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G7422

Sigma-Aldrich

Anti-GSDMD (126-138) antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

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Synonym(s):
Gasdermin D Antibody, Gasdermin D Antibody - Anti-GSDMD (126-138) antibody produced in rabbit, Gsdmd Antibody, Anti-DF5L, Anti-FKSG10, Anti-GSDMDC1, Anti-Gasdermin domain-containing protein 1
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~55 kDa

species reactivity

human

packaging

antibody small pack of 25 μL

technique(s)

immunoblotting: 1:250-1:500 using human HEK-293T cells over-expressing human recombinant. GSDMDC1.

UniProt accession no.

application(s)

research pathology

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... GSDMD(79792)

Related Categories

General description

Gasdermin D (GSDMD) is also known as DFNA5L or gasdermin domain-containing 1 (GSDMDC1), belongs to the gasdermin protein family of epithelial proliferation regulators. GSDMD is expressed in upper gastrointestinal epithelium differentiating cells.

Immunogen

synthetic peptide corresponding to amino acids 126-138 of human GSDMD

Application

Anti-GSDMD (126-138) antibody produced in rabbit has been used in:
  • immunoblotting
  • CASP4/11 assay
  • cytokine enzyme?linked immunosorbent assay

Anti-GSDMD antibody produced in rabbit is suitable for western blot analysis at a working dilution of 1:500-1:2000.
Yale Center for High Throughput Cell Biology IF-tested antibodies. Each antibody is tested by immunofluorescence against HUVEC cells using the Yale HTCB IF protocol. To learn more about us and Yale Center for High Throughput Cell Biology partnership, visit sigma.com/htcb-if.

Biochem/physiol Actions

GSDMD (gasdermin D) have been suggested to function in the regulation of epithelial apoptosis. GSDMD is expressed in differentiating cells. It may act as a tumor suppressor.
The absence of Gasdermin D (GSDMD), completely blocked LPS electroporation-triggered pyroptosis in studies performed on GSDMD siRNA knockdown or GSDMD knockout (both human HeLa cells and iBMDM mouse cells). It was also reported that caspase-4/11 specifically cleaves GSDMD after Asp275, results in gasdermin-N domain that bears intrinsic pyroptosis inducing activity. Furthermore, GSDMD-mediated pyroptosis participates in mature interleukin 1β (IL-1β) release without distressing its maturation.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Certificates of Analysis (COA)

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Pyroptosis by caspase11/4-gasdermin-D pathway in alcoholic hepatitis in mice and patients
Khanova E, et al.
Hepatology, 67(5), 1737-1753 (2018)
Caspase-8 collaborates with caspase-11 to drive tissue damage and execution of endotoxic shock
Mandal P, et al.
Immunity, 49(1), 42-55 (2018)
Immune-complexed adenovirus induce AIM2-mediated pyroptosis in human dendritic cells
Eichholz K, et al.
PLoS Pathogens, 12(9), e1005871-e1005871 (2016)
Mathias S Dick et al.
Nature communications, 7, 11929-11929 (2016-06-23)
A hallmark of inflammasome activation is the ASC speck, a micrometre-sized structure formed by the inflammasome adaptor protein ASC (apoptosis-associated speck-like protein containing a CARD), which consists of a pyrin domain (PYD) and a caspase recruitment domain (CARD). Here we
Lan H Chu et al.
Nature communications, 9(1), 996-996 (2018-03-10)
Lipopolysaccharide (LPS) of Gram-negative bacteria can elicit a strong immune response. Although extracellular LPS is sensed by TLR4 at the cell surface and triggers a transcriptional response, cytosolic LPS binds and activates non-canonical inflammasome caspases, resulting in pyroptotic cell death

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