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96458
Gasdermin D Antibody
Primary Antibodies

Gasdermin D Antibody #96458

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# Product Name Application Reactivity
  • WB
H M R

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Supporting Data

REACTIVITY
SENSITIVITY
MW (kDa) 29, 53
SOURCE Rabbit

Application Key:

  • W-Western
  • IP-Immunoprecipitation
  • IHC-Immunohistochemistry
  • ChIP-Chromatin Immunoprecipitation
  • IF-Immunofluorescence
  • F-Flow Cytometry
  • E-P-ELISA-Peptide

Species Cross-Reactivity Key:

  • H-Human
  • M-Mouse
  • R-Rat
  • Hm-Hamster
  • Mk-Monkey
  • Mi-Mink
  • C-Chicken
  • Dm-D. melanogaster
  • X-Xenopus
  • Z-Zebrafish
  • B-Bovine
  • Dg-Dog
  • Pg-Pig
  • Sc-S. cerevisiae
  • Ce-C. elegans
  • Hr-Horse
  • All-All Species Expected

Storage:

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

Specificity / Sensitivity

Gasdermin D Antibody recognizes endogenous levels of total Gasdermin D protein. This antibody detects the N-terminal fragment of Gasdermin D upon proteolytic cleavage.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Arg140 of human Gasdermin D protein. Antibodies are purified by protein A and peptide affinity chromatography.

Background

Gasdermin D (GSDMD), a member of the gasdermin family that includes GSDMA, GSDMB, and GSMDC, 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 GSMDM-N to initiate pyroptosis through the formation of pores on the plasma membrane (4-7).

  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 U S A 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.

Pathways & Proteins

Explore pathways + proteins related to this product.

For Research Use Only. Not For Use In Diagnostic Procedures.

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KARPAS cell line source: Dr. Abraham Karpas at the University of Cambridge.
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