GSDMD Antibody, HRP conjugated

Code CSB-PA009956LB01HU
Size US$166
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Product Details

Full Product Name
Rabbit anti-Homo sapiens (Human) GSDMD Polyclonal antibody
Uniprot No.
Target Names
GSDMD
Alternative Names
C-terminal antibody; Gasdermin domain-containing protein 1 antibody; Gasdermin-D antibody; GSDMD antibody; GSDMD-CT antibody; GSDMD-NT antibody; GSDMD_HUMAN antibody
Raised in
Rabbit
Species Reactivity
Human
Immunogen
Recombinant Human Gasdermin-D protein (1-256AA)
Immunogen Species
Homo sapiens (Human)
Conjugate
HRP
Clonality
Polyclonal
Isotype
IgG
Purification Method
>95%, Protein G purified
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, PH 7.4
Form
Liquid
Tested Applications
ELISA
Protocols
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
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.

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Target Background

Function
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.
Gene References into Functions
  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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Subcellular Location
[Gasdermin-D]: Cytoplasm, cytosol. Inflammasome.; [Gasdermin-D, N-terminal]: Cell membrane; Multi-pass membrane protein. Secreted.; [Gasdermin-D, C-terminal]: Cytoplasm, cytosol.
Protein Families
Gasdermin family
Tissue Specificity
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.
Database Links

HGNC: 25697

OMIM: 617042

KEGG: hsa:79792

STRING: 9606.ENSP00000262580

UniGene: Hs.118983

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