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GSDMB Antibody (Center) Blocking Peptide

Synthetic peptide

     
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Product Information
Primary Accession Q8TAX9
Clone Names 90713071
Additional Information
Gene ID 55876
Other Names Gasdermin-B, Gasdermin-like protein, GSDMB, GSDML
Target/Specificity The synthetic peptide sequence used to generate the antibody AP8559c was selected from the Center region of human GSDMB. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Format Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name GSDMB {ECO:0000303|PubMed:27281216, ECO:0000312|HGNC:HGNC:23690}
Function [Gasdermin-B]: Precursor of a pore-forming protein that acts as a downstream mediator of granzyme-mediated cell death (PubMed:32299851). 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 (PubMed:32299851). Also acts as a regulator of epithelial cell repair independently of programmed cell death: translocates to the plasma membrane and promotes epithelial maintenance and repair by regulating PTK2/FAK-mediated phosphorylation of PDGFA (PubMed:35021065).
Cellular Location [Gasdermin-B]: Cytoplasm. Note=Vesicular localization in the apical region of gastric chief cells and colonic surface mucous cells, and the basal region of neuroendocrine cells
Tissue Location In the gastrointestinal tract, expressed in proliferating cells, including in the basal cell layer of esophagus and in isthmus/neck of stomach.
Research Areas
Citations (0)
citation

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Background

GSDMB is a protein with 3' exonuclease activity. Enzymes with this activity are involved in DNA replication, repair, and recombination. Similarity to an E. coli protein suggests that this enzyme may be a subunit of DNA polymerase III, which does not have intrinsic exonuclease activity.

References

Hur,J.W., et.al., Rheumatol. Int. 28 (8), 783-789 (2008)Chen,M.J., et.al., Nucleic Acids Res. 35 (8), 2682-2694 (2007)

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$ 277.78
Cat# BP8559c
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Availability: 2 weeks
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