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Mouse Anti-GSDMD Recombinant Antibody (3F12-1B2) (CBMAB-D2080-YC)

Provided herein is a Mouse monoclonal antibody, which binds to Gasdermin D (GSDMD). The antibody can be used for immunoassay techniques, such as WB, ELISA, IHC-P, ICC, IF.
See all GSDMD antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
3F12-1B2
Antibody Isotype
IgG1
Application
WB, ELISA, IHC-P, ICC, IF

Basic Information

Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Gasdermin D
Introduction
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.
Entrez Gene ID
UniProt ID
Alternative Names
Gasdermin D; Gasdermin Domain-Containing Protein 1; Gasdermin Domain Containing 1; GSDMDC1; DFNA5L; Gasdermin-D; FKSG10; DF5L;
Function
Gasdermin-D:
Precursor of a pore-forming protein that plays a key role in host defense against pathogen infection and danger signals (PubMed:26375003, PubMed:26375259, PubMed:27281216).

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 (PubMed:26375003, PubMed:26375259, PubMed:27281216).

Gasdermin-D, N-terminal:
Promotes pyroptosis in response to microbial infection and danger signals (PubMed:26375003, PubMed:26375259, PubMed:27418190, PubMed:28392147, PubMed:32820063).

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 (PubMed:26375003, PubMed:26375259, PubMed:27418190).

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 (PubMed:27281216, PubMed:29898893).

Homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, allowing the release of mature IL1B and triggering pyroptosis (PubMed:27418190, PubMed:27281216, PubMed:29898893).

Exhibits bactericidal activity (PubMed:27281216).

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 (PubMed:27281216).

Under cell culture conditions, also active against intracellular bacteria, such as Listeria monocytogenes (By similarity).

Also active in response to MAP3K7/TAK1 inactivation by Yersinia toxin YopJ, which triggers cleavage by CASP8 and subsequent activation (By similarity).

Strongly binds to bacterial and mitochondrial lipids, including cardiolipin (PubMed:27281216).

Does not bind to unphosphorylated phosphatidylinositol, phosphatidylethanolamine nor phosphatidylcholine (PubMed:27281216).
Biological Process
Defense response to bacterium Source: GO_Central
Defense response to Gram-negative bacterium Source: UniProtKB
Defense response to Gram-positive bacterium Source: UniProtKB
Inflammatory response Source: UniProtKB-KW
Innate immune response Source: UniProtKB-KW
Neutrophil degranulation Source: Reactome
Pore complex assembly Source: UniProtKB
Pore formation in membrane of other organism Source: UniProtKB
Positive regulation of interleukin-1 beta production Source: UniProtKB
Protein homooligomerization Source: UniProtKB
Pyroptosis Source: UniProtKB
Cellular Location
Gasdermin-D: Cytosol; Inflammasome. In response to a canonical inflammasome stimulus, such as nigericin, recruited to NLRP3 inflammasone with similar kinetics to that of uncleaved CASP1 precursor.
Gasdermin-D, N-terminal: Secreted; Cell membrane. Released in the extracellular milieu following pyroptosis.
Gasdermin-D, C-terminal: Cytosol
PTM
Cleavage at Asp-275 by CASP1 (mature and uncleaved precursor forms), CASP4, CASP5 or CASP8 relieves autoinhibition and is sufficient to initiate pyroptosis (PubMed:26375003, PubMed:29898893, PubMed:32109412). Cleavage by CASP1 and CASP4 is not strictly dependent on the consensus cleavage site on GSDMD but depends on an exosite interface on CASP1 that recognizes and binds the Gasdermin-D, C-terminal (GSDMD-CT) part (PubMed:32109412). Cleavage by CASP8 takes place following inactivation of MAP3K7/TAK1 by Yersinia toxin YopJ (By similarity). Cleavage at Asp-87 by CASP3 or CAPS7 inactivates the ability to mediate pyroptosis (PubMed:28392147, PubMed:28045099).
Gasdermin-D:
Succination of Cys-191 by the Krebs cycle intermediate fumarate, which leads to S-(2-succinyl)cysteine residues, inhibits processing by caspases, and ability to initiate pyroptosis (PubMed:32820063). Succination modification is catalyzed by a non-enzymatic reaction caused by an accumulation of fumarate (PubMed:32820063).

Xie, W. J., Xia, S., Warshel, A., & Wu, H. (2022). Electrostatic influence on IL-1 transport through the GSDMD pore. Proceedings of the National Academy of Sciences, 119(6), e2120287119.

Liu, Y., Xue, N., Zhang, B., Lv, H., & Li, S. (2022). Cold Stress Induced Liver Injury of Mice through Activated NLRP3/Caspase-1/GSDMD Pyroptosis Signaling Pathway. Biomolecules, 12(7), 927.

Jiang, S., Zhang, H., Li, X., Yi, B., Huang, L., Hu, Z., ... & Zhang, W. (2021). Vitamin D/VDR attenuate cisplatin-induced AKI by down-regulating NLRP3/Caspase-1/GSDMD pyroptosis pathway. The Journal of Steroid Biochemistry and Molecular Biology, 206, 105789.

Zhang, J., Dai, Y., Yang, Y., & Xu, J. (2021). Calcitriol alleviates hyperosmotic stress-induced corneal epithelial cell damage via inhibiting the NLRP3–ASC–caspase-1–GSDMD pyroptosis pathway in dry eye disease. Journal of Inflammation Research, 14, 2955.

Yan, H., Luo, B., Wu, X., Guan, F., Yu, X., Zhao, L., ... & Yuan, J. (2021). Cisplatin induces pyroptosis via activation of MEG3/NLRP3/caspase-1/GSDMD pathway in triple-negative breast cancer. International Journal of Biological Sciences, 17(10), 2606.

Li, W., Deng, M., Loughran, P. A., Yang, M., Lin, M., Yang, C., ... & Scott, M. J. (2020). LPS induces active HMGB1 release from hepatocytes into exosomes through the coordinated activities of TLR4 and caspase-11/GSDMD signaling. Frontiers in Immunology, 11, 229.

Yang, Y., Liu, P. Y., Bao, W., Chen, S. J., Wu, F. S., & Zhu, P. Y. (2020). Hydrogen inhibits endometrial cancer growth via a ROS/NLRP3/caspase-1/GSDMD-mediated pyroptotic pathway. BMC cancer, 20, 1-19.

Schwarzer, R., Jiao, H., Wachsmuth, L., Tresch, A., & Pasparakis, M. (2020). FADD and caspase-8 regulate gut homeostasis and inflammation by controlling MLKL-and GSDMD-mediated death of intestinal epithelial cells. Immunity, 52(6), 978-993.

Karmakar, M., Minns, M., Greenberg, E. N., Diaz-Aponte, J., Pestonjamasp, K., Johnson, J. L., ... & Pearlman, E. (2020). N-GSDMD trafficking to neutrophil organelles facilitates IL-1β release independently of plasma membrane pores and pyroptosis. Nature communications, 11(1), 2212.

Pandeya, A., Li, L., Li, Z., & Wei, Y. (2019). Gasdermin D (GSDMD) as a new target for the treatment of infection. Medchemcomm, 10(5), 660-667.

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For research use only. Not intended for any clinical use.

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