Anti-GSDMD (Full length+N terminal) Rabbit Polyclonal Antibody for WB, IF/ICC, ELISA - P57764

Core Product Specifications and Parameters

Biological Background: Gasdermin-D Function and Localization

• Gasdermin-D (GSDMD) is a member of the gasdermin family, alternatively named Gasdermin domain-containing protein 1, encoded by the GSDMD gene (also known as DFNA5L, GSDMDC1, FKSG10). It functions primarily as the precursor of a pore-forming protein essential for pyroptosis and host defense against pathogens.
• Upon canonical or non-canonical inflammasome activation, inflammatory caspases (CASP1, CASP4, CASP5) cleave GSDMD, releasing the N-terminal pore-forming fragment from autoinhibition.
  Related references: PMID:26375003 PMID:26375259 PMID:27418190
• The released N‑terminal fragment translocates to the plasma membrane, strongly binding to phosphoinositides (e.g., PI4P, PI(4,5)P2), phosphatidic acid, and phosphatidylserine, but not to uncharged phospholipids, where it oligomerizes into 10–15 nm pores.
  Related references: PMID:27281216 PMID:29898893 PMID:36227980
• These pores mediate the release of mature IL‑1β and IL‑18, cytokines critical for the inflammatory response, and can also discharge mature caspase‑7 and mitochondrial DNA (mtDNA).
  Related references: PMID:27281216 PMID:27418190 PMID:29898893
• In some cell types, pyroptotic cell death ensues via downstream activation of ninjurin‑1 (NINJ1), leading to plasma membrane rupture.
  Related references: PMID:33472215 PMID:37198476
• Beyond its lytic role, GSDMD N‑terminal fragments can kill extracellular Gram‑negative and Gram‑positive bacteria directly, and under cell culture conditions, restrict intracellular pathogens like Listeria monocytogenes.
  Related references: PMID:27281216
• In the small intestine, cleavage by CASP3 or CASP7 produces a transcription coactivator that translocates to the nucleus, partnering with STAT1 to induce CIITA and MHC class II expression, thereby maintaining food tolerance. (By similarity)
• Cleavage by the papain allergen also generates the pore‑forming N‑terminal fragment, which specifically releases mature IL‑33, promoting type 2 immunity.
  Related references: PMID:35794369
• GSDMD is widely expressed, with notable presence in suprabasal esophageal cells and the gastric isthmus/neck, pit, and gland, and localizes to the cytoplasm, inflammasome, plasma membrane, mitochondria, and nucleus under various conditions.

Experimental Guidance and Technical Tips

• For Western blotting, the antibody recognizes an epitope within amino acids 154–252 of the N‑terminal domain; thus, both full‑length GSDMD (predicted ~53 kDa) and the cleaved N‑terminal fragment (~31–34 kDa) may be detected. Validate in the relevant sample system and consider using inflammasome‑activated cell lysates to observe cleavage products.
• In immunofluorescence/immunocytochemistry, GSDMD can localize to the cytoplasm, plasma membrane, and nucleus depending on activation state. Optimization of permeabilization and fixation conditions is recommended. Include appropriate controls to confirm specificity.
• For ELISA, the polyclonal nature allows potential use as both capture and detection antibodies in sandwich ELISA formats. Pairing with a monoclonal antibody specific to a distinct epitope may improve sensitivity. Standard curve using recombinant protein is advised.

CamelBio: Your One-Stop Sourcing Bridge

CamelBio serves as a comprehensive IVD raw‑material partner, supplying validated antibody pairs, optimized monoclonal and polyclonal antibodies, and bulk ancillary reagents to diagnostic manufacturers and research laboratories. In the pyroptosis and innate immunity field, we can source the materials needed for GSDMD‑related assay development, including rare‑target antibodies and recombinant proteins. Our streamlined platform helps bridge the gap from concept to clinic, ensuring a reliable supply chain for your IVD projects.