R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
Cleaved Gasdermin D (Gly276) (E9U7H) Rabbit mAb #32112
Filter:
- WB
- IP
- F
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 22 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- F-Flow Cytometry
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:100 |
| Flow Cytometry (Fixed/Permeabilized) | 1:1000 - 1:4000 |
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.
Protocol
Specificity / Sensitivity
Cleaved Gasdermin D (Gly276) (E9U7H) Rabbit mAb recognizes endogenous levels of the carboxy-terminal fragment of gasdermin D protein only when cleaved between Asp275 and Gly276.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gly276 of human gasdermin D 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).
- Kayagaki, N. et al. (2015) Nature 526, 666-71.
- 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.
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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