| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GLG1 |
| Uniprot No | Q92896 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1179aa |
| 氨基酸序列 | MAACGRVRRMFRLSAALHLLLLFAAGAEKLPGQGVHSQGQGPGANFVSFVGQAGGGGPAGQQLPQLPQSSQLQQQQQQQQQQQQPQPPQPPFPAGGPPARRGGAGAGGGWKLAEEESCREDVTRVCPKHTWSNNLAVLECLQDVREPENEISSDCNHLLWNYKLNLTTDPKFESVAREVCKSTITEIKECADEPVGKGYMVSCLVDHRGNITEYQCHQYITKMTAIIFSDYRLICGFMDDCKNDINILKCGSIRLGEKDAHSQGEVVSCLEKGLVKEAEEREPKIQVSELCKKAILRVAELSSDDFHLDRHLYFACRDDRERFCENTQAGEGRVYKCLFNHKFEESMSEKCREALTTRQKLIAQDYKVSYSLAKSCKSDLKKYRCNVENLPRSREARLSYLLMCLESAVHRGRQVSSECQGEMLDYRRMLMEDFSLSPEIILSCRGEIEHHCSGLHRKGRTLHCLMKVVRGEKGNLGMNCQQALQTLIQETDPGADYRIDRALNEACESVIQTACKHIRSGDPMILSCLMEHLYTEKMVEDCEHRLLELQYFISRDWKLDPVLYRKCQGDASRLCHTHGWNETSEFMPQGAVFSCLYRHAYRTEEQGRRLSRECRAEVQRILHQRAMDVKLDPALQDKCLIDLGKWCSEKTETGQELECLQDHLDDLVVECRDIVGNLTELESEDIQIEALLMRACEPIIQNFCHDVADNQIDSGDLMECLIQNKHQKDMNEKCAIGVTHFQLVQMKDFRFSYKFKMACKEDVLKLCPNIKKKVDVVICLSTTVRNDTLQEAKEHRVSLKCRRQLRVEELEMTEDIRLEPDLYEACKSDIKNFCSAVQYGNAQIIECLKENKKQLSTRCHQKVFKLQETEMMDPELDYTLMRVCKQMIKRFCPEADSKTMLQCLKQNKNSELMDPKCKQMITKRQITQNTDYRLNPMLRKACKADIPKFCHGILTKAKDDSELEGQVISCLKLRYADQRLSSDCEDQIRIIIQESALDYRLDPQLQLHCSDEISSLCAEEAAAQEQTGQVEECLKVNLLKIKTELCKKEVLNMLKESKADIFVDPVLHTACALDIKHHCAAITPGRGRQMSCLMEALEDKRVRLQPECKKRLNDRIEMWSYAAKVAPADGFSDLAMQVMTSPSKNYILSVISGSICILFLIGLMCGRITKRVTRELKDR |
| 预测分子量 | 134,5 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. |
以下是关于GLG1重组蛋白的模拟参考文献示例(实际文献需通过学术数据库查询)：
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1. **"Expression and Purification of Recombinant GLG1 in Mammalian Cells"**
*作者：Chen L, et al.*
**摘要**：研究通过哺乳动物表达系统成功表达并纯化GLG1重组蛋白，验证其糖基化修饰及细胞定位，为后续功能研究提供工具。
2. **"GLG1 Recombinant Protein Promotes Neuronal Adhesion via Integrin Signaling"**
*作者：Martinez R, et al.*
**摘要**：发现重组GLG1蛋白通过调控整合素信号通路增强神经元黏附，提示其在神经发育或修复中的潜在作用。
3. **"Structural Characterization of GLG1 Using Cryo-EM and Recombinant Protein Technology"**
*作者：Kim S, et al.*
**摘要**：利用冷冻电镜解析GLG1重组蛋白的三维结构，揭示其与配体结合的关键结构域，为靶向药物设计提供依据。
4. **"Recombinant GLG1 as a Biomarker in Cancer Metastasis Models"**
*作者：Wang Y, et al.*
**摘要**：通过肿瘤细胞模型证明，外源性GLG1重组蛋白可抑制癌细胞迁移，提示其作为肿瘤治疗靶点的可能性。
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**注**：以上为模拟文献，真实研究需通过PubMed、Google Scholar等平台检索关键词(如"GLG1 recombinant protein"+"expression/function")。
**Background of Recombinant GLG1 Protein**
The Golgi apparatus protein 1 (GLG1), also known as EGF-containing fibulin-like extracellular matrix protein 2 (EFEMP2), is a transmembrane glycoprotein primarily localized in the Golgi apparatus and secretory vesicles. It plays a critical role in regulating intracellular trafficking, protein sorting, and secretion. Structurally, GLG1 contains multiple epidermal growth factor (EGF)-like domains and a fibulin-like region, enabling interactions with extracellular matrix components and signaling molecules. Its involvement in modulating pathways like TGF-β, Wnt, and integrin signaling highlights its importance in cellular communication, tissue development, and homeostasis.
Recombinant GLG1 protein is engineered using biotechnological platforms, such as mammalian or insect cell expression systems, to ensure proper post-translational modifications (e.g., glycosylation). The production involves cloning the GLG1 gene into expression vectors, followed by purification via affinity chromatography. This recombinant form retains the functional domains of native GLG1. making it valuable for *in vitro* and *in vivo* studies.
Research on recombinant GLG1 has shed light on its dual roles in health and disease. It is implicated in cancer progression, angiogenesis, and fibrosis, acting either as a tumor suppressor or promoter depending on context. For instance, GLG1 regulates extracellular matrix remodeling and cell adhesion, influencing metastasis. Additionally, its interaction with growth factors positions it as a potential therapeutic target or biomarker for diseases like fibrosis and cardiovascular disorders.
Despite advancements, challenges remain in fully elucidating GLG1's signaling mechanisms and tissue-specific functions. Ongoing studies aim to leverage recombinant GLG1 to dissect molecular pathways and develop targeted therapies, underscoring its growing relevance in biomedical research.
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