Cleaved Gasdermin D (Asp275) (E7H9G) Rabbit mAb (BSA and Azide Free) #37349
- WB
- IHC
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 30 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IHC-Immunohistochemistry
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN, or CUT&Tag assays. If you require a carrier-free formulation for chromatin profiling, please contact us. Optimal dilutions/concentrations should be determined by the end user.
Formulation
For standard formulation of this product see product #36425.
Storage
Specificity / Sensitivity
Cleaved Gasdermin D (Asp275) Rabbit mAb (BSA and Azide Free) recognizes endogenous levels of Gasdermin D protein only when cleaved at Asp275.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Asp275 of human Gasdermin D protein.
Background
Gasdermin D (GSDMD), a member of the gasdermin family that includes GSDMA, GSDMB, and GSDMC, 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 U S A 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.
Limited Uses
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