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Mouse Anti-GSDMB Recombinant Antibody (CBLG1-1827) (CBMAB-G5134-LY)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
CBLG1-1827
Antibody Isotype
IgG2b
Application
WB

Basic Information

Specificity
Human
Antibody Isotype
IgG2b
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!]

Format
Liquid
Concentration
1 mg/mL
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Gasdermin B
Introduction
This gene encodes a member of the gasdermin-domain containing protein family. Other gasdermin-family genes are implicated in the regulation of apoptosis in epithelial cells, and are linked to cancer. Alternative splicing and the use of alternative promoters results in multiple transcript variants. Additional variants have been described, but they are candidates for nonsense-mediated mRNA decay (NMD) and are unlikely to be protein-coding. [provided by RefSeq, Nov 2016]
Entrez Gene ID
55876
UniProt ID
Q8TAX9
Alternative Names
Gasdermin B; Gasdermin-Like Protein; GSDML; Gasdermin-Like; Gasdermin-B; PRO2521; PP4052;
Function
Gasdermin-B:
Precursor of a pore-forming protein that acts as a downstream mediator of granzyme-mediated cell death (PubMed:32299851).

This form constitutes the precursor of the pore-forming protein: upon cleavage, the released N-terminal moiety (Gasdermin-B, N-terminal) binds to membranes and forms pores, triggering pyroptosis (PubMed:32299851).

Gasdermin-B, N-terminal:
Pore-forming protein produced by cleavage by granzyme A (GZMA), which causes membrane permeabilization and pyroptosis in target cells of cytotoxic T and natural killer (NK) cells (PubMed:27281216, PubMed:32299851).

Key downstream mediator of granzyme-mediated cell death: (1) granzyme A (GZMA), delivered to target cells from cytotoxic T- and NK-cells, (2) specifically cleaves Gasdermin-B to generate this form (PubMed:32299851).

After cleavage, moves to the plasma membrane, homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, triggering pyroptosis (PubMed:32299851).

Binds to membrane inner leaflet lipids, such as phosphatidylinositol 4-phosphate, phosphatidylinositol 5-phosphate, bisphosphorylated phosphatidylinositols, such as phosphatidylinositol (4,5)-bisphosphate, and more weakly to phosphatidic acid (PubMed:28154144).

Also binds sufatide, a component of the apical membrane of epithelial cells (PubMed:28154144).
Biological Process
Cytolysis Source: UniProtKB-KW
Cytotoxic T cell pyroptotic process Source: UniProtKB
Defense response to bacterium Source: GO_Central
Granzyme-mediated programmed cell death signaling pathway Source: UniProtKB
Pyroptosis Source: UniProtKB
Cellular Location
Gasdermin-B: Cytoplasm. Vesicular localization in the apical region of gastric chief cells and colonic surface mucous cells, and the basal region of neuroendocrine cells.
Gasdermin-B, N-terminal: Cell membrane
PTM
Cleavage by granzyme A (GZMA) relieves autoinhibition by releasing the N-terminal moiety (Gasdermin-B, N-terminal) that initiates pyroptosis (PubMed:32299851). Not cleaved by other granzymes (PubMed:32299851). Major cleavage site takes places after Lys-239; a minor cleavage site takes place after Lys-233 (PubMed:32299851).
More Infomation

Zhong, X., Zeng, H., Zhou, Z., Su, Y., Cheng, H., Hou, Y., ... & Ding, J. (2023). Structural mechanisms for regulation of GSDMB pore-forming activity. Nature, 616(7957), 598-605.

Wang, C., Shivcharan, S., Tian, T., Wright, S., Ma, D., Chang, J., ... & Ruan, J. (2023). Structural basis for GSDMB pore formation and its targeting by IpaH7. 8. Nature, 616(7957), 590-597.

Oltra, S. S., Colomo, S., Sin, L., Pérez-López, M., Lázaro, S., Molina-Crespo, A., ... & Moreno-Bueno, G. (2023). Distinct GSDMB protein isoforms and protease cleavage processes differentially control pyroptotic cell death and mitochondrial damage in cancer cells. Cell Death & Differentiation, 30(5), 1366-1381.

Rana, N., Privitera, G., Kondolf, H. C., Bulek, K., Lechuga, S., De Salvo, C., ... & Pizarro, T. T. (2022). GSDMB is increased in IBD and regulates epithelial restitution/repair independent of pyroptosis. Cell, 185(2), 283-298.

Hansen, J. M., de Jong, M. F., Wu, Q., Zhang, L. S., Heisler, D. B., Alto, L. T., & Alto, N. M. (2021). Pathogenic ubiquitination of GSDMB inhibits NK cell bactericidal functions. Cell, 184(12), 3178-3191.

Li, X., Christenson, S. A., Modena, B., Li, H., Busse, W. W., Castro, M., ... & Meyers, D. A. (2021). Genetic analyses identify GSDMB associated with asthma severity, exacerbations, and antiviral pathways. Journal of Allergy and Clinical Immunology, 147(3), 894-909.

He, H., Yi, L., Zhang, B., Yan, B., Xiao, M., Ren, J., ... & Xiong, W. (2021). USP24-GSDMB complex promotes bladder cancer proliferation via activation of the STAT3 pathway. International Journal of Biological Sciences, 17(10), 2417.

Li, L., Li, Y., & Bai, Y. (2020). Role of GSDMB in Pyroptosis and Cancer. Cancer management and research, 12, 3033.

Zhou, Z., He, H., Wang, K., Shi, X., Wang, Y., Su, Y., ... & Shao, F. (2020). Granzyme A from cytotoxic lymphocytes cleaves GSDMB to trigger pyroptosis in target cells. Science, 368(6494), eaaz7548.

Chen, Q., Shi, P., Wang, Y., Zou, D., Wu, X., Wang, D., ... & Gao, X. (2019). GSDMB promotes non-canonical pyroptosis by enhancing caspase-4 activity. Journal of molecular cell biology, 11(6), 496-508.

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

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