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Recombinant Human NAALAD2 Protein

  • 中文名: 重组人(NAALAD2)蛋白
  • 别    名: Glutamate carboxypeptidase III;GCPIII;N-acetylated-alpha-linked acidic dipeptidase II;NAALADase II
货号: PA2000-9583
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点NAALAD2
Uniprot NoQ9Y3Q0
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间32-740 aa
活性数据KPLKETTTSVRYHQSIRWKLVSEMKAENIKSFLRSFTKLPHLAGTEQNFLLAKKIQTQWKKFGLDSAKLVHYDVLLSYPNETNANYISIVDEHETEIFKTSYLEPPPDGYENVTNIVPPYNAFSAQGMPEGDLVYVNYARTEDFFKLEREMGINCTGKIVIARYGKIFRGNKVKNAMLAGAIGIILYSDPADYFAPEVQPYPKGWNLPGTAAQRGNVLNLNGAGDPLTPGYPAKEYTFRLDVEEGVGIPRIPVHPIGYNDAEILLRYLGGIAPPDKSWKGALNVSYSIGPGFTGSDSFRKVRMHVYNINKITRIYNVVGTIRGSVEPDRYVILGGHRDSWVFGAIDPTSGVAVLQEIARSFGKLMSKGWRPRRTIIFASWDAEEFGLLGSTEWAEENVKILQERSIAYINSDSSIEGNYTLRVDCTPLLYQLVYKLTKEIPSPDDGFESKSLYESWLEKDPSPENKNLPRINKLGSGSDFEAYFQRLGIASGRARYTKNKKTDKYSSYPVYHTIYETFELVEKFYDPTFKKQLSVAQLRGALVYELVDSKIIPFNIQDYAEALKNYAASIYNLSKKHDQQLTDHGVSFDSLFSAVKNFSEAASDFHKRLIQVDLNNPIAVRMMNDQLMLLERAFIDPLGLPGKLFYRHIIFAPSSHNKYAGESFPGIYDAIFDIENKANSRLAWKEVKKHISIAAFTIQAAAGTLKEVL
分子量83 kDa
蛋白标签His tag N-Terminus
缓冲液0
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

以下是关于重组人NAALAD2蛋白的3-4篇参考文献示例(注:以下文献为示例性内容,可能非真实存在):

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1. **标题**: "Cloning and Functional Characterization of Recombinant Human NAALAD2: Implications in Prostate Cancer Metabolism"

**作者**: Bacich, D.J., Pinto, J.T., Tong, W.P., Heston, W.D.

**摘要**: 本研究成功克隆并表达了重组人NAALAD2蛋白,揭示了其作为叶酸水解酶和谷氨酸衍生物代谢酶的双重功能,并探讨其在前列腺癌细胞代谢及靶向治疗中的潜在作用。

2. **标题**: "Crystal Structure of Recombinant Human NAALAD2 Reveals Substrate-Binding Mechanisms"

**作者**: Mesters, J.R., Barinka, C., Hlouchová, K.

**摘要**: 通过X射线晶体学解析了重组人NAALAD2的三维结构,阐明了其底物结合位点的关键氨基酸残基,为设计选择性抑制剂治疗神经退行性疾病提供了结构基础。

3. **标题**: "Recombinant NAALAD2 Attenuates Glutamate Excitotoxicity in Neuronal Cell Models"

**作者**: Slusher, B.S., Thomas, A.G., Rojas, C.

**摘要**: 研究利用重组NAALAD2蛋白调控细胞外神经递质NAAG的水解,证明其通过降低谷氨酸浓度减轻神经元兴奋性毒性,提示其在脑卒中或创伤中的治疗潜力。

4. **标题**: "Optimized Expression and Purification of Human NAALAD2 in a Mammalian System for Drug Discovery"

**作者**: Chang, S.S., Heston, W.D., Zhou, J.

**摘要**: 开发了一种基于哺乳动物细胞的高效重组NAALAD2蛋白表达和纯化方法,验证了其酶活性和稳定性,为基于该靶点的高通量药物筛选奠定技术基础。

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**说明**:以上文献为模拟示例,实际研究中建议通过PubMed或Google Scholar以关键词“NAALAD2”、“PSMA homolog”、“recombinant”等检索最新研究。


背景信息

NAALAD2 (N-acetylated alpha-linked acidic dipeptidase 2), also known as glutamate carboxypeptidase III (GCPIII), is a zinc-dependent metallopeptidase belonging to the M28 peptidase family. It shares structural and functional similarities with NAALADase L1 (GCPII), a well-characterized enzyme involved in hydrolyzing the neuropeptide N-acetylaspartylglutamate (NAAG) into glutamate and N-acetylaspartate. NAALAD2 is encoded by the NAALAD2 gene in humans and is expressed in various tissues, including the brain, prostate, and testis. Though less studied than GCPII, it exhibits catalytic activity toward NAAG and other dipeptidase substrates, suggesting a potential role in modulating glutamate signaling and neurotransmitter homeostasis.

The protein features a conserved catalytic domain with a binuclear zinc-binding motif critical for its enzymatic function. Unlike GCPII, which localizes to the cell membrane via a transmembrane domain, NAALAD2 lacks this anchoring region and may exist in soluble or secreted forms. Studies suggest its involvement in diverse physiological and pathological processes, such as neuroprotection, cellular differentiation, and cancer progression. In prostate cancer, elevated NAALAD2 expression correlates with tumor aggressiveness, possibly through interactions with folate metabolism or signal transduction pathways.

Recombinant human NAALAD2 protein, produced via heterologous expression systems like Escherichia coli or mammalian cells, enables in vitro studies of its enzymatic kinetics, substrate specificity, and inhibitor screening. This tool aids in exploring its therapeutic potential for neurological disorders or cancers linked to dysregulated glutamate signaling. However, its precise biological functions and regulatory mechanisms remain under investigation, warranting further research to elucidate its role in health and disease.


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