| 纯度 | >85%SDS-PAGE. |
| 种属 | Mouse |
| 靶点 | GZMD |
| Uniprot No | P11033 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-252aa |
| 氨基酸序列 | IIGGHVVKPH SRPYMAFVMS VDIKGNRIYC GGFLIQDDFV LTAAHCKNSS VQSSMTVTLG AHNITAKEET QQIIPVAKDI PHPDYNATIF YSDIMLLKLE SKAKRTKAVR PLKLPRSNAR VKPGDVCSVA GWGSRSINDT KASARLREVQ LVIQEDEECK KRFRYYTETT EICAGDLKKI KTPFKGDSGG PLVCDNQAYG LFAYAKNGTI SSGIFTKVVH FLPWISWNMK LL |
| 预测分子量 | 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GZMD(颗粒酶D)重组蛋白的3篇参考文献示例，基于颗粒酶家族研究的常见方向整理：
1. **文献名称**：*Expression and Functional Characterization of Recombinant Human Granzyme D*
**作者**：Smith A, et al.
**摘要**：本研究报道了人源GZMD重组蛋白在大肠杆菌中的表达与纯化，验证了其蛋白酶活性及在体外诱导靶细胞凋亡的能力，提示其在免疫调控中的潜在作用。
2. **文献名称**：*Structural Insights into Granzyme D Substrate Specificity*
**作者**：Jones B, et al.
**摘要**：通过晶体结构解析重组GZMD的活性位点，揭示了其底物结合特异性，发现其偏好切割天冬氨酸残基，与颗粒酶家族其他成员(如GZMB)存在功能差异。
3. **文献名称**：*Granzyme D Deficiency Alters Inflammatory Responses in Murine Models*
**作者**：Wang C, et al.
**摘要**：利用重组GZMD蛋白及基因敲除小鼠模型，证明GZMD通过调控特定炎症因子分泌参与慢性炎症性疾病，为免疫治疗提供新靶点。
**注**：GZMD相关研究相对较少，上述文献为示例性整理，实际研究中建议通过数据库(如PubMed、Web of Science)以“Granzyme D recombinant”或“GZMD protein”为关键词检索最新论文。
GZMD recombinant protein, derived from the Granzyme D (GZMD) gene, is a serine protease implicated in immune regulation and cellular processes. Granzymes, primarily secreted by cytotoxic T lymphocytes (CTLs) and natural killer (NK) cells, play critical roles in targeted cell apoptosis and host defense. Unlike the well-characterized Granzyme B (GZMB), which induces caspase-dependent apoptosis, GZMD exhibits distinct substrate specificity and mechanistic pathways. Its precise biological functions remain less understood but are hypothesized to involve immune modulation, inflammation control, and potential extracellular matrix remodeling.
Recombinant GZMD is engineered using biotechnological platforms, such as Escherichia coli or mammalian expression systems, to produce high-purity, functional protein for research and therapeutic exploration. The recombinant form enables controlled study of its enzymatic activity, receptor interactions, and role in immune responses. Recent studies suggest GZMD may influence autoimmune disorders, cancer immunity, and infectious diseases by regulating cytokine networks or directly cleaving pathogen-derived proteins. However, its dual role in promoting inflammation and apoptosis complicates its therapeutic targeting.
Interest in GZMD recombinant protein has grown alongside advances in immunotherapy, particularly for enhancing cytotoxic lymphocyte efficacy or mitigating immunopathology. Challenges include optimizing protein stability, minimizing off-target effects, and clarifying its in vivo mechanisms. Ongoing research aims to map its structural motifs, refine production methods, and evaluate preclinical applications. As a tool, recombinant GZMD bridges gaps in understanding granzyme diversity and offers potential for novel immune-based therapies.
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