Revision 1

#26776Store at -20C

1 Kit

(6 x 20 microliters)

Cell Signaling Technology

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For Research Use Only. Not for Use in Diagnostic Procedures.
Product Includes Product # Quantity Mol. Wt Isotype/Source
Gasdermin D (E5O4N) Rabbit mAb 69469 20 µl 53, 30 kDa Rabbit IgG
Cleaved Gasdermin D (Asp275) (E7H9G) Rabbit mAb 36425 20 µl 30 kDa Rabbit IgG
Gasdermin E (E2X7E) Rabbit mAb 19453 20 µl 55, 30 kDa Rabbit IgG
Cleaved Gasdermin E (Asp270) (E8G4U) Rabbit mAb 55879 20 µl 30 kDa Rabbit IgG
Gasdermin A Antibody 49307 20 µl 49 kDa Rabbit 
Gasdermin B Antibody 76439 20 µl 47 kDa Rabbit 
Anti-rabbit IgG, HRP-linked Antibody 7074 100 µl Goat 

Please visit cellsignal.com for individual component applications, species cross-reactivity, dilutions, protocols, and additional product information.

Storage

Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

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).

Like other gasdermin family members, Gasdermin E (also called DFNA5) 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 (8). In addition, cleavage of Gasdermin E can be induced by Granzyme B secreted by NK cells and contributes to tumor suppressive activity (9). Gasdermin E expression is suppressed in several types of cancer, including gastric, colorectal, and breast carcinoma, and may be associated with decreased survival (10-12). In contrast, an increase in Gasdermin E, including the amino-terminal pore-forming fragment, is associated with conditions of excessive inflammation (13-15). Gasdermin A (GSDMA) is preferentially expressed in the epithelium of the skin and gastrointestinal tract and is frequently suppressed in gastric cancer (16-18). Gasdermin B (GSDMB) has been reported to be upregulated in several tumor types, and in breast cancer has been associated with metastasis and poor prognosis (19,20). In addition, Gasdermin B has been associated with immune disorders, including asthma (21,22). Gasdermin B can be cleaved by Granzyme A secreted from cytotoxic lymphocytes leading to pyroptotic cell death (23).

  1. Kayagaki, N. et al. (2015) Nature 526, 666-71.
  2. Shi, J. et al. (2015) Nature 526, 660-5.
  3. Broz, P. and Dixit, V.M. (2016) Nat Rev Immunol 16, 407-20.
  4. Aglietti, R.A. et al. (2016) Proc Natl Acad Sci USA 113, 7858-63.
  5. Ding, J. et al. (2016) Nature 535, 111-6.
  6. Liu, X. et al. (2016) Nature 535, 153-8.
  7. Sborgi, L. et al. (2016) EMBO J 35, 1766-78.
  8. Rogers, C. et al. (2017) Nat Commun 8, 14128.
  9. Zhang, Z. et al. (2020) Nature 579, 415-420.
  10. Kim, M.S. et al. (2008) Oncogene 27, 3624-34.
  11. Kim, M.S. et al. (2008) Biochem Biophys Res Commun 370, 38-43.
  12. Yokomizo, K. et al. (2012) Anticancer Res 32, 1319-22.
  13. Tan, G. et al. (2021) Cell Rep 35, 109265.
  14. Li, Y. et al. (2021) Cell Death Differ 28, 2333-2350.
  15. Shi, H. et al. (2021) Circ Res 129, 383-396.
  16. Tamura, M. et al. (2007) Genomics 89, 618-29.
  17. Saeki, N. et al. (2000) Mamm Genome 11, 718-24.
  18. Saeki, N. et al. (2007) Oncogene 26, 6488-98.
  19. Hergueta-Redondo, M. et al. (2014) PLoS One 9, e90099.
  20. Hergueta-Redondo, M. et al. (2016) Oncotarget 7, 56295-56308.
  21. Yu, J. et al. (2011) Pediatr Pulmonol 46, 701-8.
  22. Das, S. et al. (2016) Proc Natl Acad Sci USA 113, 13132-13137.
  23. Zhou, Z. et al. (2020) Science 368, eaaz7548. doi: 10.1126/science.aaz7548.

Background References

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