在氧化应激相关疾病中的潜在应用。

2. **标题**: "Cytoglobin Overexpression Attenuates Hepatic Fibrosis in a Mouse Model"

**作者**: Chen L, et al.

**摘要**: 通过重组CYGB蛋白在小鼠肝纤维化模型中的干预实验,证明其通过抑制星状细胞活化减少胶原沉积,揭示其抗纤维化机制。

3. **标题**: "Structural Characterization of Recombinant Cytoglobin Using X-ray Crystallography"

**作者**: Tanaka K, et al.

**摘要**: 解析了重组CYGB蛋白的三维晶体结构,发现其血红素结合位点的独特构象,为理解其氧结合与信号转导功能提供结构基础。

4. **标题**: "Recombinant Cytoglobin as a Therapeutic Agent in Ischemia-Reperfusion Injury"

**作者**: Müller R, et al.

**摘要**: 在心脏缺血再灌注损伤模型中,重组CYGB蛋白通过减少ROS生成改善组织损伤,提示其作为新型治疗分子的潜力。

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注:以上文献为示例性内容,实际研究中请通过学术数据库(如PubMed、Web of Science)检索真实发表的论文。

背景信息

**Background of CYGB Recombinant Protein**

Cytoglobin (CYGB), a member of the globin family, is a ubiquitously expressed intracellular protein initially discovered in 2002. It shares structural homology with hemoglobin and myoglobin but exhibits distinct tissue distribution and functional roles. CYGB is primarily localized in fibroblasts, stromal cells, and specific neuronal populations, where it participates in cellular responses to hypoxia, oxidative stress, and nitric oxide metabolism. Its hexacoordinate heme-binding structure allows reversible oxygen binding, though its precise physiological function remains under investigation.

Recombinant CYGB protein is engineered using genetic cloning techniques, often expressed in *E. coli* or mammalian cell systems to ensure proper folding and post-translational modifications. This engineered protein retains native CYGB properties, enabling studies on its roles in oxygen homeostasis, ROS (reactive oxygen species) scavenging, and cytoprotective signaling. Research highlights CYGB's involvement in fibrotic diseases, cancer progression, and neurodegenerative disorders, where dysregulation correlates with oxidative damage or aberrant cell proliferation.

CYGB's potential as a therapeutic target or biomarker drives interest in recombinant forms. For instance, it may mitigate tissue fibrosis by modulating collagen synthesis or protect neurons via antioxidant mechanisms. Additionally, recombinant CYGB serves as a tool to explore interactions with cellular proteins, such as kinases and transcription factors, shedding light on its regulatory networks. Despite unresolved questions about its primary biological functions, CYGB recombinant protein remains pivotal in advancing mechanistic and translational studies across multiple disease contexts.

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