Rabbit anti-Human GSDMB Polyclonal Antibody, Biotin conjugated

Uniprot Id

Q8TAX9

Target Species

Human

Target Name

GSDMB

Target Full Name

Gasdermin-B

Target Function

Precursor of a pore-forming protein that acts as a downstream mediator of granzyme-mediated cell death. This form constitutes the precursor of the pore-forming protein: upon cleavage, the released N-terminal moiety (Gasdermin-B, N-terminal) binds to membranes and forms pores, triggering pyroptosis.; Pore-forming protein produced by cleavage by granzyme A (GZMA), which causes membrane permeabilization and pyroptosis in target cells of cytotoxic T and natural killer (NK) cells. Key downstream mediator of granzyme-mediated cell death: (1) granzyme A (GZMA), delivered to target cells from cytotoxic T- and NK-cells, (2) specifically cleaves Gasdermin-B to generate this form. After cleavage, moves to the plasma membrane, homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, triggering pyroptosis. Binds to membrane inner leaflet lipids, such as phosphatidylinositol 4-phosphate, phosphatidylinositol 5-phosphate, bisphosphorylated phosphatidylinositols, such as phosphatidylinositol (4,5)-bisphosphate, and more weakly to phosphatidic acid. Also binds sufatide, a component of the apical membrane of epithelial cells.

Target Subcellular Location

[Gasdermin-B]: Cytoplasm.; [Gasdermin-B, N-terminal]: Cell membrane; Multi-pass membrane protein.

Target Protein Families

Gasdermin family

Target Tissue Specificity

In the gastrointestinal tract, expressed in proliferating cells, including in the basal cell layer of esophagus and in isthmus/neck of stomach.

Target Research Area

Cell Biology

Target Synonyms

123; 156; Gasdermin B; Gasdermin like protein; Gasdermin-B; Gasdermin-like protein; GSDMB; GSDMB_HUMAN; GSDML; PP4052; PRO2521

Target Background

This gene encodes a member of the gasdermin-domain containing protein family. Other gasdermin-family genes are implicated in the regulation of apoptosis in epithelial cells, and are linked to cancer. Alternative splicing and the use of alternative promoters results in multiple transcript variants. Additional variants have been described, but they are candidates for nonsense-mediated mRNA decay (NMD) and are unlikely to be protein-coding.