The PSBO Antibody (PAC046434) is a polyclonal antibody designed for research involving PSBO, a protein involved in photosystem II in plants. This antibody, raised in rabbits, is highly reactive with plant samples and is validated for use in various applications including immunoprecipitation and immunofluorescence.PSBO is a critical component of photosystem II, which is responsible for the oxygen-evolving process in photosynthesis. Understanding the role of PSBO in photosystem II is essential for studying plant growth, development, and stress responses. The PSBO Antibody enables researchers to detect and analyze PSBO levels in plant samples, providing insights into the mechanisms of photosynthesis and potential targets for enhancing crop productivity and stress tolerance.
This antibody is a valuable tool for plant biologists, biochemists, and researchers studying photosynthesis and plant biology. Its specificity and sensitivity make it ideal for investigating the functions and regulation of PSBO in various plant species, advancing our understanding of photosynthetic processes and their impact on plant productivity and adaptation to environmental changes.
Antibody Name:
PSBO Antibody (PACO46434)
Antibody SKU:
PACO46434
Size:
50ug
Host Species:
Rabbit
Tested Applications:
ELISA
Recommended Dilutions:
Species Reactivity:
Spinacia oleracea
Immunogen:
Recombinant Spinacia oleracea Oxygen-evolving enhancer protein 1, chloroplastic protein (63-232AA)
Stabilizes the manganese cluster which is the primary site of water splitting (By similarity). Binds GTP after preillumination of photosystem II core complex. This binding is inhibited by DCMU.
Synonyms:
Oxygen-evolving enhancer protein 1, chloroplastic (OEE1) (33 kDa subunit of oxygen evolving system of photosystem II) (33 kDa thylakoid membrane protein) (OEC 33 kDa subunit), PSBO
UniProt Protein Function:
Stabilizes the manganese cluster which is the primary site of water splitting (). Binds GTP after preillumination of photosystem II core complex. This binding is inhibited by DCMU.
