The PLY Polyclonal Antibody (PACO34102) is a vital tool for researchers studying the PLY protein, which is involved in immune responses and host-pathogen interactions. This antibody, generated using rabbits, exhibits high reactivity with human samples and has been validated for use in applications such as Western blotting.The PLY protein, also known as pneumolysin, is a pore-forming toxin produced by the bacterium Streptococcus pneumoniae. It plays a crucial role in the pathogenesis of pneumococcal infections, contributing to tissue damage and immune evasion. Understanding the function and regulation of PLY is essential for developing strategies to combat pneumococcal diseases.
By targeting the PLY protein, researchers can investigate its mechanisms of action and potential therapeutic interventions. This antibody enables the detection and analysis of PLY in various experimental settings, making it a valuable resource for studies in microbiology, infectious diseases, and vaccine development. Unlocking the secrets of PLY could lead to new insights and treatments for pneumococcal infections, benefiting global health efforts.
Antibody Name:
ply Antibody (PACO34102)
Antibody SKU:
PACO34102
Size:
50ug
Host Species:
Rabbit
Tested Applications:
ELISA
Recommended Dilutions:
Species Reactivity:
Streptococcus pneumoniae serotype 4
Immunogen:
Recombinant Streptococcus pneumoniae serotype 4 Pneumolysin protein (2-471AA)
Sulfhydryl-activated toxin that causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Cholesterol may be required for binding to host membranes, membrane insertion and pore formation. Can be reversibly inactivated by oxidation (By similarity).
Synonyms:
Pneumolysin (Thiol-activated cytolysin), ply
UniProt Protein Function:
Sulfhydryl-activated toxin that causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Cholesterol may be required for binding to host membranes, membrane insertion and pore formation. Can be reversibly inactivated by oxidation ().
