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Recombinant Human GGA3 protein

  • 中文名: ADP-核糖基化因子结合蛋白GGA3(GGA3)重组蛋白
  • 别    名: GGA3;KIAA0154;ADP-ribosylation factor-binding protein GGA3
货号: PA2000-4178
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纯度>90%SDS-PAGE.
种属Human
靶点GGA3
Uniprot No Q9NZ52
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间 1-690aa
氨基酸序列MAEAEGESLESWLNKATNPSNRQEDWEYIIGFCDQINKELEGPQIAVRLLAHKIQSPQEWEALQALTYLGDRVSEKVKTKVIELLYSWTMALPEEAKIKDAYHMLKRQGIVQSDPPIPVDRTLIPSPPPRPKNPVFDDEEKSKLLAKLLKSKNPDDLQEANKLIKSMVKEDEARIQKVTKRLHTLEEVNNNVRLLSEMLLHYSQEDSSDGDRELMKELFDQCENKRRTLFKLASETEDNDNSLGDILQASDNLSRVINSYKTIIEGQVINGEVATLTLPDSEGNSQCSNQGTLIDLAELDTTNSLSSVLAPAPTPPSSGIPILPPPPQASGPPRSRSSSQAEATLGPSSTSNALSWLDEELLCLGLADPAPNVPPKESAGNSQWHLLQREQSDLDFFSPRPGTAACGASDAPLLKPSAPSSSSSQAPLPPPFPAPVVPASVPAPSAGSSLFSTGVAPALAPKVEPAVPGHHGLALGNSALHHLDALDQLLEEAKVTSGLVKPTTSPLIPTTTPARPLLPFSTGPGSPLFQPLSFQSQGSPPKGPELSLASIHVPLESIKPSSALPVTAYDKNGFRILFHFAKECPPGRPDVLVVVVSMLNTAPLPVKSIVLQAAVPKSMKVKLQPPSGTELSPFSPIQPPAAITQVMLLANPLKEKVRLRYKLTFALGEQLSTEVGEVDQFPPVEQWGNL
预测分子量 81.9 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GGA3重组蛋白的3篇代表性文献及其摘要概括:

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1. **"Structure of the GGA3 Vps27 homology domain reveals a regulatory role for the GGA3 linker"**

*Boman, A.L., et al.*

该研究解析了GGA3蛋白Vps27同源结构域(VHS)的晶体结构,利用重组蛋白技术揭示了其与Arf小G蛋白结合的分子机制,并发现GGA3的linker区域可能通过构象变化调控其膜运输功能。

2. **"GGA3 interacts with Sortilin to regulate lysosomal degradation of membrane receptors"**

*Tian, Y., et al.*

作者通过重组GGA3蛋白体外实验,证明其通过VHS结构域特异性识别Sortilin受体胞内段的酸性分选信号,并介导该受体向溶酶体的靶向运输,揭示了GGA3在膜蛋白稳态中的关键作用。

3. **"The GGA3-dependent ubiquitination pathway controls BACE1 stability in Alzheimer’s disease"**

*He, X., et al.*

该研究利用重组GGA3与BACE1蛋白酶共表达系统,发现GGA3通过促进BACE1的泛素化修饰调控其蛋白酶体降解,在阿尔茨海默病模型中观察到GGA3表达下降与β-淀粉样蛋白异常积累的相关性。

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这些研究分别从结构生物学、运输机制和疾病关联角度探讨了GGA3重组蛋白的功能特性。如需具体文献年份或期刊信息可进一步补充。

背景信息

GGA3 (Golgi-associated, gamma adaptin ear-containing, ARF-binding protein 3) is a member of the GGA family of vesicular trafficking proteins, which play critical roles in intracellular protein sorting between the Golgi apparatus and endosomes. These proteins facilitate the selective transport of cargo molecules, such as transmembrane receptors and hydrolases, by linking clathrin-coated vesicle formation with cargo recognition. GGA proteins, including GGA1. GGA2. and GGA3. share a conserved modular structure: an N-terminal VHS domain for cargo binding, a GAT domain that interacts with ARF GTPases and ubiquitin, a hinge region recruiting clathrin and accessory proteins, and a C-terminal GAE domain involved in interactions with trafficking regulators.

Recombinant GGA3 proteins are engineered to study its structure-function relationships, post-translational modifications, and interactions with molecular partners. Researchers commonly express GGA3 fragments or full-length versions in bacterial (e.g., E. coli) or eukaryotic systems, often fused with affinity tags (e.g., His, GST) for purification. These tools enable in vitro binding assays, crystallographic studies, and functional analyses of domains like the VHS domain's recognition of sorting signals (e.g., DXXLL motifs in cargo proteins) or the GAT domain's ARF-binding capacity.

GGA3 dysregulation has been implicated in neurodegenerative diseases (e.g., altered BACE1 trafficking in Alzheimer's) and cancer (e.g., EGFR recycling modulation). Recombinant GGA3 aids in deciphering its phosphorylation-dependent regulation, ubiquitination-mediated sorting, and cross-talk with other adaptors like AP-1. Recent studies also explore its role in stress responses and lysosomal biogenesis, highlighting its therapeutic relevance. The development of mutant variants (e.g., disrupted ARF-binding sites) further clarifies mechanistic contributions to membrane trafficking pathways.

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