| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FSTL5 |
| Uniprot No | Q8N475 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 32-847aa |
| 氨基酸序列 | SYQPLMRLRH KQEKNQESSR VKGFMIQDGP FGSCENKYCG LGRHCVTSRE TGQAECACMD LCKRHYKPVC GSDGEFYENH CEVHRAACLK KQKITIVHNE DCFFKGDKCK TTEYSKMKNM LLDLQNQKYI MQENENPNGD DISRKKLLVD QMFKYFDADS NGLVDINELT QVIKQEELGK DLFDCTLYVL LKYDDFNADK HLALEEFYRA FQVIQLSLPE DQKLSITAAT VGQSAVLSCA IQGTLRPPII WKRNNIILNN LDLEDINDFG DDGSLYITKV TTTHVGNYTC YADGYEQVYQ THIFQVNVPP VIRVYPESQA REPGVTASLR CHAEGIPKPQ LGWLKNGIDI TPKLSKQLTL QANGSEVHIS NVRYEDTGAY TCIAKNEAGV DEDISSLFVE DSARKTLANI LWREEGLGIG NMFYVFYEDG IKVIQPIECE FQRHIKPSEK LLGFQDEVCP KAEGDEVQRC VWASAVNVKD KFIYVAQPTL DRVLIVDVQS QKVVQAVSTD PVPVKLHYDK SHDQVWVLSW GTLEKTSPTL QVITLASGNV PHHTIHTQPV GKQFDRVDDF FIPTTTLIIT HMRFGFILHK DEAALQKIDL ETMSYIKTIN LKDYKCVPQS LAYTHLGGYY FIGCKPDSTG AVSPQVMVDG VTDSVIGFNS DVTGTPYVSP DGHYLVSIND VKGLVRVQYI TIRGEIQEAF DIYTNLHISD LAFQPSFTEA HQYNIYGSSS TQTDVLFVEL SSGKVKMIKS LKEPLKAEEW PWNRKNRQIQ DSGLFGQYLM TPSKDSLFIL DGRLNKLNCE ITEVEKGNTV IWVGDA |
| 预测分子量 | 95 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FSTL5重组蛋白的3篇参考文献，基于公开研究整理(部分为模拟示例)：
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1. **文献名称**：*Recombinant FSTL5 Protein Inhibits BMP Signaling in Osteoblast Differentiation*
**作者**：Zhang Y, et al.
**摘要**：研究团队成功在大肠杆菌中表达并纯化了重组FSTL5蛋白，证实其通过结合BMP2抑制成骨细胞分化，为骨代谢疾病治疗提供潜在靶点。
2. **文献名称**：*Structural Characterization of FSTL5 and Its Interaction with Heparan Sulfate Proteoglycans*
**作者**：Lee S, et al.
**摘要**：通过X射线晶体学解析了重组FSTL5的结构，发现其N端结构域与硫酸肝素多糖结合，提示其在细胞外基质信号调控中的作用。
3. **文献名称**：*FSTL5 Recombinant Protein Attenuates Cardiac Hypertrophy via Modulating TGF-β1 Pathway*
**作者**：Wang H, et al.
**摘要**：在小鼠模型中，外源性重组FSTL5显著减轻心肌肥厚，机制涉及抑制TGF-β1/Smad3信号通路，表明其在心血管疾病中的治疗潜力。
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**备注**：以上文献为示例，实际研究中FSTL5相关论文较少，建议通过PubMed或Google Scholar以“FSTL5 recombinant protein”为关键词检索最新进展。部分研究可能聚焦于FSTL家族其他成员(如FSTL1、FSTL3)。
**Background of FSTL5 Recombinant Protein**
Follistatin-like 5 (FSTL5) is a secreted glycoprotein belonging to the follistatin-related protein family, which is characterized by conserved follistatin-like (FS) domains. Initially identified through genomic analyses, FSTL5 shares structural homology with other follistatin members but exhibits distinct expression patterns and functional roles. It is encoded by the *FSTL5* gene and is primarily expressed in tissues such as the heart, skeletal muscle, and certain immune cells. While its exact physiological function remains under investigation, FSTL5 is hypothesized to modulate cellular signaling pathways, particularly those involving TGF-β (transforming growth factor-beta) superfamily members, which regulate processes like cell differentiation, inflammation, and tissue repair.
Recombinant FSTL5 protein is engineered using biotechnological methods, often expressed in mammalian or bacterial systems to ensure proper folding and post-translational modifications. This engineered protein enables researchers to study FSTL5's interactions, receptor binding, and downstream signaling mechanisms in vitro or in vivo. Emerging studies suggest its potential involvement in cardiovascular diseases, fibrosis, and cancer progression, though mechanistic details are still emerging. For instance, FSTL5 may influence extracellular matrix remodeling or immune responses, making it a candidate biomarker or therapeutic target.
Current research focuses on elucidating FSTL5's role in disease models and its crosstalk with other signaling molecules. The availability of recombinant FSTL5 facilitates structural studies, antibody development, and high-throughput screening for drug discovery. Despite its promise, challenges remain in fully defining its biological context and clinical relevance, necessitating further interdisciplinary investigations.
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