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Recombinant Human CRYGC protein

  • 中文名: 晶状体蛋白γC(CRYGC)重组蛋白
  • 别    名: CRYGC;CRYG3;Gamma-crystallin C
货号: PA1000-725DB
Price: ¥询价
数量:
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产品详情

纯度>95%SDS-PAGE.
种属Human
靶点CRYGC
Uniprot NoP07315
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-174aa
氨基酸序列MGSSHHHHHH SSGLVPRGSH MGSHMGKITF YEDRAFQGRS YETTTDCPNL QPYFSRCNSI RVESGCWMLY ERPNYQGQQY LLRRGEYPDYQQWMGLSDSI RSCCLIPQTV SHRLRLYERE DHKGLMMELS EDCPSIQDRF HLSEIRSLHV LEGCWVLYEL PNYRGRQYLL RPQEYRRCQDWGAMDAKAGS LRRVVDLY
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CRYGC重组蛋白的模拟参考文献示例(请注意,以下内容为假设性描述,实际文献需通过学术数据库查询):

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1. **《Expression and purification of recombinant human CRYGC in Escherichia coli for structural studies》**

- **作者**: Zhang L, et al.

- **摘要**: 本研究成功构建了人源CRYGC基因的重组表达载体,并利用大肠杆菌系统实现高效表达。通过亲和层析纯化获得高纯度蛋白,经圆二色谱和X射线晶体学分析证实其正确折叠,为后续白内障相关突变体的结构功能研究奠定基础。

2. **《Functional analysis of cataract-associated mutations in CRYGC using recombinant protein models》**

- **作者**: Wang Y, et al.

- **摘要**: 通过重组CRYGC蛋白模拟常见致白内障突变(如R58H),发现突变体蛋白热稳定性显著降低,易形成聚集体。研究揭示了CRYGC突变导致晶状体浑浊的分子机制,为靶向治疗提供理论依据。

3. **《Biophysical characterization of recombinant CRYGC under oxidative stress conditions》**

- **作者**: Kumar S, et al.

- **摘要**: 利用重组CRYGC蛋白分析氧化应激(如H₂O₂处理)对其溶解度的影响,发现CRYGC在氧化环境下易发生错误折叠和聚集,提示其在年龄相关性白内障中的潜在作用。

4. **《Optimization of CRYGC recombinant protein production in mammalian expression systems》**

- **作者**: Chen H, et al.

- **摘要**: 比较大肠杆菌、昆虫细胞及哺乳动物系统表达CRYGC的效率,发现哺乳动物系统(如HEK293)可产生更接近天然构象的蛋白,适用于药物筛选和抗体开发。

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**建议**:如需真实文献,可通过以下方式检索:

1. 访问 **PubMed** 或 **Google Scholar**,搜索关键词:`"CRYGC recombinant protein"` 或 `"gamma-crystallin recombinant expression"`。

2. 筛选近年研究,重点关注蛋白表达、突变分析或疾病机制相关论文。

背景信息

CRYGC (Gamma-Crystallin C) is a member of the crystallin protein family, primarily expressed in the lens of the eye. As a key structural component, it contributes to the transparency and refractive properties of the lens, enabling proper light focusing onto the retina. Crystallins, including CRYGC, are classified into α, β, and γ families, with γ-crystallins being highly abundant in the lens nucleus. CRYGC is encoded by the *CRYGC* gene, located on chromosome 2 in humans, and consists of two highly conserved Greek key motifs that stabilize its tertiary structure, critical for maintaining lens clarity under physiological stress.

Recombinant CRYGC protein is produced using heterologous expression systems (e.g., *E. coli* or mammalian cell lines) to study its biochemical properties, structural dynamics, and pathological roles. Mutations in *CRYGC* are linked to congenital cataracts, a leading cause of childhood blindness. These mutations often disrupt protein solubility or promote aggregation, leading to lens opacification. Recombinant CRYGC allows researchers to dissect mutation-driven misfolding mechanisms, screen therapeutic agents, or engineer mutants to mimic disease phenotypes.

Studies using recombinant CRYGC have revealed its susceptibility to oxidative stress and UV-induced damage, factors implicated in age-related cataracts. Its high thermodynamic stability and compact structure make it a model for investigating protein folding diseases. Additionally, recombinant CRYGC is utilized in structural biology (e.g., X-ray crystallography, NMR) to resolve conformational changes and interactions with chaperones or small molecules. Challenges remain in mimicking post-translational modifications (e.g., phosphorylation) in vitro, which may influence its function. Overall, recombinant CRYGC serves as a vital tool for understanding cataract pathogenesis and developing targeted therapies.

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