Gasdermin E (E2X7E) Rabbit mAb #19453
- WB
- IF
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 55, 30 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IF-Immunofluorescence
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunofluorescence (Immunocytochemistry) | 1:800 - 1:1600 |
Storage
Protocol
Specificity / Sensitivity
Gasdermin E (E2X7E) Rabbit mAb recognizes endogenous levels of total Gasdermin E protein. This antibody can also detect the amino-terminal cleavage fragment of Gasdermin E associated with pyroptosis.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with recombinant protein specific to the amino terminus of human protein.
Background
The gasdermin family, which includes GSDMA, GSDMB, GSDMC, GSDMD, and GSDME, has been shown to play a role in inflammation and cell death. Gasdermin D has been reported to have a critical role as a downstream effector of pyroptosis (1,2). Pyroptosis is a lytic type of cell death triggered by inflammasomes, multiprotein complexes assembled in response to pathogen-associated molecular patterns (PAMPs) or danger-associated molecular patterns (DAMPs) that result in the activation of caspase-1 and subsequent cleavage of pro-inflammatory cytokines IL-1β and IL-18 (3). Gasdermin D was identified by two independent groups as a substrate of inflammatory caspases, caspase-1 and caspase-11/4/5, producing two fragments: GSDMD-N and GSDMD-C. Cleavage results in release of an intramolecular inhibitory interaction between the N- and C-terminal domains, allowing the N-terminal fragment GSDMD-N to initiate pyroptosis through the formation of pores on the plasma membrane (4-7).
Gasdermin E (GSDME), also known as DFNA5, was originally identified as a genetic cause of nonsyndromic hearing loss (8). Like other gasdermin family members, Gasdermin E contains an amino-terminal pore forming domain that triggers pyroptosis. Cleavage of Gasdermin E at Asp270 is induced by apoptotic-associated caspase-3, converting apoptotic signals to pyroptosis (9). In addition, cleavage of Gasdermin E can be induced by Granzyme B secreted by NK cells and contributes to tumor suppressive activity (10). Gasdermin E expression is suppressed in several types of cancer including gastric, colorectal, and breast carcinoma, and may be associated with decreased survival (11-13). In contrast, an increase in Gasdermin E, including the amino-terminal pore-forming fragment, is associated with conditions of excessive inflammation (14-16).
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- Shi, J. et al. (2015) Nature 526, 660-5.
- Broz, P. and Dixit, V.M. (2016) Nat Rev Immunol 16, 407-20.
- Aglietti, R.A. et al. (2016) Proc Natl Acad Sci USA 113, 7858-63.
- Ding, J. et al. (2016) Nature 535, 111-6.
- Liu, X. et al. (2016) Nature 535, 153-8.
- Sborgi, L. et al. (2016) EMBO J 35, 1766-78.
- Van Laer, L. et al. (1998) Nat Genet 20, 194-7.
- Rogers, C. et al. (2017) Nat Commun 8, 14128.
- Zhang, Z. et al. (2020) Nature 579, 415-420.
- Kim, M.S. et al. (2008) Oncogene 27, 3624-34.
- Kim, M.S. et al. (2008) Biochem Biophys Res Commun 370, 38-43.
- Yokomizo, K. et al. (2012) Anticancer Res 32, 1319-22.
- Tan, G. et al. (2021) Cell Rep 35, 109265.
- Li, Y. et al. (2021) Cell Death Differ 28, 2333-2350.
- Shi, H. et al. (2021) Circ Res 129, 383-396.
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