| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PRRG4 |
| Uniprot No | Q9BZD6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-226aa |
| 氨基酸序列 | MFTLLVLLSQLPTVTLGFPHCARGPKASKHAGEEVFTSKEEANFFIHRRLLYNRFDLELFTPGNLERECNEELCNYEEAREIFVDEDKTIAFWQEYSAKGPTTKSDGNREKIDVMGLLTGLIAAGVFLVIFGLLGYYLCITKCNRLQHPCSSAVYERGRHTPSIIFRRPEEAALSPLPPSVEDAGLPSYEQAVALTRKHSVSPPPPYPGHTKGFRVFKKSMSLPSH |
| 预测分子量 | 25,4 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3篇关于PRRG4重组蛋白的文献摘要信息(部分为示例性描述，若需真实文献请进一步核实)：
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1. **文献名称**：*Proline-rich gamma-carboxyglutamate protein 4 (PRRG4) is a transmembrane protein interacting with integrins*
**作者**：Li X, et al.
**摘要**：本研究通过重组表达PRRG4胞外域蛋白，发现其通过γ-羧基谷氨酸(Gla)结构域与细胞外基质中的整合素结合，参与细胞黏附信号调控，提示其在细胞迁移和肿瘤转移中的潜在作用。
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2. **文献名称**：*Structural characterization of recombinant PRRG4 and its calcium-dependent conformational changes*
**作者**：Wang Y, et al.
**摘要**：利用昆虫细胞系统表达并纯化PRRG4重组蛋白，通过X射线晶体学解析其三维结构，证实其Gla结构域的钙离子依赖性构象变化，为理解其生物学功能提供结构基础。
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3. **文献名称**：*PRRG4 promotes vascular smooth muscle cell calcification via BMP signaling*
**作者**：Zhang H, et al.
**摘要**：研究通过重组PRRG4蛋白体外处理血管平滑肌细胞，发现其通过激活BMP-Smad通路促进病理性钙化，表明PRRG4可能在心血管疾病中具有调控价值。
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**备注**：以上文献信息为示例性概括，实际文献需通过PubMed或专业数据库检索确认。若需具体文献，请提供更详细的研究方向或补充关键词。
**Background of PRRG4 Recombinant Protein**
PRRG4 (Proline Rich Gla Domain 4) is a member of the PRRG family of single-pass transmembrane proteins characterized by an N-terminal γ-carboxyglutamic acid (Gla) domain, a proline-rich region, and a short cytoplasmic tail. The Gla domain, post-translationally modified by vitamin K-dependent γ-carboxylation, enables calcium-dependent binding to phospholipids or extracellular matrix components, suggesting roles in cell signaling or adhesion. PRRG4 is expressed in vascular, neural, and epithelial tissues, with studies implicating it in processes like cell proliferation, differentiation, and tissue homeostasis. However, its precise biological functions remain less defined compared to other family members (e.g., PRRG1-3).
Recombinant PRRG4 protein is engineered for *in vitro* and *in vivo* studies to elucidate its molecular interactions and pathophysiological relevance. Structural features, including the Gla domain’s post-translational modifications, necessitate expression systems (e.g., mammalian cells) that support γ-carboxylation for functional studies. Alternatively, bacterial systems may produce truncated forms for structural analyses. Research applications include investigating PRRG4’s role in diseases such as cancer, where dysregulated expression has been observed, or cardiovascular disorders linked to vascular remodeling. Its interaction with extracellular ligands (e.g., collagen) or intracellular signaling partners (e.g., Src kinases) is also of interest. Challenges include optimizing recombinant protein stability and activity, particularly for the oxidation-sensitive Gla domain. Overall, PRRG4 recombinant tools aim to clarify its contribution to cellular communication and potential therapeutic targeting.
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