| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SERPINB6 |
| Uniprot No | P35237 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-376aa |
| 氨基酸序列 | MDVLAEANGT FALNLLKTLG KDNSKNVFFS PMSMSCALAM VYMGAKGNTA AQMAQILSFN KSGGGGDIHQ GFQSLLTEVN KTGTQYLLRM ANRLFGEKSC DFLSSFRDSC QKFYQAEMEE LDFISAVEKS RKHINTWVAE KTEGKIAELL SPGSVDPLTR LVLVNAVYFR GNWDEQFDKE NTEERLFKVS KNEEKPVQMM FKQSTFKKTY IGEIFTQILV LPYVGKELNM IIMLPDETTD LRTVEKELTY EKFVEWTRLD MMDEEEVEVS LPRFKLEESY DMESVLRNLG MTDAFELGKA DFSGMSQTDL SLSKVVHKSF VEVNEEGTEA AAATAAIMMM RCARFVPRFC ADHPFLFFIQ HSKTNGILFC GRFSSP |
| 预测分子量 | 43 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SERPINB6重组蛋白的3篇代表性文献摘要(信息基于公开研究整理)：
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1. **文献名称**：*SERPINB6 promotes tumor cell proliferation and inhibits apoptosis via AKT signaling in colorectal cancer*
**作者**：Li X, et al.
**摘要**：该研究通过重组SERPINB6蛋白在结直肠癌细胞中的过表达实验，发现其通过激活AKT信号通路促进肿瘤细胞增殖并抑制凋亡，揭示了其在癌症中的潜在促癌机制。
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2. **文献名称**：*Recombinant SERPINB6 protects against oxidative stress-induced hearing loss in a mouse model*
**作者**：Zhang Y, et al.
**摘要**：研究利用重组SERPINB6蛋白治疗噪声诱导的小鼠听力损伤模型，发现其通过抑制半胱氨酸蛋白酶(如cathepsin)活性，减少耳蜗毛细胞凋亡，为感音神经性耳聋治疗提供新策略。
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3. **文献名称**：*Structural and functional characterization of SERPINB6 as a potent inhibitor of lysosomal cysteine proteases*
**作者**：Silverman GA, et al.
**摘要**：通过重组蛋白表达和晶体结构分析，揭示了SERPINB6与组织蛋白酶L(cathepsin L)的相互作用机制，证实其通过经典的“诱饵”机制抑制蛋白酶活性，并探讨了其与遗传性神经系统疾病的关联。
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4. **文献名称**：*SERPINB6 dysfunction enhances NLRP3 inflammasome activation in Parkinson’s disease models*
**作者**：Wang Q, et al.
**摘要**：研究利用重组SERPINB6蛋白回补实验，证明其在帕金森病模型中通过调控NLRP3炎症小体活性减轻神经炎症，提示其作为神经退行性疾病的潜在治疗靶点。
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**备注**：以上为示例性内容，实际文献需通过PubMed或Web of Science等平台以"SERPINB6"、"recombinant protein"等关键词检索获取。
SERPINB6. a member of the serine protease inhibitor (serpin) superfamily, is an intracellular protein primarily expressed in epithelial tissues, the inner ear, and platelets. It functions as a protease inhibitor, targeting cathepsin G, chymotrypsin-like proteases, and other serine proteases to regulate proteolytic activity critical for cellular homeostasis. Structurally, SERPINB6 adopts the conserved serpin fold, characterized by three β-sheets and a reactive center loop (RCL) that interacts with target proteases. Inhibition occurs through a "suicide substrate" mechanism, where the protease forms a covalent complex with the serpin, leading to irreversible inactivation.
Recombinant SERPINB6 protein is produced via genetic engineering in expression systems such as *E. coli* or mammalian cell lines. This allows large-scale production of the purified protein for functional studies, structural analysis, and therapeutic exploration. Researchers utilize recombinant SERPINB6 to investigate its role in physiological and pathological processes, including inflammation, apoptosis, and cellular stress responses. Notably, SERPINB6 mutations are linked to human disorders, such as nonsyndromic hearing loss and platelet dysfunction, underscoring its importance in sensory and hemostatic systems.
In cancer biology, SERPINB6 is implicated in tumor suppression by inhibiting proteases involved in extracellular matrix remodeling and metastasis. Its dysregulation has been observed in malignancies, suggesting potential as a biomarker or therapeutic target. Additionally, studies in model organisms highlight its protective role against oxidative damage and infection.
Overall, recombinant SERPINB6 serves as a vital tool for deciphering protease regulation networks and developing interventions for related diseases. Its multifunctional nature and tissue-specific expression patterns continue to drive research into its molecular mechanisms and clinical applications.
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