Gasdermin D Proteins (GSDMD)

Gasdermin D is a member of the gasdermin family. Additionally we are shipping Gasdermin D Antibodies (28) and Gasdermin D Kits (6) and many more products for this protein.

list all proteins Gene Name GeneID UniProt
GSDMD 79792 P57764
GSDMD 69146 Q9D8T2
GSDMD 315084  
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Top Gasdermin D Proteins at antibodies-online.com

Showing 6 out of 6 products:

Catalog No. Origin Source Conjugate Images Quantity Delivery Price Details
Insect Cells Human His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg 60 Days
$9,626.73
Details
Insect Cells Mouse His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg 60 Days
$9,626.73
Details
Wheat germ Human GST tag 10 μg 11 to 12 Days
$414.29
Details
Escherichia coli (E. coli) Human His tag   50 μg 15 to 18 Days
$320.00
Details
Escherichia coli (E. coli) Mouse His tag   50 μg 15 to 18 Days
$350.00
Details
Escherichia coli (E. coli) Rat His tag   50 μg 15 to 18 Days
$360.00
Details

GSDMD Proteins by Origin and Source

Origin Expressed in Conjugate
Human , ,
,
Mouse (Murine) ,

Rat (Rattus)

More Proteins for Gasdermin D (GSDMD) Interaction Partners

Human Gasdermin D (GSDMD) interaction partners

  1. our current work demonstrates that IL-1beta release from stimulated THP1 cells is regulated by GSDM-D, and P2X7 is a dual-step process

  2. Our findings provide the first demonstration of GSDMD-determined pyroptotic cell death responsible for I/R induced release of IL-1beta and this would provide a mandate to better understand the unconventional mechanisms of cytokine release in the sterile innate immune system.

  3. role of GSDMD in the stretch-induced inflammatory response in human periodontal ligament cells

  4. Gasdermin D plays a key role in the pathogenesis of non-alcoholic steatohepatitis (NASH) by regulating lipogenesis, the inflammatory response, and the NF-kB signaling pathway, revealing potential treatment targets for NASH in humans.

  5. findings suggest that NLRP3 is central to the activation/release of active caspase-1/GSDM-D encapsulated in microparticles (MP) by Francisella.

  6. GSDMD is proteolytically activated by neutrophil proteases and, in turn, affects protease activation and nuclear expansion in a feed-forward loop. In addition to the central role of GSDMD in pyroptosis, we propose that GSDMD also plays an essential function in NETosis.

  7. GSDMD regulates the release of microparticulate active caspase 1 from monocytes essential for induction of cell death and thereby may play a critical role in sepsis-induced endothelial cell injury.

  8. Once inserted, the N-terminal domain of GSDMD assembles arc-, slit-, and ring-shaped oligomers, each of which being able to form transmembrane pores. This assembly and pore formation process is independent on whether GSDMD has been cleaved by caspase-1, caspase-4, or caspase-5.

  9. Study reports the crystal structure of GSDMD C-terminal domain. Two interaction sites mediate the association of C and N domains. Mutations of GSDMD C-domain residues predicted to locate at its interface with the N-domain enhanced pyroptosis. Results suggest that GSDMDs may employ a distinct mode of intramolecular domain interaction and autoinhibition, which may be relevant to its unique role in pyroptosis.

  10. 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

  11. High GSDMD expression is associated with tumor-node-metastasis in nonsmall cell lung cancer.

  12. the gasdermin-D pore: Executor of pyroptotic cell death

  13. Results implicate pyroptosis induced by the CASP11/4-GSDMD pathway in the pathogenesis of alcoholic hepatitis

  14. 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.

  15. 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

  16. 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.

  17. 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.

  18. GsdmD p30 kills cells by forming pores that compromise the integrity of the cell membrane.

  19. 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.

  20. Remarkably, the Enterovirus 71 protease 3C directly targets GSDMD and induces its cleavage, which is dependent on the protease activity.

Mouse (Murine) Gasdermin D (GSDMD) interaction partners

  1. study highlights a function for GSDMD in promoting caspase-1 activation by AIM2 inflammasome

  2. Gasdermin D plays a key role in the pathogenesis of non-alcoholic fatty liver disease (NAFLD) by regulating lipogenesis, the inflammatory response, and the NF-kB signaling pathway, revealing potential treatment targets for NASH in humans.

  3. Clostridium difficile infection of FMF knock-in macrophages that express a chimeric Familial Mediterranean Fever-associated Mefv(V726A) Pyrin elicited pyroptosis and gasdermin D (GSDMD)-mediated interleukin (IL)-1beta secretion.

  4. This study clarifies the molecular mechanism and biological roles of caspase-1-induced apoptosis in GSDMD-low/null cell types.

  5. Our studies reveal that neutrophils use an inflammasome- and GSDMD-dependent mechanism to activate NETosis as a defense response against cytosolic bacteria.

  6. GSDMD is proteolytically activated by neutrophil proteases and, in turn, affects protease activation and nuclear expansion in a feed-forward loop. In addition to the central role of GSDMD in pyroptosis, we propose that GSDMD also plays an essential function in NETosis.

  7. these findings have uncovered an additional interferon regulatory module involving gasdermin D and K(+) efflux.

  8. this study establishes the importance of TAK1 and IKK activity in the control of GSDMD cleavage and cytotoxicity.

  9. caspase-1 protease activity is required for canonical IL-1 secretion, pyroptosis, and inflammasome-mediated immunity.

  10. Study reports the crystal structure of GSDMD C-terminal domain. Two interaction sites mediate the association of C and N domains. Mutations of GSDMD C-domain residues predicted to locate at its interface with the N-domain enhanced pyroptosis. Results suggest that GSDMDs may employ a distinct mode of intramolecular domain interaction and autoinhibition, which may be relevant to its unique role in pyroptosis.

  11. Genetic inactivation of GPX4 increases lipid peroxidation, thus exacerbating GSDMD-mediated pyroptosis in macrophages as well as septic lethality in mice.

  12. Because DFNA5-induced secondary necrosis and GSDMD-induced pyroptosis are dependent on CASP3 activation, we propose that they are forms of programmed necrosis.

  13. the gasdermin-D pore: Executor of pyroptotic cell death

  14. Results implicate pyroptosis induced by the CASP11/4-GSDMD pathway in the pathogenesis of alcoholic hepatitis

  15. 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.

  16. 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.

  17. 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.

  18. identification of gasdermin D (Gsdmd) by genome-wide clustered regularly interspaced palindromic repeat (CRISPR)-Cas9 nuclease screens of caspase-11- and caspase-1-mediated pyroptosis in mouse bone marrow macrophages

  19. gasdermin D is essential for caspase-11-dependent pyroptosis and interleukin-1beta maturation

  20. This study clearly shows that Gsdmd is not essential for development of mouse intestinal tract or epithelial cell differentiation.

Gasdermin D (GSDMD) Protein Profile

Protein Summary

Gasdermin D is a member of the gasdermin family. Members of this family appear to play a role in regulation of epithelial proliferation. Gasdermin D has been suggested to act as a tumor suppressor. Alternatively spliced transcript variants have been described.

Gene names and symbols associated with Gasdermin D Proteins (GSDMD)

  • gasdermin D (GSDMD)
  • gasdermin D (Gsdmd)
  • 1810036L03Rik protein
  • AW558049 protein
  • DF5L protein
  • Dfna5l protein
  • GSDMD protein
  • Gsdmdc1 protein
  • M2-4 protein

Protein level used designations for Gasdermin D Proteins (GSDMD)

gasdermin domain containing 1 , gasdermin-D , gasdermin D , gasdermin domain-containing protein 1

GENE ID SPECIES
513939 Bos taurus
609395 Canis lupus familiaris
697137 Macaca mulatta
739712 Pan troglodytes
100604427 Nomascus leucogenys
79792 Homo sapiens
69146 Mus musculus
315084 Rattus norvegicus
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