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Recombinant Human GGH protein

  • 中文名: γ-谷氨酰水解酶(GGH)重组蛋白
  • 别    名: GGH;Gamma-glutamyl hydrolase
货号: PA1000-1235
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点GGH
Uniprot NoQ92820
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间25-318aa
氨基酸序列MGSSHHHHHHSSGLVPRGSHMRPHGDTAKKPIIGILMQKCRNKVMKNYGR YYIAASYVKYLESAGARVVPVRLDLTEKDYEILFKSINGILFPGGSVDLR RSDYAKVAKIFYNLSIQSFDDGDYFPVWGTCLGFEELSLLISGECLLTAT DTVDVAMPLNFTGGQLHSRMFQNFPTELLLSLAVEPLTANFHKWSLSVKN FTMNEKLKKFFNVLTTNTDGKIEFISTMEGYKYPVYGVQWHPEKAPYEWK NLDGISHAPNAVKTAFYLAEFFVNEARKNNHHFKSESEEEKALIYQFSPI YTGNISSFQQCYIFD
预测分子量36 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 **GGH(γ-谷氨酰水解酶)重组蛋白** 的3篇代表性文献及其摘要概括:

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1. **文献名称**: *Cloning and Stable Expression of Human γ-Glutamyl Hydrolase (GGH) in a Human Cell Line*

**作者**: Moran, R.G., et al.

**摘要**: 该研究成功克隆了人类GGH的cDNA,并在哺乳动物细胞系中实现了稳定表达。通过重组蛋白的功能分析,发现GGH在叶酸代谢中起关键作用,并可能影响甲氨蝶呤(MTX)等抗叶酸药物的细胞内代谢和耐药性。

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2. **文献名称**: *Crystal Structure of γ-Glutamyl Hydrolase from Arabidopsis thaliana*

**作者**: Shane, B., et al.

**摘要**: 研究通过X射线晶体学解析了拟南芥来源的GGH三维结构,揭示了其底物结合位点和催化机制。重组蛋白的酶活实验表明,GGH通过水解多聚谷氨酰链调控叶酸衍生物的生物学活性,为设计靶向GGH的药物提供结构基础。

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3. **文献名称**: *GGH Overexpression in Cancer Cells: Implications for Chemotherapy Resistance*

**作者**: Rhee, M.S., et al.

**摘要**: 研究发现多种癌细胞中GGH的异常高表达与甲氨蝶呤耐药性显著相关。通过重组GGH蛋白的功能验证,证明其通过加速叶酸类似物的代谢降低药物疗效,提示抑制GGH活性可能成为克服化疗耐药的新策略。

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**备注**:以上文献为示例,实际引用时需核对具体来源及数据库(如PubMed、ScienceDirect)。如需更精准的文献,建议结合关键词“GGH recombinant protein”或“gamma-glutamyl hydrolase expression”进一步检索。

背景信息

**Background of Recombinant GGH Protein**

Gamma-glutamyl hydrolase (GGH), also known as folate hydrolase or conjugase, is a lysosomal enzyme that plays a critical role in folate metabolism by cleaving polyglutamate chains from dietary folate derivatives. This process converts polyglutamylated folates into monoglutamate forms, enabling their cellular export or retention. GGH’s activity influences intracellular folate levels, which are vital for nucleotide synthesis, DNA repair, and methylation reactions. Dysregulation of GGH expression has been linked to diseases, including cancer and neural tube defects, as well as altered efficacy of antifolate chemotherapies like methotrexate.

Recombinant GGH protein is produced using genetic engineering techniques, where the *GGH* gene is cloned into expression vectors and expressed in host systems (e.g., *E. coli*, mammalian cells). This allows large-scale production of purified, bioactive GGH for research and therapeutic applications. Recombinant GGH is widely used to study folate metabolism mechanisms, screen antifolate drugs, and explore its role in cancer resistance. For instance, elevated GGH levels in tumors can reduce the retention of antifolates, diminishing chemotherapy effects. Understanding GGH’s structure-function relationships through recombinant protein studies aids in designing inhibitors to modulate its activity.

Challenges in producing recombinant GGH include ensuring proper post-translational modifications (e.g., glycosylation in eukaryotic systems) and maintaining enzyme stability. Advances in protein engineering and structural biology (e.g., X-ray crystallography) have improved production strategies, enabling precise characterization of GGH’s catalytic site and substrate interactions. Current research focuses on leveraging recombinant GGH as a therapeutic target or biomarker to optimize folate-related treatments and personalize cancer therapies.

In summary, recombinant GGH protein serves as a vital tool for elucidating folate biology and developing strategies to address folate-linked pathologies and drug resistance.

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