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  4. GSDMD Antibody, FITC conjugated

GSDMD Antibody, FITC conjugated

  • 中文名稱：
    GSDMD兔多克隆抗體, FITC偶聯
  • 貨號：
    CSB-PA009956LC01HU
  • 規格：
    ￥880
  • 其他：

產品詳情

  • 產品名稱：
    Rabbit anti-Homo sapiens (Human) GSDMD Polyclonal antibody
  • Uniprot No.：
  • 基因名：
  • 別名：
    C-terminal antibody; Gasdermin domain-containing protein 1 antibody; Gasdermin-D antibody; GSDMD antibody; GSDMD-CT antibody; GSDMD-NT antibody; GSDMD_HUMAN antibody
  • 宿主：
    Rabbit
  • 反應種屬：
    Human
  • 免疫原：
    Recombinant Human Gasdermin-D protein (1-256AA)
  • 免疫原種屬：
    Homo sapiens (Human)
  • 標記方式：
    FITC
  • 克隆類型：
    Polyclonal
  • 抗體亞型：
    IgG
  • 純化方式：
    >95%, Protein G purified
  • 濃度：
    It differs from different batches. Please contact us to confirm it.
  • 保存緩沖液：
    Preservative: 0.03% Proclin 300
    Constituents: 50% Glycerol, 0.01M PBS, PH 7.4
  • 產品提供形式：
    Liquid
  • 儲存條件：
    Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
  • 貨期：
    Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
  • 用途：
    For Research Use Only. Not for use in diagnostic or therapeutic procedures.

產品評價

靶點詳情

  • 功能：
    Precursor of a pore-forming protein that plays a key role in host defense against pathogen infection and danger signals. This form constitutes the precursor of the pore-forming protein: upon cleavage, the released N-terminal moiety (Gasdermin-D, N-terminal) binds to membranes and forms pores, triggering pyroptosis.; Promotes pyroptosis in response to microbial infection and danger signals. Produced by the cleavage of gasdermin-D by inflammatory caspases CASP1, CASP4 or CASP5 in response to canonical, as well as non-canonical (such as cytosolic LPS) inflammasome activators. After cleavage, moves to the plasma membrane where it strongly binds to inner leaflet lipids, including monophosphorylated phosphatidylinositols, such as phosphatidylinositol 4-phosphate, bisphosphorylated phosphatidylinositols, such as phosphatidylinositol (4,5)-bisphosphate, as well as phosphatidylinositol (3,4,5)-bisphosphate, and more weakly to phosphatidic acid and phosphatidylserine. Homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, allowing the release of mature IL1B and triggering pyroptosis. Exhibits bactericidal activity. Gasdermin-D, N-terminal released from pyroptotic cells into the extracellular milieu rapidly binds to and kills both Gram-negative and Gram-positive bacteria, without harming neighboring mammalian cells, as it does not disrupt the plasma membrane from the outside due to lipid-binding specificity. Under cell culture conditions, also active against intracellular bacteria, such as Listeria monocytogenes. Also active in response to MAP3K7/TAK1 inactivation by Yersinia toxin YopJ, which triggers cleavage by CASP8 and subsequent activation. Strongly binds to bacterial and mitochondrial lipids, including cardiolipin. Does not bind to unphosphorylated phosphatidylinositol, phosphatidylethanolamine nor phosphatidylcholine.
  • 基因功能參考文獻：
    1. lncRNA RP185F18.6 and DeltaNp63 may be considered unfavorable biomarkers, whereas GSDMD may be a favorable biomarker in colorectal cancer (CRC) ; these markers may prove valuable in the future diagnosis and prognosis of CRC PMID: 30226619
    2. High GSDMD expression is associated with tumor-node-metastasis in nonsmall cell lung cancer. PMID: 30106450
    3. the gasdermin-D pore: Executor of pyroptotic cell death PMID: 27557502
    4. Results implicate pyroptosis induced by the CASP11/4-GSDMD pathway in the pathogenesis of alcoholic hepatitis PMID: 29108122
    5. The present study not only contributes to our understanding of GSDMD recognition by inflammatory caspases but also reports a specific inhibitor for these caspases that can serve as a tool for investigating inflammasome signaling. PMID: 29891674
    6. Pyroptosis regulator gasdermin D was necessary for IL-1beta secretion from living macrophages that have been exposed to inflammasome activators, such as bacteria and their products or host-derived oxidized lipids PMID: 29195811
    7. These findings reveal that GSDMD-C acts as an auto-inhibition executor and GSDMD-N could form pore structures via a charge-charge interaction upon cleavage by caspases during cell pyroptosis. PMID: 28928145
    8. This study reveals the pore-forming activity of GSDMD and channel-forming activity of MLKL determine different ways of plasma membrane rupture in pyroptosis and necroptosis. PMID: 27573174
    9. GsdmD p30 kills cells by forming pores that compromise the integrity of the cell membrane. PMID: 27339137
    10. Data, including data from studies using recombinant fusion forms of GSDMD, suggest that GSDMD participates in inflammasome-dependent pyroptosis of macrophages in response to various stimuli; this mechanism involves proteolysis of GSDMD by caspase-1 and caspase-11. PMID: 28726636
    11. Remarkably, the Enterovirus 71 protease 3C directly targets GSDMD and induces its cleavage, which is dependent on the protease activity. PMID: 28679757
    12. The pyroptosis is redefined as gasdermin D-mediated programmed necrosis. Gasdermin D are associated with various genetic diseases, and their cellular function and mechanism of activation. PMID: 27932073
    13. Overall, these data demonstrate that GSDMD is the direct and final executor of pyroptotic cell death. PMID: 27418190
    14. Studies show that the membrane-pores composed of gasdermin D-N domains (GSDMD-N domain) are required for pyroptosis. PMID: 27460194
    15. Studies indicate that gasdermin D (GSDMD) is cleaved by the activated caspases-1/4/5/11 between its N-terminal and C-terminal domains. PMID: 27604419
    16. Gene deletion of GSDMD demonstrated that GSDMD is required for pyroptosis and for the secretion but not proteolytic maturation of IL-1beta in both canonical and non-canonical inflammasome responses. PMID: 26611636
    17. GSDMD N-terminal cleavage product oligomerizes in membranes to form pores that are visible by electron microscopy PMID: 27383986
    18. caspase-1 and caspase-4/5/11 specifically cleaved the linker between the amino-terminal gasdermin-N and carboxy-terminal gasdermin-C domains in GSDMD, which was required and sufficient for pyroptosis PMID: 26375003

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  • 亞細胞定位：
    [Gasdermin-D]: Cytoplasm, cytosol. Inflammasome.; [Gasdermin-D, N-terminal]: Cell membrane; Multi-pass membrane protein. Secreted.; [Gasdermin-D, C-terminal]: Cytoplasm, cytosol.
  • 蛋白家族：
    Gasdermin family
  • 組織特異性：
    Expressed in the suprabasal cells of esophagus, as well as in the isthmus/neck, pit, and gland of the stomach, suggesting preferential expression in differentiating cells.
  • 數據庫鏈接：

    HGNC: 25697

    OMIM: 617042

    KEGG: hsa:79792

    STRING: 9606.ENSP00000262580

    UniGene: Hs.118983



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