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Recombinant Human TMPRSS11A protein

  • 中文名: 跨膜丝氨酸蛋白酶11A(TMPRSS11A)重组蛋白
  • 别    名: TMPRSS11A;ECRG1;HATL1;HESP;Transmembrane protease serine 11A
货号: PA2000-4099
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点TMPRSS11A
Uniprot No Q6ZMR5
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间 40-421aa
氨基酸序列HFLVFDQKKEYYHGSFKILDPQINNNFGQSNTYQLKDLRETTENLVSQVDEIFIDSAWKKNYIKNQVVRLTPEEDGVKVDVIMVFQFPSTEQRAVREKKIQSILNQKIRNLRALPINASSVQVNAMSSSTGELTVQASCGKRVVPLNVNRIASGVIAPKAAWPWQASLQYDNIHQCGATLISNTWLVTAAHCFQKYKNPHQWTVSFGTKINPPLMKRNVRRFIIHEKYRSAAREYDIAVVQVSSRVTFSDDIRRICLPEASASFQPNLTVHITGFGALYYGGESQNDLREARVKIISDDVCKQPQVYGNDIKPGMFCAGYMEGIYDACRGDSGGPLVTRDLKDTWYLIGIVSWGDNCGQKDKPGVYTQVTYYRNWIASKTGI
预测分子量 44.3 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.

参考文献

以下是关于TMPRSS11A重组蛋白的假设性参考文献示例,内容基于典型研究方向的合理推测:

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1. **文献名称**:*Expression and Enzymatic Characterization of Recombinant Human TMPRSS11A in Mammalian Cells*

**作者**:Li, X., Zhang, Y., & Wang, H.

**摘要**:本研究在HEK293细胞中成功表达了重组TMPRSS11A蛋白,并通过亲和层析技术纯化。酶活性分析表明,该重组蛋白具有丝氨酸蛋白酶活性,可特异性切割合成底物Boc-QAR-AMC。研究还发现其活性受肝素类抑制剂显著抑制,提示其在细胞外基质重塑中的潜在作用。

2. **文献名称**:*TMPRSS11A Facilitates Influenza A Virus Entry by Cleaving Hemagglutinin*

**作者**:Smith, J.R., Tanaka, K., & Gonzalez, M.E.

**摘要**:通过体外实验验证了重组TMPRSS11A对流感病毒HA蛋白的切割作用。结果显示,TMPRSS11A的蛋白酶活性增强了病毒与宿主细胞膜的融合效率。抑制实验进一步证明,其活性缺失会显著降低病毒感染性,提示其作为抗病毒治疗靶点的可能性。

3. **文献名称**:*Structural Insights into TMPRSS11A via Cryo-EM and Its Implications for Substrate Recognition*

**作者**:Chen, L., Wu, F., & Patel, R.

**摘要**:利用冷冻电镜技术解析了重组TMPRSS11A的三维结构(分辨率为3.1Å),揭示了其底物结合口袋的关键氨基酸残基。分子对接模拟表明,该区域对病毒刺突蛋白的识别至关重要,为设计特异性抑制剂提供了结构基础。

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**注意**:以上文献为假设性示例,实际研究中需通过学术数据库(如PubMed、Web of Science)检索真实文献。若需具体文章,建议使用关键词“TMPRSS11A recombinant protein”或“TMPRSS11A expression and function”进一步查询。

背景信息

**Background of TMPRSS11A Recombinant Protein**

TMPRSS11A (Transmembrane Serine Protease 11A) is a member of the type II transmembrane serine protease (TTSP) family, characterized by a conserved trypsin-like catalytic domain. Primarily expressed in epithelial tissues, including the respiratory tract, it plays roles in extracellular matrix remodeling, cellular signaling, and host-pathogen interactions. Its structural features include an N-terminal transmembrane anchor, a stem region with diverse domains, and a C-terminal catalytic domain.

Recombinant TMPRSS11A protein is engineered in vitro using expression systems (e.g., mammalian, insect, or bacterial cells) to produce soluble, functional forms of the protease for research. This involves cloning the catalytic domain or full-length cDNA into vectors, followed by purification via affinity chromatography. The recombinant protein retains enzymatic activity, enabling studies on substrate specificity, inhibition, and regulatory mechanisms.

TMPRSS11A has gained attention due to its potential involvement in viral entry mechanisms, particularly for influenza and coronaviruses, where proteolytic activation of viral surface proteins is critical. It may also contribute to cancer progression by modulating growth factor signaling or tumor microenvironment interactions. Research using recombinant TMPRSS11A aids in elucidating its physiological roles, developing diagnostic tools, and screening therapeutic inhibitors. However, its precise biological functions and disease relevance remain under investigation, necessitating further structural and functional studies.

Overall, TMPRSS11A recombinant protein serves as a vital tool for dissecting protease-driven pathways in health and disease, with implications for antiviral and anticancer drug development.

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